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Entry
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- *153619 - LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 3; LGALS3
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- OMIM
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</li>
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</ul>
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</div>
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</nav>
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</div>
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<div id="mimSearch" class="hidden-print">
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<div class="container">
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<form method="get" action="/search" id="mimEntrySearchForm" name="entrySearchForm" class="form-horizontal">
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<input type="hidden" id="mimSearchIndex" name="index" value="entry" />
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<input type="hidden" id="mimSearchStart" name="start" value="1" />
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<input type="hidden" id="mimSearchLimit" name="limit" value="10" />
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<input type="hidden" id="mimSearchSort" name="sort" value="score desc, prefix_sort desc" />
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<div class="row">
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<div class="col-lg-8 col-md-8 col-sm-8 col-xs-8">
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<div class="form-group">
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<div class="input-group">
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<input type="search" id="mimEntrySearch" name="search" class="form-control" value="" placeholder="Search OMIM..." maxlength="5000" autocomplete="off" autocorrect="off" autocapitalize="none" spellcheck="false" autofocus />
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<div class="input-group-btn">
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<button type="submit" id="mimEntrySearchSubmit" class="btn btn-default" style="width: 5em;"><span class="glyphicon glyphicon-search"></span></button>
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<button type="button" class="btn btn-default dropdown-toggle" data-toggle="dropdown"> Options <span class="caret"></span></button>
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<ul class="dropdown-menu dropdown-menu-right">
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<li class="dropdown-header">
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Advanced Search
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</li>
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<li style="margin-left: 0.5em;">
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<a href="/search/advanced/entry"> OMIM </a>
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</li>
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<li style="margin-left: 0.5em;">
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<a href="/search/advanced/clinicalSynopsis"> Clinical Synopses </a>
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</li>
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<li style="margin-left: 0.5em;">
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<a href="/search/advanced/geneMap"> Gene Map </a>
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</li>
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<li role="separator" class="divider"></li>
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<li>
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<a href="/history"> Search History </a>
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</li>
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</ul>
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</div>
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</div>
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<div class="autocomplete" id="mimEntrySearchAutocomplete"></div>
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</div>
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<div class="col-lg-4 col-md-4 col-sm-4 col-xs-4">
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<span class="small">
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</div>
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</form>
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<div class="row">
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<p />
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</div>
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</div>
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<!-- <div id="mimSearch"> -->
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<div id="mimContent">
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<div class="container hidden-print">
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<div class="col-lg-12 col-md-12 col-sm-12 col-xs-12">
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<div id="mimAlertBanner">
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</div>
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</div>
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</div>
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<div class="row">
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<div class="col-lg-2 col-md-2 col-sm-2 hidden-sm hidden-xs">
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<div id="mimFloatingTocMenu" class="small" role="navigation">
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<p>
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<span class="h4">*153619</span>
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<br />
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<strong>Table of Contents</strong>
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</p>
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<nav>
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<ul id="mimFloatingTocMenuItems" class="nav nav-pills nav-stacked mim-floating-toc-padding">
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<li role="presentation">
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<a href="#title"><strong>Title</strong></a>
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</li>
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<li role="presentation">
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<a href="#text"><strong>Text</strong></a>
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</li>
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<li role="presentation" style="margin-left: 1em">
|
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<a href="#cloning">Cloning and Expression</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
|
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<a href="#geneFunction">Gene Function</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="#geneStructure">Gene Structure</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="#mapping">Mapping</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="#animalModel">Animal Model</a>
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</li>
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<li role="presentation">
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<a href="#references"><strong>References</strong></a>
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</li>
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<li role="presentation">
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<a href="#contributors"><strong>Contributors</strong></a>
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</li>
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<li role="presentation">
|
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<a href="#creationDate"><strong>Creation Date</strong></a>
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</li>
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<li role="presentation">
|
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<a href="#editHistory"><strong>Edit History</strong></a>
|
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</li>
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</ul>
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</nav>
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</div>
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</div>
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<div class="col-lg-2 col-lg-push-8 col-md-2 col-md-push-8 col-sm-2 col-sm-push-8 col-xs-12">
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<div id="mimFloatingLinksMenu">
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<div class="panel panel-primary" style="margin-bottom: 0px; border-radius: 4px 4px 0px 0px">
|
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<div class="panel-heading mim-panel-heading" role="tab" id="mimExternalLinks">
|
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<h4 class="panel-title">
|
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<a href="#mimExternalLinksFold" id="mimExternalLinksToggle" class="mimTriangleToggle" role="button" data-toggle="collapse">
|
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<div style="display: table-row">
|
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<div id="mimExternalLinksToggleTriangle" class="small" style="color: white; display: table-cell;">▼</div>
|
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<div style="display: table-cell;">External Links</div>
|
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</div>
|
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</a>
|
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</h4>
|
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</div>
|
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</div>
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<div id="mimExternalLinksFold" class="collapse in">
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<div class="panel-group" id="mimExternalLinksAccordion" role="tablist" aria-multiselectable="true">
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
|
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<div class="panel-heading mim-panel-heading" role="tab" id="mimGenome">
|
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<span class="panel-title">
|
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<span class="small">
|
|
<a href="#mimGenomeLinksFold" id="mimGenomeLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
|
<span id="mimGenomeLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Genome
|
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</a>
|
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</span>
|
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</span>
|
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</div>
|
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<div id="mimGenomeLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="genome">
|
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<div class="panel-body small mim-panel-body">
|
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|
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<div><a href="https://www.ensembl.org/Homo_sapiens/Location/View?db=core;g=ENSG00000131981;t=ENST00000254301" class="mim-tip-hint" title="Genome databases for vertebrates and other eukaryotic species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
|
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|
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<div><a href="https://www.ncbi.nlm.nih.gov/genome/gdv/browser/gene/?id=3958" class="mim-tip-hint" title="Detailed views of the complete genomes of selected organisms from vertebrates to protozoa." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Genome Viewer', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Genome Viewer</a></div>
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|
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=153619" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
|
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</div>
|
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</div>
|
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</div>
|
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
|
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<div class="panel-heading mim-panel-heading" role="tab" id="mimDna">
|
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<span class="panel-title">
|
|
<span class="small">
|
|
<a href="#mimDnaLinksFold" id="mimDnaLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
|
<span id="mimDnaLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> DNA
|
|
</a>
|
|
</span>
|
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</span>
|
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</div>
|
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<div id="mimDnaLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
|
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<div class="panel-body small mim-panel-body">
|
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<div><a href="https://www.ensembl.org/Homo_sapiens/Transcript/Sequence_cDNA?db=core;g=ENSG00000131981;t=ENST00000254301" class="mim-tip-hint" title="Transcript-based views for coding and noncoding DNA." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl (MANE Select)</a></div>
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|
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_001357678,NM_002306,NR_003225" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_002306" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq (MANE)', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq (MANE Select)</a></div>
|
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=153619" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
|
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</div>
|
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</div>
|
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</div>
|
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
|
|
<div class="panel-heading mim-panel-heading" role="tab" id="mimProtein">
|
|
<span class="panel-title">
|
|
<span class="small">
|
|
<a href="#mimProteinLinksFold" id="mimProteinLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
|
<span id="mimProteinLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Protein
|
|
</a>
|
|
</span>
|
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</span>
|
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</div>
|
|
<div id="mimProteinLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
|
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<div class="panel-body small mim-panel-body">
|
