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<script type="text/javascript" src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.boots.min.js"> </script><title>99mTc-Labeled cysteine-tagged dimeric epidermal growth factor - Molecular Imaging and Contrast Agent Database (MICAD) - NCBI Bookshelf</title>
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<meta name="citation_inbook_title" content="Molecular Imaging and Contrast Agent Database (MICAD) [Internet]">
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<meta name="citation_title" content="99mTc-Labeled cysteine-tagged dimeric epidermal growth factor">
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<meta name="citation_date" content="2009/07/15">
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<meta name="citation_author" content="Arvind Chopra">
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<meta name="DC.Title" content="99mTc-Labeled cysteine-tagged dimeric epidermal growth factor">
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<meta name="DC.Contributor" content="Arvind Chopra">
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<meta name="description" content="Growth factors such as the epidermal growth factor (EGF), the vascular endothelial growth factor (VEGF), and the tumor necrosis factor are known to have important roles in the development and progression of cancers (1-3). The EGF mediates its activity through a group of tyrosine kinase (TK)–dependent EGF receptors (EGFR) that promote not only cell proliferation but also cell survival and the motility phenotype that is necessary for the development of an invasive cancer (4). As a consequence, the EGFRs and their associated TKs are the targets of several anti-EGFR antibodies and TK inhibitors that are either approved by the United States Food and Drug Administration or are being evaluated in clinical trials for the treatment of various neoplasms. Before treatment, the patients are screened to determine the extent of EGFR expression in the tumors with the use of immunohistochemistry (IHC) or fluorescence in situ hybridization (FISH) because these techniques help predict the probable therapeutic response and outcome for the individual (5, 6). However, only 10–25% of the patients who are EGFR-positive according to IHC or FISH analysis respond to the anti-EGFR therapy, which indicates that a poor correlation exists between the EGFR expression analysis and the treatment (7, 8). This is probably because only the active receptors are important to predict the efficacy of the anti-EGFR agents for the treatment of cancers, and ICH and FISH do not distinguish between the active and inactive EGFRs (9).">
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<meta name="og:description" content="Growth factors such as the epidermal growth factor (EGF), the vascular endothelial growth factor (VEGF), and the tumor necrosis factor are known to have important roles in the development and progression of cancers (1-3). The EGF mediates its activity through a group of tyrosine kinase (TK)–dependent EGF receptors (EGFR) that promote not only cell proliferation but also cell survival and the motility phenotype that is necessary for the development of an invasive cancer (4). As a consequence, the EGFRs and their associated TKs are the targets of several anti-EGFR antibodies and TK inhibitors that are either approved by the United States Food and Drug Administration or are being evaluated in clinical trials for the treatment of various neoplasms. Before treatment, the patients are screened to determine the extent of EGFR expression in the tumors with the use of immunohistochemistry (IHC) or fluorescence in situ hybridization (FISH) because these techniques help predict the probable therapeutic response and outcome for the individual (5, 6). However, only 10–25% of the patients who are EGFR-positive according to IHC or FISH analysis respond to the anti-EGFR therapy, which indicates that a poor correlation exists between the EGFR expression analysis and the treatment (7, 8). This is probably because only the active receptors are important to predict the efficacy of the anti-EGFR agents for the treatment of cancers, and ICH and FISH do not distinguish between the active and inactive EGFRs (9).">
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id="jr-fip-info-p"><a id="jr-fip-prev" class="wsprkl btn" title="Jump to previuos match">◀</a><button id="jr-fip-matches">no matches yet</button><a id="jr-fip-next" class="wsprkl btn" title="Jump to next match">▶</a></nav></nav></div><div id="jr-epub-interstitial" class="hidden"></div><div id="jr-content"><article data-type="main"><div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><div class="fm-sec"><h1 id="_NBK23369_"><span class="title" itemprop="name"><sup>99m</sup>Tc-Labeled cysteine-tagged dimeric epidermal growth factor</span></h1><div itemprop="alternativeHeadline" class="subtitle whole_rhythm">[<sup>99m</sup>Tc]Cys-dEGF</div><p class="contribs">Chopra A.</p><p class="fm-aai"><a href="#_NBK23369_pubdet_">Publication Details</a></p></div></div><div class="jig-ncbiinpagenav body-content whole_rhythm" data-jigconfig="allHeadingLevels: ['h2'],smoothScroll: false" itemprop="text"><div class="iconblock whole_rhythm clearfix ten_col table-wrap" id="figCysdEGF99mTcT1"><a href="/books/NBK23369/table/CysdEGF99mTc.T1/?report=objectonly" target="object" title="Table" class="img_link icnblk_img figpopup" rid-figpopup="figCysdEGF99mTcT1" rid-ob="figobCysdEGF99mTcT1"><img class="small-thumb" src="/books/NBK23369/table/CysdEGF99mTc.T1/?report=thumb" src-large="/books/NBK23369/table/CysdEGF99mTc.T1/?report=previmg" alt="Image " /></a><div class="icnblk_cntnt"><h4 id="CysdEGF99mTc.T1"><a href="/books/NBK23369/table/CysdEGF99mTc.T1/?report=objectonly" target="object" rid-ob="figobCysdEGF99mTcT1">Table</a></h4><p class="float-caption no_bottom_margin">