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<div><a href="https://hprd.org/summary?hprd_id=01090&isoform_id=01090_1&isoform_name=Isoform_1" class="mim-tip-hint" title="The Human Protein Reference Database; manually extracted and visually depicted information on human proteins." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HPRD', 'domain': 'hprd.org'})">HPRD</a></div>
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<div><a href="https://www.proteinatlas.org/search/LGALS3" class="mim-tip-hint" title="The Human Protein Atlas contains information for a large majority of all human protein-coding genes regarding the expression and localization of the corresponding proteins based on both RNA and protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HumanProteinAtlas', 'domain': 'proteinatlas.org'})">Human Protein Atlas</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/protein/179531,186922,299602,1196442,2385452,12005990,12005991,12654571,23342432,23342434,27348224,28071074,31657226,34365022,45786143,48145911,49457147,62088362,115430223,119601064,119601066,119601067,189067453,215274262,308219158,311461928,1274095930" class="mim-tip-hint" title="NCBI protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Protein', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Protein</a></div>
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<div><a href="https://www.uniprot.org/uniprotkb/P17931" class="mim-tip-hint" title="Comprehensive protein sequence and functional information, including supporting data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UniProt', 'domain': 'uniprot.org'})">UniProt</a></div>
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</div>
|
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</div>
|
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</div>
|
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
|
|
<div class="panel-heading mim-panel-heading" role="tab" id="mimGeneInfo">
|
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<span class="panel-title">
|
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<span class="small">
|
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<a href="#mimGeneInfoLinksFold" id="mimGeneInfoLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
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<div style="display: table-row">
|
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<div id="mimGeneInfoLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
|
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<div style="display: table-cell;">Gene Info</div>
|
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</div>
|
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</a>
|
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</span>
|
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</span>
|
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</div>
|
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<div id="mimGeneInfoLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
|
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<div class="panel-body small mim-panel-body">
|
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<div><a href="http://biogps.org/#goto=genereport&id=3958" class="mim-tip-hint" title="The Gene Portal Hub; customizable portal of gene and protein function information." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'BioGPS', 'domain': 'biogps.org'})">BioGPS</a></div>
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<div><a href="https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000131981;t=ENST00000254301" class="mim-tip-hint" title="Orthologs, paralogs, regulatory regions, and splice variants." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
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<div><a href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=LGALS3" class="mim-tip-hint" title="The Human Genome Compendium; web-based cards integrating automatically mined information on human genes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneCards', 'domain': 'genecards.org'})">GeneCards</a></div>
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<div><a href="http://amigo.geneontology.org/amigo/search/annotation?q=LGALS3" class="mim-tip-hint" title="Terms, defined using controlled vocabulary, representing gene product properties (biologic process, cellular component, molecular function) across species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneOntology', 'domain': 'amigo.geneontology.org'})">Gene Ontology</a></div>
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<div><a href="https://www.genome.jp/dbget-bin/www_bget?hsa+3958" class="mim-tip-hint" title="Kyoto Encyclopedia of Genes and Genomes; diagrams of signaling pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'KEGG', 'domain': 'genome.jp'})">KEGG</a></div>
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<dd><a href="http://v1.marrvel.org/search/gene/LGALS3" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></dd>
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<dd><a href="https://monarchinitiative.org/NCBIGene:3958" class="mim-tip-hint" title="Monarch Initiative." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Monarch', 'domain': 'monarchinitiative.org'})">Monarch</a></dd>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/3958" class="mim-tip-hint" title="Gene-specific map, sequence, expression, structure, function, citation, and homology data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Gene', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Gene</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_chrom=chr14&hgg_gene=ENST00000254301.14&hgg_start=55129252&hgg_end=55145430&hgg_type=knownGene" class="mim-tip-hint" title="UCSC Genome Bioinformatics; gene-specific structure and function information with links to other databases." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC', 'domain': 'genome.ucsc.edu'})">UCSC</a></div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimClinicalResources">
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<span class="panel-title">
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<span class="small">
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<a href="#mimClinicalResourcesLinksFold" id="mimClinicalResourcesLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimClinicalResourcesLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Clinical Resources</div>
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</a>
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<div id="mimClinicalResourcesLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="clinicalResources">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ncbi.nlm.nih.gov/gtr/all/tests/?term=153619[mim]" class="mim-tip-hint" title="Genetic Testing Registry." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GTR', 'domain': 'ncbi.nlm.nih.gov'})">GTR</a></div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimVariation">
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<span class="small">
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<a href="#mimVariationLinksFold" id="mimVariationLinksToggle" class=" mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimVariationLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">▼</span> Variation
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</a>
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<div id="mimVariationLinksFold" class="panel-collapse collapse in mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ncbi.nlm.nih.gov/clinvar?term=153619[MIM]" class="mim-tip-hint" title="ClinVar aggregates information about sequence variation and its relationship to human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">ClinVar</a></div>
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<div><a href="https://www.deciphergenomics.org/gene/LGALS3/overview/clinical-info" class="mim-tip-hint" title="DECIPHER" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'DECIPHER', 'domain': 'DECIPHER'})">DECIPHER</a></div>
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<div><a href="https://gnomad.broadinstitute.org/gene/ENSG00000131981" class="mim-tip-hint" title="The Genome Aggregation Database (gnomAD), Broad Institute." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'gnomAD', 'domain': 'gnomad.broadinstitute.org'})">gnomAD</a></div>
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<div><a href="https://www.ebi.ac.uk/gwas/search?query=LGALS3" class="mim-tip-hint" title="GWAS Catalog; NHGRI-EBI Catalog of published genome-wide association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Catalog', 'domain': 'gwascatalog.org'})">GWAS Catalog </a></div>
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<div><a href="https://www.gwascentral.org/search?q=LGALS3" class="mim-tip-hint" title="GWAS Central; summary level genotype-to-phenotype information from genetic association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Central', 'domain': 'gwascentral.org'})">GWAS Central </a></div>
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<div><a href="https://evs.gs.washington.edu/EVS/PopStatsServlet?searchBy=Gene+Hugo&target=LGALS3&upstreamSize=0&downstreamSize=0&x=0&y=0" class="mim-tip-hint" title="National Heart, Lung, and Blood Institute Exome Variant Server." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NHLBI EVS', 'domain': 'evs.gs.washington.edu'})">NHLBI EVS</a></div>
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<div><a href="https://www.pharmgkb.org/gene/PA30340" class="mim-tip-hint" title="Pharmacogenomics Knowledge Base; curated and annotated information regarding the effects of human genetic variations on drug response." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PharmGKB', 'domain': 'pharmgkb.org'})">PharmGKB</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimAnimalModels">
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<span class="panel-title">
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<span class="small">
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<a href="#mimAnimalModelsLinksFold" id="mimAnimalModelsLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimAnimalModelsLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Animal Models</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimAnimalModelsLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.alliancegenome.org/gene/HGNC:6563" class="mim-tip-hint" title="Search Across Species; explore model organism and human comparative genomics." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Alliance Genome', 'domain': 'alliancegenome.org'})">Alliance Genome</a></div>
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<div><a href="https://flybase.org/reports/FBgn0031289.html" class="mim-tip-hint" title="A Database of Drosophila Genes and Genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'FlyBase', 'domain': 'flybase.org'})">FlyBase</a></div>
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<div><a href="https://www.mousephenotype.org/data/genes/MGI:96778" class="mim-tip-hint" title="International Mouse Phenotyping Consortium." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'IMPC', 'domain': 'knockoutmouse.org'})">IMPC</a></div>
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<div><a href="http://v1.marrvel.org/search/gene/LGALS3#HomologGenesPanel" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></div>
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<div><a href="http://www.informatics.jax.org/marker/MGI:96778" class="mim-tip-hint" title="Mouse Genome Informatics; international database resource for the laboratory mouse, including integrated genetic, genomic, and biological data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MGI Mouse Gene', 'domain': 'informatics.jax.org'})">MGI Mouse Gene</a></div>
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<div><a href="https://www.mmrrc.org/catalog/StrainCatalogSearchForm.php?search_query=" class="mim-tip-hint" title="Mutant Mouse Resource & Research Centers." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MMRRC', 'domain': 'mmrrc.org'})">MMRRC</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/3958/ortholog/" class="mim-tip-hint" title="Orthologous genes at NCBI." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Orthologs', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Orthologs</a></div>
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<div><a href="https://www.orthodb.org/?ncbi=3958" class="mim-tip-hint" title="Hierarchical catalogue of orthologs." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'OrthoDB', 'domain': 'orthodb.org'})">OrthoDB</a></div>
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<div><a href="mim#WormbaseGeneFold" id="mimWormbaseGeneToggle" data-toggle="collapse" class="mim-tip-hint mimTriangleToggle" title="Database of the biology and genome of Caenorhabditis elegans and related nematodes."><span id="mimWormbaseGeneToggleTriangle" class="small" style="margin-left: -0.8em;">►</span>Wormbase Gene</div>
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<div id="mimWormbaseGeneFold" class="collapse">
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<div style="margin-left: 0.5em;"><a href="https://wormbase.org/db/gene/gene?name=WBGene00002270;class=Gene" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Wormbase Gene', 'domain': 'wormbase.org'})">WBGene00002270 </a></div><div style="margin-left: 0.5em;"><a href="https://wormbase.org/db/gene/gene?name=WBGene00002271;class=Gene" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Wormbase Gene', 'domain': 'wormbase.org'})">WBGene00002271 </a></div>
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</div>
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<div><a href="https://zfin.org/ZDB-GENE-030131-4324" class="mim-tip-hint" title="The Zebrafish Model Organism Database." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ZFin', 'domain': 'zfin.org'})">ZFin</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimCellularPathways">
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<span class="panel-title">
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<span class="small">
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<a href="#mimCellularPathwaysLinksFold" id="mimCellularPathwaysLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimCellularPathwaysLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Cellular Pathways</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimCellularPathwaysLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://reactome.org/content/query?q=LGALS3&species=Homo+sapiens&types=Reaction&types=Pathway&cluster=true" class="definition" title="Protein-specific information in the context of relevant cellular pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {{'name': 'Reactome', 'domain': 'reactome.org'}})">Reactome</a></div>
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</div>
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</div>
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</div>
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<span>
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<span class="mim-tip-bottom" qtip_title="<strong>Looking for this gene or this phenotype in other resources?</strong>" qtip_text="Select a related resource from the dropdown menu and click for a targeted link to information directly relevant.">
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</span>
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<div class="col-lg-8 col-lg-pull-2 col-md-8 col-md-pull-2 col-sm-8 col-sm-pull-2 col-xs-12">
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<div>
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<a id="title" class="mim-anchor"></a>
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<div>
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<a id="number" class="mim-anchor"></a>
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<div class="text-right">
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<div>
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<span class="h3">
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<span class="mim-font mim-tip-hint" title="Gene description">
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<span class="text-danger"><strong>*</strong></span>
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153619
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</span>
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</span>
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</div>
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</div>
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<div>
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<a id="preferredTitle" class="mim-anchor"></a>
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<h3>
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<span class="mim-font">
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LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 3; LGALS3
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</span>
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</h3>
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</div>
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<div>
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<br />
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</div>
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<div>
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<a id="alternativeTitles" class="mim-anchor"></a>
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<div>
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<p>
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<span class="mim-font">
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<em>Alternative titles; symbols</em>
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</span>
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</p>
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</div>
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<div>
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<h4>
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<span class="mim-font">
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MACROPHAGE GALACTOSE-SPECIFIC LECTIN; MAC2<br />
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GALACTOSIDE-BINDING PROTEIN; GALBP<br />
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GALECTIN 3; GAL3
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</span>
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</h4>
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</div>
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</div>
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<div>
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<br />
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</div>
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<div>
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<a id="includedTitles" class="mim-anchor"></a>
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<div>
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<p>
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<span class="mim-font">
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Other entities represented in this entry:
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</span>
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</p>
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</div>
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<div>
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<span class="h3 mim-font">
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GALECTIN 3 INTERNAL GENE, INCLUDED; GALIG, INCLUDED
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</span>
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</div>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<a id="approvedGeneSymbols" class="mim-anchor"></a>
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<p>
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<span class="mim-text-font">
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<strong><em>HGNC Approved Gene Symbol: <a href="https://www.genenames.org/tools/search/#!/genes?query=LGALS3" class="mim-tip-hint" title="HUGO Gene Nomenclature Committee." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HGNC', 'domain': 'genenames.org'})">LGALS3</a></em></strong>
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</span>
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</p>
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</div>
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<div>
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<a id="cytogeneticLocation" class="mim-anchor"></a>
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<p>
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<span class="mim-text-font">
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<strong>
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<em>
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Cytogenetic location: <a href="/geneMap/14/256?start=-3&limit=10&highlight=256">14q22.3</a>
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Genomic coordinates <span class="small">(GRCh38)</span> : <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&position=chr14:55129252-55145430&dgv=pack&knownGene=pack&omimGene=pack" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">14:55,129,252-55,145,430</a> </span>
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</em>
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</strong>
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<a href="https://www.ncbi.nlm.nih.gov/" target="_blank" class="small"> (from NCBI) </a>
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</span>
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</p>
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</div>
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<div>
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</div>
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<div>
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<br />
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</div>
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<div>
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<a id="text" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<span class="mim-tip-floating" qtip_title="<strong>Looking For More References?</strong>" qtip_text="Click the 'reference plus' icon <span class='glyphicon glyphicon-plus-sign'></span> at the end of each OMIM text paragraph to see more references related to the content of the preceding paragraph.">
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<strong>TEXT</strong>
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</span>
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</span>
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</h4>
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<div>
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<a id="cloning" class="mim-anchor"></a>
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<h4 href="#mimCloningFold" id="mimCloningToggle" class="mimTriangleToggle" style="cursor: pointer;" data-toggle="collapse">
|
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<span id="mimCloningToggleTriangle" class="small mimTextToggleTriangle">▼</span>
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<p>The murine Mac2 protein is a galactose- and IgE-binding lectin secreted by inflammatory macrophages. <a href="#4" class="mim-tip-reference" title="Cherayil, B. J., Chaitovitz, S., Wong, C., Pillai, S. <strong>Molecular cloning of a human macrophage lectin specific for galactose.</strong> Proc. Nat. Acad. Sci. 87: 7324-7328, 1990.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2402511/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2402511</a>] [<a href="https://doi.org/10.1073/pnas.87.18.7324" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2402511">Cherayil et al. (1990)</a> cloned and characterized a cDNA representing the human homolog. The amino acid sequence derived therefrom indicated that the protein is evolutionarily highly conserved, especially in the C-terminal lectin domain. Human MAC2 synthesized in vitro is recognized by a monoclonal antibody to mouse Mac2 and behaves like a galactose-specific lectin in its binding to the desialylated glycoprotein asialofetuin. It also binds to purified laminin (see <a href="/entry/150320">150320</a>), indicating a potential role in macrophage extracellular matrix interactions. MAC2 is also known as galectin-3 (LGALS3), as mentioned in <a href="#9" class="mim-tip-reference" title="Madsen, P., Rasmussen, H. H., Flint, T., Gromov, P., Kruse, T. A., Honore, B., Vorum, H., Celis, J. E. <strong>Cloning, expression, and chromosome mapping of human galectin-7.</strong> J. Biol. Chem. 270: 5823-5829, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7534301/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7534301</a>] [<a href="https://doi.org/10.1074/jbc.270.11.5823" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7534301">Madsen et al. (1995)</a>. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2402511+7534301" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>From a human fibrosarcoma cDNA library, <a href="#19" class="mim-tip-reference" title="Raz, A., Carmi, P., Raz, T., Hogan, V., Mohamed, A., Wolman, S. R. <strong>Molecular cloning and chromosomal mapping of a human galactoside-binding protein.</strong> Cancer Res. 51: 2173-2178, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2009535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2009535</a>]" pmid="2009535">Raz et al. (1991)</a> cloned a galactoside-binding protein with a molecular weight of 31,000. The deduced 242-amino acid protein has the characteristics of a carbohydrate-binding protein. The deduced amino acid sequence contains 95 residues at the N terminus that are homologous to the predicted amino acid sequence of the second exon of the oncogene LMYC (<a href="/entry/164850">164850</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2009535" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#8" class="mim-tip-reference" title="Huflejt, M. E., Jordan, E. T., Gitt, M. A., Barondes, S. H., Leffler, H. <strong>Strikingly different localization of galectin-3 and galectin-4 in human colon adenocarcinoma T84 cells: galectin-4 is localized at sites of cell adhesion.</strong> J. Biol. Chem. 272: 14294-14303, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9162064/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9162064</a>] [<a href="https://doi.org/10.1074/jbc.272.22.14294" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9162064">Huflejt et al. (1997)</a> found that LGALS3 and LGALS4 (<a href="/entry/602518">602518</a>) have very different cellular localizations in human colon adenocarcinoma T84 cells, suggesting that these LGALSs have different targeting mechanisms, ligands, and functions. In confluent T84 cells, LGALS3 is concentrated mainly at the apical membrane in large granular inclusions. In subconfluent T84 cells, it is distributed along most of the cell periphery and is concentrated in the posterior part of lamellipodia. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9162064" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>By RT-PCR of a human osteosarcoma cell line, <a href="#16" class="mim-tip-reference" title="Raimond, J., Rouleux, F., Monsigny, M., Legrand, A. <strong>The second intron of the human galectin-3 gene has a strong promoter activity down-regulated by p53.</strong> FEBS Lett. 363: 165-169, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7729540/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7729540</a>] [<a href="https://doi.org/10.1016/0014-5793(95)00310-6" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7729540">Raimond et al. (1995)</a> identified galectin-3 transcripts initiated from the promoter upstream of exon 1 and from the internal promoter within intron 2. Using RT-PCR and EST database analysis, <a href="#5" class="mim-tip-reference" title="Guittaut, M., Charpentier, S., Normand, T., Dubois, M., Raimond, J., Legrand, A. <strong>Identification of an internal gene to the human galectin-3 gene with two different overlapping reading frames that do not encode galectin-3.</strong> J. Biol. Chem. 276: 2652-2657, 2001.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11160123/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11160123</a>] [<a href="https://doi.org/10.1074/jbc.m002523200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11160123">Guittaut et al. (2001)</a> obtained transcripts originating from the internal promoter in intron 2 of LGALS3 from several cDNA libraries. They concluded that these transcripts arise from a gene embedded within LGALS3 that they called 'galectin-3 internal gene,' or GALIG. The GALIG transcripts contain 2 overlapping ORFs, ORF1 and ORF2, that initiate in exon 3 of LGALS3 and are out-of-frame relative to the LGALS3 coding sequence. RT-PCR detected variable and tissue-specific expression of LGALS3 and GALIG transcripts. GALIG transcripts showed highest expression in peripheral blood leukocytes, but overall they were much less abundant than LGALS3 transcripts. In transfected osteosarcoma cells, fluorescence-tagged ORF1 localized to cytosol and nucleus, and fluorescence-tagged ORF2 localized to mitochondria. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=7729540+11160123" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>Galectin-3 is expressed in various tissues and organs, but is significantly absent in normal hepatocytes. However, evaluation of patient liver biopsies for galectin-3 expression revealed that hepatocellular carcinoma (HCC) frequently expressed significant levels of this lectin; 76% were immunohistochemically positive. Further investigations showed that galectin-3 expression in HCC is independent of whether the patient had prior hepatitis B virus infection (<a href="#7" class="mim-tip-reference" title="Hsu, D. K., Dowling, C. A., Jeng, K.-C. G., Chen, J.-T., Yang, R.-Y., Liu, F.-T. <strong>Galectin-3 expression is induced in cirrhotic liver and hepatocellular carcinoma.</strong> Int. J. Cancer 81: 519-526, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10225438/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10225438</a>] [<a href="https://doi.org/10.1002/(sici)1097-0215(19990517)81:4<519::aid-ijc3>3.0.co;2-0" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10225438">Hsu et al., 1999</a>). <a href="#7" class="mim-tip-reference" title="Hsu, D. K., Dowling, C. A., Jeng, K.-C. G., Chen, J.-T., Yang, R.-Y., Liu, F.-T. <strong>Galectin-3 expression is induced in cirrhotic liver and hepatocellular carcinoma.</strong> Int. J. Cancer 81: 519-526, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10225438/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10225438</a>] [<a href="https://doi.org/10.1002/(sici)1097-0215(19990517)81:4<519::aid-ijc3>3.0.co;2-0" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10225438">Hsu et al. (1999)</a> suggested that deregulated expression of galectin-3 can result in tumor transformation and invasiveness, or confer propensity for tumor cell survival. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10225438" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Using reporter gene assays, <a href="#16" class="mim-tip-reference" title="Raimond, J., Rouleux, F., Monsigny, M., Legrand, A. <strong>The second intron of the human galectin-3 gene has a strong promoter activity down-regulated by p53.</strong> FEBS Lett. 363: 165-169, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7729540/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7729540</a>] [<a href="https://doi.org/10.1016/0014-5793(95)00310-6" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7729540">Raimond et al. (1995)</a> showed that p53 (TP53; <a href="/entry/191170">191170</a>) downregulated expression of the GALIG promoter when cotransfected into a human osteosarcoma cell line. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7729540" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In the thyroid, expression of galectin-3 protein had been described in differentiated follicular cancer, suggesting that the immunohistochemical study of galectin-3 may be a potential marker of malignancy in thyroid neoplasms. <a href="#11" class="mim-tip-reference" title="Martins, L., Matsuo, S. E., Ebina, K. N., Kulcsar, M. A. V., Friguglietti, C. U. M., Kimura, E. T. <strong>Galectin-3 messenger ribonucleic acid and protein are expressed in benign thyroid tumors.</strong> J. Clin. Endocr. Metab. 87: 4806-4810, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12364477/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12364477</a>] [<a href="https://doi.org/10.1210/jc.2002-020094" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12364477">Martins et al. (2002)</a> analyzed galectin-3 protein and mRNA expression in thyroid tissues from 87 patients with histomorphologic diagnosis of multinodular goiter (MNG), follicular adenoma, follicular carcinoma, papillary carcinoma, and 5 normal tissues. Galectin-3 mRNA expression was detected by RT-PCR. Their results showed that the majority of carcinomas expressed galectin-3 protein (follicular, 90%; papillary, 100%). However, in contrast to the previously published data, benign lesions also expressed galectin-3 (adenoma, 45%; MNG, 17%). The authors showed by RT-PCR that thyroid tissues with diagnosis of adenoma and MNG expressed galectin-3 mRNA. Although the galectin-3 immunostaining demonstrated a sensitivity of 93.8% in the identification of cancer, the accuracy in the distinction between benign and malignant tissues was 77.0%. This accuracy was even lower (68.6%) when galectin-3 expression in follicular adenoma was compared with follicular carcinoma. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12364477" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Using micro-Boyden chamber analysis, <a href="#21" class="mim-tip-reference" title="Sano, H., Hsu, D. K., Yu, L., Apgar, J. R., Kuwabara, I., Yamanaka, T., Hirashima, M., Liu, F.-T. <strong>Human galectin-3 is a novel chemoattractant for monocytes and macrophages.</strong> J. Immun. 165: 2156-2164, 2000.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10925302/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10925302</a>] [<a href="https://doi.org/10.4049/jimmunol.165.4.2156" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10925302">Sano et al. (2000)</a> determined that LGALS3 has chemoattractant activity not for eosinophils, like LGALS9 (<a href="/entry/601879">601879</a>), but for monocytes and mature macrophages. At high concentrations LGALS3 activity is chemotactic, i.e., cells migrate towards the attractant, whereas at low concentrations it is chemokinetic, i.e., it enhances movement of cells in all directions. <a href="#21" class="mim-tip-reference" title="Sano, H., Hsu, D. K., Yu, L., Apgar, J. R., Kuwabara, I., Yamanaka, T., Hirashima, M., Liu, F.-T. <strong>Human galectin-3 is a novel chemoattractant for monocytes and macrophages.</strong> J. Immun. 165: 2156-2164, 2000.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10925302/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10925302</a>] [<a href="https://doi.org/10.4049/jimmunol.165.4.2156" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10925302">Sano et al. (2000)</a> found that the chemoattractant activity is inhibited by lactose, indicating that the C-terminal lectin domain of LGALS3 is required. A C-terminal domain fragment was unable to mediate chemoattraction, suggesting that the N-terminal domain is also necessary for activity. Both migration and increased intracellular calcium concentration were pertussis toxin sensitive and therefore probably mediated by a G protein-coupled receptor. The authors determined that LGALS3 does not, however, use the chemokine receptors CCR1 (<a href="/entry/601159">601159</a>), CCR2 (<a href="/entry/601267">601267</a>), CCR5 (<a href="/entry/601373">601373</a>), and CXCR4 (<a href="/entry/162643">162643</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10925302" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#23" class="mim-tip-reference" title="Yoshimura, A., Gemma, A., Hosoya, Y., Komaki, E., Hosomi, Y., Okano, T., Takenaka, K., Matuda, K., Seike, M., Uematsu, K., Hibino, S., Shibuya, M., Yamada, T., Hirohashi, S., Kudoh, S. <strong>Increased expression of the LGALS3 (galectin 3) gene in human non-small-cell lung cancer.</strong> Genes Chromosomes Cancer 37: 159-164, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12696064/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12696064</a>] [<a href="https://doi.org/10.1002/gcc.10205" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12696064">Yoshimura et al. (2003)</a> found increased expression of the LGALS3 gene in human nonsmall cell lung cancer, and suggested that it may play a role in the process of metastasis in this malignancy but not in small cell lung cancer. They considered that LGALS3 may be a phenotypic marker that excludes small cell lung cancer and a novel target molecule in therapy of nonsmall cell lung cancer. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12696064" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#13" class="mim-tip-reference" title="Nikiforova, M. N., Lynch, R. A., Biddinger, P. W., Alexander, E. K., Dorn, G. W., II, Tallini, G., Kroll, T. G., Nikiforov, Y. E. <strong>RAS point mutations and PAX8-PPAR-gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma.</strong> J. Clin. Endocr. Metab. 88: 2318-2326, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12727991/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12727991</a>] [<a href="https://doi.org/10.1210/jc.2002-021907" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12727991">Nikiforova et al. (2003)</a> analyzed a series of 88 conventional follicular and Hurthle cell thyroid tumors for RAS (HRAS, <a href="/entry/190020">190020</a>; NRAS, <a href="/entry/164790">164790</a>; KRAS, <a href="/entry/190070">190070</a>) mutations and PAX8 (<a href="/entry/167415">167415</a>)-PPARG (<a href="/entry/601487">601487</a>) rearrangements using molecular methods and for galectin-3 and mesothelioma antibody HBME-1 expression by immunohistochemistry. Forty-nine percent of conventional follicular carcinomas had RAS mutations, 36% had PAX8-PPARG rearrangement, and only 1 (3%) had both. Of follicular adenomas, 48% had RAS mutations, 4% had PAX8-PPARG rearrangement, and 48% had neither. Follicular carcinomas with RAS mutations most often displayed an HBME-1-positive/galectin-3-negative immunophenotype and were either minimally or overtly invasive. Hurthle cell tumors infrequently had PAX8-PPARG rearrangement or RAS mutations. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12727991" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#14" class="mim-tip-reference" title="Ohshima, S., Kuchen, S., Seemayer, C. A., Kyburz, D., Hirt, A., Klinzing, S., Michel, B. A., Gay, R. E., Liu, F.-T., Gay, S., Neidhart, M. <strong>Galectin 3 and its binding protein in rheumatoid arthritis.</strong> Arthritis Rheum. 48: 2788-2795, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/14558084/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">14558084</a>] [<a href="https://doi.org/10.1002/art.11287" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="14558084">Ohshima et al. (2003)</a> found that galectin-3 mRNA and protein are expressed throughout synovial tissue in rheumatoid arthritis (RA; <a href="/entry/180300">180300</a>) and that both galectin-3 and its binding protein are found at sites of joint destruction. In addition, levels of galectin-3 in serum and synovial fluid as well as levels of its binding protein in synovial fluid were significantly elevated in RA compared to osteoarthritis and healthy controls (p less than 0.001). Serum galectin-3 levels correlated significantly with C-reactive protein levels (p less than 0.001), and levels of its binding protein correlated with levels of cartilage oligomeric matrix protein in both serum and synovial fluid (p less than 0.001 and 0.005, respectively). In vitro, RA synovial fibroblasts showed an increased release of galectin-3 into culture medium but decreased secretion of its binding protein. <a href="#14" class="mim-tip-reference" title="Ohshima, S., Kuchen, S., Seemayer, C. A., Kyburz, D., Hirt, A., Klinzing, S., Michel, B. A., Gay, R. E., Liu, F.-T., Gay, S., Neidhart, M. <strong>Galectin 3 and its binding protein in rheumatoid arthritis.</strong> Arthritis Rheum. 48: 2788-2795, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/14558084/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">14558084</a>] [<a href="https://doi.org/10.1002/art.11287" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="14558084">Ohshima et al. (2003)</a> concluded that galectin-3 and its binding protein are not only involved in inflammation but also contribute to the activation of synovial fibroblasts, and thus represent markers of disease activity in rheumatoid arthritis. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=14558084" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#15" class="mim-tip-reference" title="Partridge, E. A., Le Roy, C., Di Guglielmo, G. M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I. R., Wrana, J. L., Dennis, J. W. <strong>Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis.</strong> Science 306: 120-124, 2004.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/15459394/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">15459394</a>] [<a href="https://doi.org/10.1126/science.1102109" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="15459394">Partridge et al. (2004)</a> reported that expression of Mgat5 (<a href="/entry/601774">601774</a>) sensitized mouse cells to multiple cytokines. Gal3 crosslinked Mgat5-modified N-glycans on epidermal growth factor and transforming growth factor-beta receptors at the cell surface and delayed their removal by constitutive endocytosis. Mgat5 expression in mammary carcinoma was rate limiting for cytokine signaling and consequently for epithelial-mesenchymal transition, cell motility, and tumor metastasis. Mgat5 also promoted cytokine-mediated leukocyte signaling, phagocytosis, and extravasation in vivo. <a href="#15" class="mim-tip-reference" title="Partridge, E. A., Le Roy, C., Di Guglielmo, G. M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I. R., Wrana, J. L., Dennis, J. W. <strong>Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis.</strong> Science 306: 120-124, 2004.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/15459394/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">15459394</a>] [<a href="https://doi.org/10.1126/science.1102109" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="15459394">Partridge et al. (2004)</a> concluded that conditional regulation of N-glycan processing drives synchronous modification of cytokine receptors, which balances their surface retention against loss through endocytosis. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=15459394" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#6" class="mim-tip-reference" title="Henderson, N. C., Mackinnon, A. C., Farnworth, S. L., Poirier, F., Russo, F. P., Iredale, J. P., Haslett, C., Simpson, K. J., Sethi, T. <strong>Galectin-3 regulates myofibroblast activation and hepatic fibrosis.</strong> Proc. Nat. Acad. Sci. 103: 5060-5065, 2006.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16549783/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16549783</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16549783[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1073/pnas.0511167103" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="16549783">Henderson et al. (2006)</a> found that galectin-3 was upregulated in established human fibrotic liver disease. In experimental hepatic fibrosis in rats, galectin-3 upregulation was associated with induction and resolution of fibrosis. Disruption of the galectin-3 gene blocked myofibroblast activation and procollagen I expression in vitro and in vivo and attenuated liver fibrosis. Exogenous recombinant galectin-3 reversed this abnormality. Following liver injury and inflammation, hepatic fibrosis was reduced in galectin-3-null mice compared with wildtype mice. Tgf-beta (<a href="/entry/190180">190180</a>) failed to activate galectin-3-null mouse hepatic stellate cells, indicating that galectin-3 is required for Tgf-beta-mediated myofibroblast activation and matrix production. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16549783" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Both MUC1 (<a href="/entry/158340">158340</a>) and galectin-3 are widely expressed in human carcinomas. <a href="#18" class="mim-tip-reference" title="Ramasamy, S., Duraisamy, S., Barbashov, S., Kawano, T., Kharbanda, S., Kufe, D. <strong>The MUC1 and galectin-3 oncoproteins function in a microRNA-dependent regulatory loop.</strong> Molec. Cell 27: 992-1004, 2007.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/17889671/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">17889671</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=17889671[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1016/j.molcel.2007.07.031" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="17889671">Ramasamy et al. (2007)</a> showed that, following glycosylation on asn36, the MUC1 C-terminal subunit (MUC1C) induced galectin-3 expression by suppressing expression of miRNA322 (MIRN322; <a href="/entry/300682">300682</a>), a microRNA that destabilizes galectin-3 transcripts. In turn, galectin-3 bound MUC1C at the glycosylated asn36 site and formed a bridge between MUC1 and epidermal growth factor receptor (EGFR; <a href="/entry/131550">131550</a>), integrating MUC1 with EGF (<a href="/entry/131530">131530</a>) signaling. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=17889671" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#12" class="mim-tip-reference" title="Mazurek, N., Sun, Y. J., Liu, K.-F., Gilcrease, M. Z., Schober, W., Nangia-Makker, P., Raz, A., Bresalier, R. S. <strong>Phosphorylated galectin-3 mediates tumor necrosis factor-related apoptosis-inducing ligand signaling by regulating phosphatase and tensin homologue deleted on chromosome 10 in human breast carcinoma cells.</strong> J. Biol. Chem. 282: 21337-21348, 2007.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/17420249/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">17420249</a>] [<a href="https://doi.org/10.1074/jbc.M608810200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="17420249">Mazurek et al. (2007)</a> stated that GAL3 may exert anti- or pro- apoptotic activity depending on the cell type and the nature of the stimulus. They showed that introduction of phosphorylated GAL3 into a GAL3-null human breast cancer cell line promoted apoptotic cell death through TRAIL (TNFSF10; <a href="/entry/603598">603598</a>), a member of the tumor necrosis factor family that transmits death signals through death domain-containing receptors. Downstream, TRAIL sensitivity depended upon induction of PTEN (<a href="/entry/601728">601728</a>) expression, resulting in inactivation of the PI3K (see PIK3CA; <a href="/entry/171834">171834</a>)/AKT (AKT1; <a href="/entry/164730">164730</a>) survival pathway. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=17420249" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#2" class="mim-tip-reference" title="Chen, H.-Y., Fermin, A., Vardhana, S., Weng, I.-C., Lo, K. F. R., Chang, E.-Y., Maverakis, E., Yang, R.-Y., Hsu, D. K., Dustin, M. L., Liu, F.-T. <strong>Galectin-3 negatively regulates TCR-mediated CD4+ T-cell activation at the immunological synapse.</strong> Proc. Nat. Acad. Sci. 106: 14496-14501, 2009.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/19706535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">19706535</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=19706535[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1073/pnas.0903497106" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="19706535">Chen et al. (2009)</a> reported that Cd4 (<a href="/entry/186940">186940</a>)-positive T cells from mice lacking Gal3 secreted more Ifng (<a href="/entry/147570">147570</a>) and Il4 (<a href="/entry/147780">147780</a>) than wildtype cells after engagement of the T-cell receptor (TCR). In activated mouse and human T cells, GAL3 was recruited to the cytoplasmic side of the immunologic synapse, primarily in the peripheral supramolecular activation cluster (SMAC). Wildtype mouse T cells formed central SMAC less effectively and adhered to antigen-presenting cells less firmly than Gal3 -/- cells, suggesting that GAL3 is involved in stabilizing the immunologic synapse. Yeast 2-hybrid analysis of a human T-cell cDNA library, followed by coimmunoprecipitation and immunofluorescence analyses, identified ALIX (PDCD6IP; <a href="/entry/608074">608074</a>) as a GAL3 binding partner and showed that ALIX translocated to the immunologic synapse in activated T cells. <a href="#2" class="mim-tip-reference" title="Chen, H.-Y., Fermin, A., Vardhana, S., Weng, I.-C., Lo, K. F. R., Chang, E.-Y., Maverakis, E., Yang, R.-Y., Hsu, D. K., Dustin, M. L., Liu, F.-T. <strong>Galectin-3 negatively regulates TCR-mediated CD4+ T-cell activation at the immunological synapse.</strong> Proc. Nat. Acad. Sci. 106: 14496-14501, 2009.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/19706535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">19706535</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=19706535[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1073/pnas.0903497106" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="19706535">Chen et al. (2009)</a> concluded that GAL3 is an inhibitory regulator of T-cell activation and that it functions intracellularly by promoting TCR downregulation, possibly through modulation of ALIX function at the immunologic synapse. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=19706535" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Using real-time quantitative PCR, <a href="#10" class="mim-tip-reference" title="Mammen, M. J., Sands, M. F., Abou-Jaoude, E., Aalinkeel, R., Reynolds, J. L., Parikh, N. U., Sharma, U., Schwartz, S. A., Mahajan, S. D. <strong>Role of galectin-3 in the pathophysiology underlying allergic lung inflammation in a tissue inhibitor of metalloproteinases 1 knockout model of murine asthma.</strong> Immunology 153: 387-396, 2017.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/28992358/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">28992358</a>] [<a href="https://doi.org/10.1111/imm.12848" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="28992358">Mammen et al. (2017)</a> found significantly increased Gal3, Il17 (see <a href="/entry/603149">603149</a>), and Tgf-beta-1 gene expression in lung tissue of ovalbumin (OVA)-sensitized Timp1 (<a href="/entry/305370">305370</a>)-knockout mice, a model of allergic asthma, compared with sham-treated wildtype mice. ELISA revealed significantly increased Gal3 protein levels in serum of OVA-sensitized wildtype and Timp1-knockout mice compared with sham-treated wildtype and Timp1-knockout mice, but the increase was higher in the Timp1-knockout mice. Real-time quantitative PCR and Western blot analyses demonstrated increased Gal3 gene and protein expression in lung tissue of OVA-sensitized wildtype and Timp1-knockout mice compared with sham-treated wildtype and Timp1-knockout mice. Knockdown of GAL3 expression in A549 human lung epithelial cells suggested that GAL3 plays a pivotal role in the balance between a proinflammatory response and a protective antiinflammatory response by modulating IL17 levels. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=28992358" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#24" class="mim-tip-reference" title="Zhou, Y., He, C. H., Yang, D. S., Nguyen, T., Cao, Y., Kamle, S., Lee, C., Gochuico, B. R., Gahl, W. A., Shea, B. S., Lee, C. G., Elias, J. A. <strong>Galectin-3 interacts with the CHI3L1 axis and contributes to Hermansky-Pudlak syndrome lung disease.</strong> J. Immun. 200: 2140-2153, 2018.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/29427412/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">29427412</a>] [<a href="https://doi.org/10.4049/jimmunol.1701442" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="29427412">Zhou et al. (2018)</a> found that expression and accumulation of Gal3 increased in lungs during bleomycin-induced fibroproliferative repair in Hps1 (<a href="/entry/203300">203300</a>)-deficient 'pale ear' mice, a model of Hermansky-Pudlak syndrome-1 (HPS1; <a href="/entry/203300">203300</a>), compared with wildtype mice. Fibroblasts and macrophages from pale ear mice expressed and contained more Gal3 than wildtype cells and had a Gal3 trafficking defect that augmented intracellular accumulation of Gal3 and decreased secretion of Gal3 into extracellular space. In contrast, lung epithelial cells did not show induction or production of Gal3 in wildtype or pale ear mice. Comparison of the bleomycin-induced epithelial injury (apoptosis) and fibroproliferative repair (collagen accumulation) responses showed that intracellular Gal3 drove fibroproliferative repair by inhibiting fibroblast apoptosis, increasing fibroblast proliferation and differentiation. Extracellular Gal3, on the other hand, was a potent stimulator of lung epithelial apoptosis and did not produce effects like those of intracellular Gal3. Intracellular Gal3 did not regulate macrophage apoptosis but increased M2-like macrophage differentiation in pale ear mice. Further analysis showed that Gal3 inhibited the antiapoptotic effects of Chi3l1 (<a href="/entry/601525">601525</a>) to activate antiapoptotic signaling pathways and played a critical role in Chi3l1-induced Wnt (see <a href="/entry/606359">606359</a>)/beta-catenin (CTNNB1; <a href="/entry/116806">116806</a>) signaling in lung macrophages. Coimmunoprecipitation analysis demonstrated that Gal3 physically interacted with Chi3l1 and its receptor components, thereby abrogating Chi3l1-induced antiapoptotic signaling, augmenting Wnt/beta-catenin signaling, and contributing to development of epithelial cell death and tissue fibrosis in lungs of Hps1-deficient mice. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=29427412" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Using mice and mouse and human cells, <a href="#3" class="mim-tip-reference" title="Chen, Y., Wang, H., Shen, J., Deng, R., Yao, X., Guo, Q., Lu, A., Sun, B., Zhang, Y., Meng, G. <strong>Gasdermin D drives the nonexosomal secretion of galectin-3, an insulin signal antagonist.</strong> J. Immun. 203: 2712-2723, 2019.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/31597705/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">31597705</a>] [<a href="https://doi.org/10.4049/jimmunol.1900212" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="31597705">Chen et al. (2019)</a> showed that secretion of galectin-3, including serum galectin-3, relied on activation of the NLRP3 (<a href="/entry/606416">606416</a>) inflammasome. The exosome pathway did not mediate NLRP3 inflammasome-driven galectin-3 secretion. Instead, gasdermin D (GSDMD; <a href="/entry/617042">617042</a>) perforated the plasma membrane to allow nonexosomal release of galectin-3. Knockout analysis in mice demonstrated that galectin-3 was an Nlrp3 inflammasome effector that desensitized insulin signaling. Nlrp3 inflammasome-mediated galectin-3 secretion exacerbated insulin resistance in mice. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=31597705" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#5" class="mim-tip-reference" title="Guittaut, M., Charpentier, S., Normand, T., Dubois, M., Raimond, J., Legrand, A. <strong>Identification of an internal gene to the human galectin-3 gene with two different overlapping reading frames that do not encode galectin-3.</strong> J. Biol. Chem. 276: 2652-2657, 2001.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11160123/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11160123</a>] [<a href="https://doi.org/10.1074/jbc.m002523200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11160123">Guittaut et al. (2001)</a> reported that the LGALS3 gene contains 6 exons. It has a proximal promoter upstream of exon 1 and a conserved internal promoter within the 5-prime region of intron 2. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11160123" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#19" class="mim-tip-reference" title="Raz, A., Carmi, P., Raz, T., Hogan, V., Mohamed, A., Wolman, S. R. <strong>Molecular cloning and chromosomal mapping of a human galactoside-binding protein.</strong> Cancer Res. 51: 2173-2178, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2009535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2009535</a>]" pmid="2009535">Raz et al. (1991)</a> mapped the gene encoding galactoside-binding protein, symbolized GALBP by them, to 1p13 by in situ hybridization. Conflicting mapping results were obtained by <a href="#17" class="mim-tip-reference" title="Raimond, J., Zimonjic, D. B., Mignon, C., Mattei, M.-G., Popescu, N. C., Monsigny, M., Legrand, A. <strong>Mapping of the galectin-3 gene (LGALS3) to human chromosome 14 at region 14q21-22.</strong> Mammalian Genome 8: 706-707, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9271684/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9271684</a>] [<a href="https://doi.org/10.1007/s003359900548" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9271684">Raimond et al. (1997)</a>, who mapped the LGALS3 gene to 14q21-q22 by fluorescence in situ hybridization and confirmed the location by isotopic hybridization with a tritium-labeled probe. No secondary peak of hybridization was observed by either method on the short arm of chromosome 1 where the gene had been tentatively assigned by <a href="#19" class="mim-tip-reference" title="Raz, A., Carmi, P., Raz, T., Hogan, V., Mohamed, A., Wolman, S. R. <strong>Molecular cloning and chromosomal mapping of a human galactoside-binding protein.</strong> Cancer Res. 51: 2173-2178, 1991.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2009535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2009535</a>]" pmid="2009535">Raz et al. (1991)</a>. Presumably, the chromosome 14 location is the true one. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2009535+9271684" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>Neutrophil extravasation is mediated by ITGB2 (<a href="/entry/600065">600065</a>) and selectins (e.g., SELE; <a href="/entry/131210">131210</a>). Using an in vivo streptococcal pneumonia mouse model, <a href="#22" class="mim-tip-reference" title="Sato, S., Ouellet, N., Pelletier, I., Simard, M., Rancourt, A., Bergeron, M. G. <strong>Role of galectin-3 as an adhesion molecule for neutrophil extravasation during streptococcal pneumonia.</strong> J. Immun. 168: 1813-1822, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11823514/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11823514</a>] [<a href="https://doi.org/10.4049/jimmunol.168.4.1813" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11823514">Sato et al. (2002)</a> showed by Western blot analysis an accumulation of galectin-3 in the bronchoalveolar lavage fluid that correlated with the kinetics of neutrophil emigration to alveoli during S. pneumoniae, but not E. coli, infection. Immunohistochemical analysis demonstrated galectin-3 expression on endothelial and epithelial cell layers and interstitial spaces in lung tissue. Functional analysis indicated that galectin-3 promoted neutrophil adhesion to endothelial cells and that this resulted from direct crosslinking of neutrophils and was dependent on galectin-3 oligomerization. <a href="#22" class="mim-tip-reference" title="Sato, S., Ouellet, N., Pelletier, I., Simard, M., Rancourt, A., Bergeron, M. G. <strong>Role of galectin-3 as an adhesion molecule for neutrophil extravasation during streptococcal pneumonia.</strong> J. Immun. 168: 1813-1822, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11823514/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11823514</a>] [<a href="https://doi.org/10.4049/jimmunol.168.4.1813" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11823514">Sato et al. (2002)</a> suggested that galectin-3 plays a role in ITGB2-independent neutrophil extravasation during alveolar infection with S. pneumoniae. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11823514" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Using models of corneal wound healing, <a href="#1" class="mim-tip-reference" title="Cao, Z., Said, N., Amin, S., Wu, H. K., Bruce, A., Garate, M., Hsu, D. K., Kuwabara, I., Liu, F.-T., Panjwani, N. <strong>Galectin-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds.</strong> J. Biol. Chem. 277: 42299-42305, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12194966/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12194966</a>] [<a href="https://doi.org/10.1074/jbc.M200981200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12194966">Cao et al. (2002)</a> found that reepithelialization of wounds was significantly slower in Gal3-null mice compared with wildtype mice, and the difference was not due to a reduced epithelial cell proliferation rate. Gene expression analysis using cDNA microarrays revealed that healing corneas of Gal3-null mice had reduced levels of Gal7 (<a href="/entry/600615">600615</a>). Exogenous application of Gal7, but not Gal3, accelerated reepithelialization of wounds in Gal3-null mice. Both Gal3 and Gal7 accelerated corneal wound healing in wildtype mice. <a href="#1" class="mim-tip-reference" title="Cao, Z., Said, N., Amin, S., Wu, H. K., Bruce, A., Garate, M., Hsu, D. K., Kuwabara, I., Liu, F.-T., Panjwani, N. <strong>Galectin-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds.</strong> J. Biol. Chem. 277: 42299-42305, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12194966/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12194966</a>] [<a href="https://doi.org/10.1074/jbc.M200981200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12194966">Cao et al. (2002)</a> concluded that both GAL3 and GAL7 play a role in reepithelialization of corneal wounds. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12194966" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#20" class="mim-tip-reference" title="Sano, H., Hsu, D. K., Apgar, J. R., Yu, L., Sharma, B. B., Kuwabara, I., Izui, S., Liu, F.-T. <strong>Critical role of galectin-3 in phagocytosis by macrophages.</strong> J. Clin. Invest. 112: 389-397, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12897206/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12897206</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=12897206[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1172/JCI17592" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12897206">Sano et al. (2003)</a> demonstrated reduced phagocytosis of IgG-opsonized erythrocytes and apoptotic thymocytes in Gal3 -/- macrophages compared to wildtype. Gal3-null mice showed attenuated phagocytic clearance of apoptotic thymocytes by peritoneal macrophages and reduced IgG-mediated phagocytosis of erythrocytes by Kupffer cells in a mouse model of autoimmune hemolytic anemia. Extracellular Gal3 did not contribute to phagocytosis. <a href="#20" class="mim-tip-reference" title="Sano, H., Hsu, D. K., Apgar, J. R., Yu, L., Sharma, B. B., Kuwabara, I., Izui, S., Liu, F.-T. <strong>Critical role of galectin-3 in phagocytosis by macrophages.</strong> J. Clin. Invest. 112: 389-397, 2003.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12897206/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12897206</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=12897206[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1172/JCI17592" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="12897206">Sano et al. (2003)</a> concluded that GAL3 may play an important role in both innate and adaptive immunity by contributing to phagocytic clearance of microorganisms and apoptotic cells. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12897206" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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Cao, Z., Said, N., Amin, S., Wu, H. K., Bruce, A., Garate, M., Hsu, D. K., Kuwabara, I., Liu, F.-T., Panjwani, N.
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<strong>Galectin-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds.</strong>
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J. Biol. Chem. 277: 42299-42305, 2002.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12194966/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12194966</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12194966" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1074/jbc.M200981200" target="_blank">Full Text</a>]
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<a id="Chen2009" class="mim-anchor"></a>
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Chen, H.-Y., Fermin, A., Vardhana, S., Weng, I.-C., Lo, K. F. R., Chang, E.-Y., Maverakis, E., Yang, R.-Y., Hsu, D. K., Dustin, M. L., Liu, F.-T.
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<strong>Galectin-3 negatively regulates TCR-mediated CD4+ T-cell activation at the immunological synapse.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/19706535/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">19706535</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=19706535[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=19706535" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1073/pnas.0903497106" target="_blank">Full Text</a>]
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Chen, Y., Wang, H., Shen, J., Deng, R., Yao, X., Guo, Q., Lu, A., Sun, B., Zhang, Y., Meng, G.
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<strong>Gasdermin D drives the nonexosomal secretion of galectin-3, an insulin signal antagonist.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/31597705/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">31597705</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=31597705" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.4049/jimmunol.1900212" target="_blank">Full Text</a>]
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Cherayil, B. J., Chaitovitz, S., Wong, C., Pillai, S.
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<strong>Molecular cloning of a human macrophage lectin specific for galactose.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2402511/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2402511</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2402511" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1073/pnas.87.18.7324" target="_blank">Full Text</a>]
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Guittaut, M., Charpentier, S., Normand, T., Dubois, M., Raimond, J., Legrand, A.
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<strong>Identification of an internal gene to the human galectin-3 gene with two different overlapping reading frames that do not encode galectin-3.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11160123/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11160123</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11160123" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1074/jbc.m002523200" target="_blank">Full Text</a>]
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Henderson, N. C., Mackinnon, A. C., Farnworth, S. L., Poirier, F., Russo, F. P., Iredale, J. P., Haslett, C., Simpson, K. J., Sethi, T.
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<strong>Galectin-3 regulates myofibroblast activation and hepatic fibrosis.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16549783/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16549783</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16549783[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16549783" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1073/pnas.0511167103" target="_blank">Full Text</a>]
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Hsu, D. K., Dowling, C. A., Jeng, K.-C. G., Chen, J.-T., Yang, R.-Y., Liu, F.-T.
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<strong>Galectin-3 expression is induced in cirrhotic liver and hepatocellular carcinoma.</strong>
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Int. J. Cancer 81: 519-526, 1999.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10225438/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10225438</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10225438" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1002/(sici)1097-0215(19990517)81:4<519::aid-ijc3>3.0.co;2-0" target="_blank">Full Text</a>]
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Huflejt, M. E., Jordan, E. T., Gitt, M. A., Barondes, S. H., Leffler, H.
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<strong>Strikingly different localization of galectin-3 and galectin-4 in human colon adenocarcinoma T84 cells: galectin-4 is localized at sites of cell adhesion.</strong>
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J. Biol. Chem. 272: 14294-14303, 1997.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9162064/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9162064</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9162064" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1074/jbc.272.22.14294" target="_blank">Full Text</a>]
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Madsen, P., Rasmussen, H. H., Flint, T., Gromov, P., Kruse, T. A., Honore, B., Vorum, H., Celis, J. E.
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<strong>Cloning, expression, and chromosome mapping of human galectin-7.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7534301/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7534301</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7534301" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1074/jbc.270.11.5823" target="_blank">Full Text</a>]
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<a id="Mammen2017" class="mim-anchor"></a>
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Mammen, M. J., Sands, M. F., Abou-Jaoude, E., Aalinkeel, R., Reynolds, J. L., Parikh, N. U., Sharma, U., Schwartz, S. A., Mahajan, S. D.
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<strong>Role of galectin-3 in the pathophysiology underlying allergic lung inflammation in a tissue inhibitor of metalloproteinases 1 knockout model of murine asthma.</strong>
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Immunology 153: 387-396, 2017.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/28992358/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">28992358</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=28992358" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1111/imm.12848" target="_blank">Full Text</a>]
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Martins, L., Matsuo, S. E., Ebina, K. N., Kulcsar, M. A. V., Friguglietti, C. U. M., Kimura, E. T.
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<strong>Galectin-3 messenger ribonucleic acid and protein are expressed in benign thyroid tumors.</strong>
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J. Clin. Endocr. Metab. 87: 4806-4810, 2002.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12364477/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12364477</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12364477" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1210/jc.2002-020094" target="_blank">Full Text</a>]
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<strong>Phosphorylated galectin-3 mediates tumor necrosis factor-related apoptosis-inducing ligand signaling by regulating phosphatase and tensin homologue deleted on chromosome 10 in human breast carcinoma cells.</strong>
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[<a href="https://doi.org/10.1074/jbc.M608810200" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1210/jc.2002-021907" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1002/art.11287" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1126/science.1102109" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1016/0014-5793(95)00310-6" target="_blank">Full Text</a>]
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[<a href="https://doi.org/10.1007/s003359900548" target="_blank">Full Text</a>]
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/17889671/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">17889671</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=17889671[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=17889671" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1016/j.molcel.2007.07.031" target="_blank">Full Text</a>]
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12897206/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12897206</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=12897206[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12897206" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1172/JCI17592" target="_blank">Full Text</a>]
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J. Immun. 165: 2156-2164, 2000.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10925302/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10925302</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10925302" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.4049/jimmunol.165.4.2156" target="_blank">Full Text</a>]
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Sato, S., Ouellet, N., Pelletier, I., Simard, M., Rancourt, A., Bergeron, M. G.
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<strong>Role of galectin-3 as an adhesion molecule for neutrophil extravasation during streptococcal pneumonia.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11823514/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11823514</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11823514" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.4049/jimmunol.168.4.1813" target="_blank">Full Text</a>]
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Yoshimura, A., Gemma, A., Hosoya, Y., Komaki, E., Hosomi, Y., Okano, T., Takenaka, K., Matuda, K., Seike, M., Uematsu, K., Hibino, S., Shibuya, M., Yamada, T., Hirohashi, S., Kudoh, S.
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<strong>Increased expression of the LGALS3 (galectin 3) gene in human non-small-cell lung cancer.</strong>
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/12696064/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">12696064</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=12696064" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1002/gcc.10205" target="_blank">Full Text</a>]
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Zhou, Y., He, C. H., Yang, D. S., Nguyen, T., Cao, Y., Kamle, S., Lee, C., Gochuico, B. R., Gahl, W. A., Shea, B. S., Lee, C. G., Elias, J. A.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/29427412/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">29427412</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=29427412" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.4049/jimmunol.1701442" target="_blank">Full Text</a>]
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Bao Lige - updated : 03/10/2020
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<span class="mim-text-font">
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Bao Lige - updated : 11/13/2018<br>Paul J. Converse - updated : 10/17/2011<br>Patricia A. Hartz - updated : 12/26/2007<br>Patricia A. Hartz - updated : 11/2/2007<br>Patricia A. Hartz - updated : 10/18/2007<br>Patricia A. Hartz - updated : 6/2/2006<br>Marla J. F. O'Neill - updated : 2/21/2005<br>Ada Hamosh - updated : 2/2/2005<br>Marla J. F. O'Neill - updated : 9/1/2004<br>John A. Phillips, III - updated : 9/2/2003<br>Victor A. McKusick - updated : 8/7/2003<br>John A. Phillips, III - updated : 4/8/2003<br>Patricia A. Hartz - updated : 12/17/2002<br>Paul J. Converse - updated : 3/25/2002<br>Paul J. Converse - updated : 9/22/2000<br>Victor A. McKusick - updated : 6/8/1999<br>Victor A. McKusick - updated : 9/16/1997
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Victor A. McKusick : 10/16/1990
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carol : 11/14/2018<br>mgross : 11/13/2018<br>carol : 08/18/2016<br>carol : 07/13/2016<br>mgross : 11/3/2011<br>terry : 10/17/2011<br>wwang : 12/26/2007<br>mgross : 11/7/2007<br>terry : 11/2/2007<br>mgross : 10/23/2007<br>mgross : 10/23/2007<br>terry : 10/18/2007<br>mgross : 6/8/2006<br>terry : 6/2/2006<br>terry : 3/16/2005<br>terry : 2/21/2005<br>carol : 2/18/2005<br>terry : 2/2/2005<br>carol : 10/27/2004<br>carol : 9/2/2004<br>terry : 9/1/2004<br>alopez : 9/2/2003<br>tkritzer : 8/12/2003<br>terry : 8/7/2003<br>cwells : 5/1/2003<br>terry : 4/8/2003<br>mgross : 1/3/2003<br>terry : 12/17/2002<br>mgross : 3/26/2002<br>terry : 3/25/2002<br>mgross : 9/22/2000<br>jlewis : 6/18/1999<br>jlewis : 6/17/1999<br>terry : 6/8/1999<br>dkim : 7/21/1998<br>dholmes : 4/14/1998<br>jenny : 9/19/1997<br>terry : 9/16/1997<br>mark : 8/19/1997<br>mark : 5/21/1996<br>mark : 6/16/1995<br>supermim : 3/16/1992<br>carol : 10/16/1990
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<span class="mim-font">
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<strong>*</strong> 153619
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<h3>
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LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 3; LGALS3
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</h3>
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<em>Alternative titles; symbols</em>
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MACROPHAGE GALACTOSE-SPECIFIC LECTIN; MAC2<br />
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GALACTOSIDE-BINDING PROTEIN; GALBP<br />
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GALECTIN 3; GAL3
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Other entities represented in this entry:
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GALECTIN 3 INTERNAL GENE, INCLUDED; GALIG, INCLUDED
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<strong><em>HGNC Approved Gene Symbol: LGALS3</em></strong>
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Cytogenetic location: 14q22.3
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Genomic coordinates <span class="small">(GRCh38)</span> : 14:55,129,252-55,145,430 </span>
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<span class="small">(from NCBI)</span>
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<strong>TEXT</strong>
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<strong>Cloning and Expression</strong>
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<p>The murine Mac2 protein is a galactose- and IgE-binding lectin secreted by inflammatory macrophages. Cherayil et al. (1990) cloned and characterized a cDNA representing the human homolog. The amino acid sequence derived therefrom indicated that the protein is evolutionarily highly conserved, especially in the C-terminal lectin domain. Human MAC2 synthesized in vitro is recognized by a monoclonal antibody to mouse Mac2 and behaves like a galactose-specific lectin in its binding to the desialylated glycoprotein asialofetuin. It also binds to purified laminin (see 150320), indicating a potential role in macrophage extracellular matrix interactions. MAC2 is also known as galectin-3 (LGALS3), as mentioned in Madsen et al. (1995). </p><p>From a human fibrosarcoma cDNA library, Raz et al. (1991) cloned a galactoside-binding protein with a molecular weight of 31,000. The deduced 242-amino acid protein has the characteristics of a carbohydrate-binding protein. The deduced amino acid sequence contains 95 residues at the N terminus that are homologous to the predicted amino acid sequence of the second exon of the oncogene LMYC (164850). </p><p>Huflejt et al. (1997) found that LGALS3 and LGALS4 (602518) have very different cellular localizations in human colon adenocarcinoma T84 cells, suggesting that these LGALSs have different targeting mechanisms, ligands, and functions. In confluent T84 cells, LGALS3 is concentrated mainly at the apical membrane in large granular inclusions. In subconfluent T84 cells, it is distributed along most of the cell periphery and is concentrated in the posterior part of lamellipodia. </p><p>By RT-PCR of a human osteosarcoma cell line, Raimond et al. (1995) identified galectin-3 transcripts initiated from the promoter upstream of exon 1 and from the internal promoter within intron 2. Using RT-PCR and EST database analysis, Guittaut et al. (2001) obtained transcripts originating from the internal promoter in intron 2 of LGALS3 from several cDNA libraries. They concluded that these transcripts arise from a gene embedded within LGALS3 that they called 'galectin-3 internal gene,' or GALIG. The GALIG transcripts contain 2 overlapping ORFs, ORF1 and ORF2, that initiate in exon 3 of LGALS3 and are out-of-frame relative to the LGALS3 coding sequence. RT-PCR detected variable and tissue-specific expression of LGALS3 and GALIG transcripts. GALIG transcripts showed highest expression in peripheral blood leukocytes, but overall they were much less abundant than LGALS3 transcripts. In transfected osteosarcoma cells, fluorescence-tagged ORF1 localized to cytosol and nucleus, and fluorescence-tagged ORF2 localized to mitochondria. </p>
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<strong>Gene Function</strong>
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<p>Galectin-3 is expressed in various tissues and organs, but is significantly absent in normal hepatocytes. However, evaluation of patient liver biopsies for galectin-3 expression revealed that hepatocellular carcinoma (HCC) frequently expressed significant levels of this lectin; 76% were immunohistochemically positive. Further investigations showed that galectin-3 expression in HCC is independent of whether the patient had prior hepatitis B virus infection (Hsu et al., 1999). Hsu et al. (1999) suggested that deregulated expression of galectin-3 can result in tumor transformation and invasiveness, or confer propensity for tumor cell survival. </p><p>Using reporter gene assays, Raimond et al. (1995) showed that p53 (TP53; 191170) downregulated expression of the GALIG promoter when cotransfected into a human osteosarcoma cell line. </p><p>In the thyroid, expression of galectin-3 protein had been described in differentiated follicular cancer, suggesting that the immunohistochemical study of galectin-3 may be a potential marker of malignancy in thyroid neoplasms. Martins et al. (2002) analyzed galectin-3 protein and mRNA expression in thyroid tissues from 87 patients with histomorphologic diagnosis of multinodular goiter (MNG), follicular adenoma, follicular carcinoma, papillary carcinoma, and 5 normal tissues. Galectin-3 mRNA expression was detected by RT-PCR. Their results showed that the majority of carcinomas expressed galectin-3 protein (follicular, 90%; papillary, 100%). However, in contrast to the previously published data, benign lesions also expressed galectin-3 (adenoma, 45%; MNG, 17%). The authors showed by RT-PCR that thyroid tissues with diagnosis of adenoma and MNG expressed galectin-3 mRNA. Although the galectin-3 immunostaining demonstrated a sensitivity of 93.8% in the identification of cancer, the accuracy in the distinction between benign and malignant tissues was 77.0%. This accuracy was even lower (68.6%) when galectin-3 expression in follicular adenoma was compared with follicular carcinoma. </p><p>Using micro-Boyden chamber analysis, Sano et al. (2000) determined that LGALS3 has chemoattractant activity not for eosinophils, like LGALS9 (601879), but for monocytes and mature macrophages. At high concentrations LGALS3 activity is chemotactic, i.e., cells migrate towards the attractant, whereas at low concentrations it is chemokinetic, i.e., it enhances movement of cells in all directions. Sano et al. (2000) found that the chemoattractant activity is inhibited by lactose, indicating that the C-terminal lectin domain of LGALS3 is required. A C-terminal domain fragment was unable to mediate chemoattraction, suggesting that the N-terminal domain is also necessary for activity. Both migration and increased intracellular calcium concentration were pertussis toxin sensitive and therefore probably mediated by a G protein-coupled receptor. The authors determined that LGALS3 does not, however, use the chemokine receptors CCR1 (601159), CCR2 (601267), CCR5 (601373), and CXCR4 (162643). </p><p>Yoshimura et al. (2003) found increased expression of the LGALS3 gene in human nonsmall cell lung cancer, and suggested that it may play a role in the process of metastasis in this malignancy but not in small cell lung cancer. They considered that LGALS3 may be a phenotypic marker that excludes small cell lung cancer and a novel target molecule in therapy of nonsmall cell lung cancer. </p><p>Nikiforova et al. (2003) analyzed a series of 88 conventional follicular and Hurthle cell thyroid tumors for RAS (HRAS, 190020; NRAS, 164790; KRAS, 190070) mutations and PAX8 (167415)-PPARG (601487) rearrangements using molecular methods and for galectin-3 and mesothelioma antibody HBME-1 expression by immunohistochemistry. Forty-nine percent of conventional follicular carcinomas had RAS mutations, 36% had PAX8-PPARG rearrangement, and only 1 (3%) had both. Of follicular adenomas, 48% had RAS mutations, 4% had PAX8-PPARG rearrangement, and 48% had neither. Follicular carcinomas with RAS mutations most often displayed an HBME-1-positive/galectin-3-negative immunophenotype and were either minimally or overtly invasive. Hurthle cell tumors infrequently had PAX8-PPARG rearrangement or RAS mutations. </p><p>Ohshima et al. (2003) found that galectin-3 mRNA and protein are expressed throughout synovial tissue in rheumatoid arthritis (RA; 180300) and that both galectin-3 and its binding protein are found at sites of joint destruction. In addition, levels of galectin-3 in serum and synovial fluid as well as levels of its binding protein in synovial fluid were significantly elevated in RA compared to osteoarthritis and healthy controls (p less than 0.001). Serum galectin-3 levels correlated significantly with C-reactive protein levels (p less than 0.001), and levels of its binding protein correlated with levels of cartilage oligomeric matrix protein in both serum and synovial fluid (p less than 0.001 and 0.005, respectively). In vitro, RA synovial fibroblasts showed an increased release of galectin-3 into culture medium but decreased secretion of its binding protein. Ohshima et al. (2003) concluded that galectin-3 and its binding protein are not only involved in inflammation but also contribute to the activation of synovial fibroblasts, and thus represent markers of disease activity in rheumatoid arthritis. </p><p>Partridge et al. (2004) reported that expression of Mgat5 (601774) sensitized mouse cells to multiple cytokines. Gal3 crosslinked Mgat5-modified N-glycans on epidermal growth factor and transforming growth factor-beta receptors at the cell surface and delayed their removal by constitutive endocytosis. Mgat5 expression in mammary carcinoma was rate limiting for cytokine signaling and consequently for epithelial-mesenchymal transition, cell motility, and tumor metastasis. Mgat5 also promoted cytokine-mediated leukocyte signaling, phagocytosis, and extravasation in vivo. Partridge et al. (2004) concluded that conditional regulation of N-glycan processing drives synchronous modification of cytokine receptors, which balances their surface retention against loss through endocytosis. </p><p>Henderson et al. (2006) found that galectin-3 was upregulated in established human fibrotic liver disease. In experimental hepatic fibrosis in rats, galectin-3 upregulation was associated with induction and resolution of fibrosis. Disruption of the galectin-3 gene blocked myofibroblast activation and procollagen I expression in vitro and in vivo and attenuated liver fibrosis. Exogenous recombinant galectin-3 reversed this abnormality. Following liver injury and inflammation, hepatic fibrosis was reduced in galectin-3-null mice compared with wildtype mice. Tgf-beta (190180) failed to activate galectin-3-null mouse hepatic stellate cells, indicating that galectin-3 is required for Tgf-beta-mediated myofibroblast activation and matrix production. </p><p>Both MUC1 (158340) and galectin-3 are widely expressed in human carcinomas. Ramasamy et al. (2007) showed that, following glycosylation on asn36, the MUC1 C-terminal subunit (MUC1C) induced galectin-3 expression by suppressing expression of miRNA322 (MIRN322; 300682), a microRNA that destabilizes galectin-3 transcripts. In turn, galectin-3 bound MUC1C at the glycosylated asn36 site and formed a bridge between MUC1 and epidermal growth factor receptor (EGFR; 131550), integrating MUC1 with EGF (131530) signaling. </p><p>Mazurek et al. (2007) stated that GAL3 may exert anti- or pro- apoptotic activity depending on the cell type and the nature of the stimulus. They showed that introduction of phosphorylated GAL3 into a GAL3-null human breast cancer cell line promoted apoptotic cell death through TRAIL (TNFSF10; 603598), a member of the tumor necrosis factor family that transmits death signals through death domain-containing receptors. Downstream, TRAIL sensitivity depended upon induction of PTEN (601728) expression, resulting in inactivation of the PI3K (see PIK3CA; 171834)/AKT (AKT1; 164730) survival pathway. </p><p>Chen et al. (2009) reported that Cd4 (186940)-positive T cells from mice lacking Gal3 secreted more Ifng (147570) and Il4 (147780) than wildtype cells after engagement of the T-cell receptor (TCR). In activated mouse and human T cells, GAL3 was recruited to the cytoplasmic side of the immunologic synapse, primarily in the peripheral supramolecular activation cluster (SMAC). Wildtype mouse T cells formed central SMAC less effectively and adhered to antigen-presenting cells less firmly than Gal3 -/- cells, suggesting that GAL3 is involved in stabilizing the immunologic synapse. Yeast 2-hybrid analysis of a human T-cell cDNA library, followed by coimmunoprecipitation and immunofluorescence analyses, identified ALIX (PDCD6IP; 608074) as a GAL3 binding partner and showed that ALIX translocated to the immunologic synapse in activated T cells. Chen et al. (2009) concluded that GAL3 is an inhibitory regulator of T-cell activation and that it functions intracellularly by promoting TCR downregulation, possibly through modulation of ALIX function at the immunologic synapse. </p><p>Using real-time quantitative PCR, Mammen et al. (2017) found significantly increased Gal3, Il17 (see 603149), and Tgf-beta-1 gene expression in lung tissue of ovalbumin (OVA)-sensitized Timp1 (305370)-knockout mice, a model of allergic asthma, compared with sham-treated wildtype mice. ELISA revealed significantly increased Gal3 protein levels in serum of OVA-sensitized wildtype and Timp1-knockout mice compared with sham-treated wildtype and Timp1-knockout mice, but the increase was higher in the Timp1-knockout mice. Real-time quantitative PCR and Western blot analyses demonstrated increased Gal3 gene and protein expression in lung tissue of OVA-sensitized wildtype and Timp1-knockout mice compared with sham-treated wildtype and Timp1-knockout mice. Knockdown of GAL3 expression in A549 human lung epithelial cells suggested that GAL3 plays a pivotal role in the balance between a proinflammatory response and a protective antiinflammatory response by modulating IL17 levels. </p><p>Zhou et al. (2018) found that expression and accumulation of Gal3 increased in lungs during bleomycin-induced fibroproliferative repair in Hps1 (203300)-deficient 'pale ear' mice, a model of Hermansky-Pudlak syndrome-1 (HPS1; 203300), compared with wildtype mice. Fibroblasts and macrophages from pale ear mice expressed and contained more Gal3 than wildtype cells and had a Gal3 trafficking defect that augmented intracellular accumulation of Gal3 and decreased secretion of Gal3 into extracellular space. In contrast, lung epithelial cells did not show induction or production of Gal3 in wildtype or pale ear mice. Comparison of the bleomycin-induced epithelial injury (apoptosis) and fibroproliferative repair (collagen accumulation) responses showed that intracellular Gal3 drove fibroproliferative repair by inhibiting fibroblast apoptosis, increasing fibroblast proliferation and differentiation. Extracellular Gal3, on the other hand, was a potent stimulator of lung epithelial apoptosis and did not produce effects like those of intracellular Gal3. Intracellular Gal3 did not regulate macrophage apoptosis but increased M2-like macrophage differentiation in pale ear mice. Further analysis showed that Gal3 inhibited the antiapoptotic effects of Chi3l1 (601525) to activate antiapoptotic signaling pathways and played a critical role in Chi3l1-induced Wnt (see 606359)/beta-catenin (CTNNB1; 116806) signaling in lung macrophages. Coimmunoprecipitation analysis demonstrated that Gal3 physically interacted with Chi3l1 and its receptor components, thereby abrogating Chi3l1-induced antiapoptotic signaling, augmenting Wnt/beta-catenin signaling, and contributing to development of epithelial cell death and tissue fibrosis in lungs of Hps1-deficient mice. </p><p>Using mice and mouse and human cells, Chen et al. (2019) showed that secretion of galectin-3, including serum galectin-3, relied on activation of the NLRP3 (606416) inflammasome. The exosome pathway did not mediate NLRP3 inflammasome-driven galectin-3 secretion. Instead, gasdermin D (GSDMD; 617042) perforated the plasma membrane to allow nonexosomal release of galectin-3. Knockout analysis in mice demonstrated that galectin-3 was an Nlrp3 inflammasome effector that desensitized insulin signaling. Nlrp3 inflammasome-mediated galectin-3 secretion exacerbated insulin resistance in mice. </p>
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<strong>Gene Structure</strong>
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<p>Guittaut et al. (2001) reported that the LGALS3 gene contains 6 exons. It has a proximal promoter upstream of exon 1 and a conserved internal promoter within the 5-prime region of intron 2. </p>
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<span class="mim-font">
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<strong>Mapping</strong>
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<p>Raz et al. (1991) mapped the gene encoding galactoside-binding protein, symbolized GALBP by them, to 1p13 by in situ hybridization. Conflicting mapping results were obtained by Raimond et al. (1997), who mapped the LGALS3 gene to 14q21-q22 by fluorescence in situ hybridization and confirmed the location by isotopic hybridization with a tritium-labeled probe. No secondary peak of hybridization was observed by either method on the short arm of chromosome 1 where the gene had been tentatively assigned by Raz et al. (1991). Presumably, the chromosome 14 location is the true one. </p>
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<strong>Animal Model</strong>
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<p>Neutrophil extravasation is mediated by ITGB2 (600065) and selectins (e.g., SELE; 131210). Using an in vivo streptococcal pneumonia mouse model, Sato et al. (2002) showed by Western blot analysis an accumulation of galectin-3 in the bronchoalveolar lavage fluid that correlated with the kinetics of neutrophil emigration to alveoli during S. pneumoniae, but not E. coli, infection. Immunohistochemical analysis demonstrated galectin-3 expression on endothelial and epithelial cell layers and interstitial spaces in lung tissue. Functional analysis indicated that galectin-3 promoted neutrophil adhesion to endothelial cells and that this resulted from direct crosslinking of neutrophils and was dependent on galectin-3 oligomerization. Sato et al. (2002) suggested that galectin-3 plays a role in ITGB2-independent neutrophil extravasation during alveolar infection with S. pneumoniae. </p><p>Using models of corneal wound healing, Cao et al. (2002) found that reepithelialization of wounds was significantly slower in Gal3-null mice compared with wildtype mice, and the difference was not due to a reduced epithelial cell proliferation rate. Gene expression analysis using cDNA microarrays revealed that healing corneas of Gal3-null mice had reduced levels of Gal7 (600615). Exogenous application of Gal7, but not Gal3, accelerated reepithelialization of wounds in Gal3-null mice. Both Gal3 and Gal7 accelerated corneal wound healing in wildtype mice. Cao et al. (2002) concluded that both GAL3 and GAL7 play a role in reepithelialization of corneal wounds. </p><p>Sano et al. (2003) demonstrated reduced phagocytosis of IgG-opsonized erythrocytes and apoptotic thymocytes in Gal3 -/- macrophages compared to wildtype. Gal3-null mice showed attenuated phagocytic clearance of apoptotic thymocytes by peritoneal macrophages and reduced IgG-mediated phagocytosis of erythrocytes by Kupffer cells in a mouse model of autoimmune hemolytic anemia. Extracellular Gal3 did not contribute to phagocytosis. Sano et al. (2003) concluded that GAL3 may play an important role in both innate and adaptive immunity by contributing to phagocytic clearance of microorganisms and apoptotic cells. </p>
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<strong>REFERENCES</strong>
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Cao, Z., Said, N., Amin, S., Wu, H. K., Bruce, A., Garate, M., Hsu, D. K., Kuwabara, I., Liu, F.-T., Panjwani, N.
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<strong>Galectin-3 and -7, but not galectin-1, play a role in re-epithelialization of wounds.</strong>
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J. Biol. Chem. 277: 42299-42305, 2002.
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[PubMed: 12194966]
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[Full Text: https://doi.org/10.1074/jbc.M200981200]
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Chen, H.-Y., Fermin, A., Vardhana, S., Weng, I.-C., Lo, K. F. R., Chang, E.-Y., Maverakis, E., Yang, R.-Y., Hsu, D. K., Dustin, M. L., Liu, F.-T.
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<strong>Galectin-3 negatively regulates TCR-mediated CD4+ T-cell activation at the immunological synapse.</strong>
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Proc. Nat. Acad. Sci. 106: 14496-14501, 2009.
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[PubMed: 19706535]
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[Full Text: https://doi.org/10.1073/pnas.0903497106]
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Chen, Y., Wang, H., Shen, J., Deng, R., Yao, X., Guo, Q., Lu, A., Sun, B., Zhang, Y., Meng, G.
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<strong>Gasdermin D drives the nonexosomal secretion of galectin-3, an insulin signal antagonist.</strong>
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