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<i>In vitro</i>
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Rodents
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</p></div></div><div id="CysdEGF99mTc.Background"><h2 id="_CysdEGF99mTc_Background_">Background</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=role+of+growth+factors+in+cancer" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Growth factors such as the epidermal growth factor (EGF), the vascular endothelial growth factor (VEGF), and the tumor necrosis factor are known to have important roles in the development and progression of cancers (<a class="bibr" href="#CysdEGF99mTc.REF.1" rid="CysdEGF99mTc.REF.1 CysdEGF99mTc.REF.2 CysdEGF99mTc.REF.3">1-3</a>). The EGF mediates its activity through a group of tyrosine kinase (TK)–dependent EGF receptors (EGFR) that promote not only cell proliferation but also cell survival and the motility phenotype that is necessary for the development of an invasive cancer (<a class="bibr" href="#CysdEGF99mTc.REF.4" rid="CysdEGF99mTc.REF.4">4</a>). As a consequence, the EGFRs and their associated TKs are the targets of several <a href="http://clinicaltrials.gov/ct2/results?term=anti-EGFR+antibodies" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">anti-EGFR antibodies</a> and <a href="http://clinicaltrials.gov/ct2/results?term=EGFR+tyrosine+kinase+inhibitors" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">TK inhibitors</a> that are either approved by the United States Food and Drug Administration or are being evaluated in clinical trials for the treatment of various neoplasms. Before treatment, the patients are screened to determine the extent of EGFR expression in the tumors with the use of immunohistochemistry (IHC) or fluorescence <i>in situ</i> hybridization (FISH) because these techniques help predict the probable therapeutic response and outcome for the individual (<a class="bibr" href="#CysdEGF99mTc.REF.5" rid="CysdEGF99mTc.REF.5 CysdEGF99mTc.REF.6">5, 6</a>). However, only 10–25% of the patients who are EGFR-positive according to IHC or FISH analysis respond to the anti-EGFR therapy, which indicates that a poor correlation exists between the EGFR expression analysis and the treatment (<a class="bibr" href="#CysdEGF99mTc.REF.7" rid="CysdEGF99mTc.REF.7 CysdEGF99mTc.REF.8">7, 8</a>). This is probably because only the active receptors are important to predict the efficacy of the anti-EGFR agents for the treatment of cancers, and ICH and FISH do not distinguish between the active and inactive EGFRs (<a class="bibr" href="#CysdEGF99mTc.REF.9" rid="CysdEGF99mTc.REF.9">9</a>).</p><p>On binding the ligand, a characteristic feature of a functional EGFR is that it is internalized by the cell. Levashova et al. (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>) envisioned that perhaps the natural ligand EGF itself could be used as an imaging agent to detect the active EGFRs in tumors. The investigators used an <i>Escherichia coli</i> (<i>E. coli</i>)–expressed dimeric EGF (dEGF) molecule in which the second EGF molecule is linked to the first through a linker of 9 amino acids, with the first EGF molecule having an N-terminal cysteine fusion tag (Cys-EGF) of 15 amino acids that could be used to conjugate therapeutic or imaging probes as done earlier with VEGF (<a class="bibr" href="#CysdEGF99mTc.REF.11" rid="CysdEGF99mTc.REF.11">11</a>). In addition, the investigators also expressed EGF containing an N-terminal cysteine fusion tag (<a class="bibr" href="#CysdEGF99mTc.REF.11" rid="CysdEGF99mTc.REF.11">11</a>). The dEGF and the EGF were then respectively labeled with radioactive technetium (<sup>99m</sup>Tc) to obtain [<sup>99m</sup>Tc]Cys-dEGF and [<sup>99m</sup>Tc]Cys-EGF. The biodistribution and imaging characteristics of the two molecules were subsequently investigated in xenograft tumor-bearing mice. It is pertinent to mention here that the imaging and biodistribution studies of only [<sup>99m</sup>Tc]Cys-dEGF are described in this chapter. Investigations performed with [<sup>99m</sup>Tc]Cys-EGF are described separately in MICAD (<a href="http://www.micad.nih.gov" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">www.micad.nih.gov</a>).</p></div><div id="CysdEGF99mTc.Synthesis"><h2 id="_CysdEGF99mTc_Synthesis_">Synthesis</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=Cys-tagged+EGF+synthesis" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>The Cys-dEGF was expressed in and purified from <i>E. coli</i> as described elsewhere to obtain Cys-tagged single-chain VEGF (Cys-scVEGF) (<a class="bibr" href="#CysdEGF99mTc.REF.12" rid="CysdEGF99mTc.REF.12">12</a>). To label purified Cys-dEGF with <sup>99m</sup>Tc, the protein was first incubated with an equimolar amount of dithiothreitol for 20 min at 25°C in 0.1 M Tris-HCl buffer (pH 8.0) to reduce all the sulfhydryl groups in the tagged protein (<a class="bibr" href="#CysdEGF99mTc.REF.11" rid="CysdEGF99mTc.REF.11 CysdEGF99mTc.REF.12">11, 12</a>). The reduced protein was then labeled with <sup>99m</sup>Tc as detailed for Cys-scVEGF (<a class="bibr" href="#CysdEGF99mTc.REF.11" rid="CysdEGF99mTc.REF.11">11</a>). The radiolabeled Cys-dEGF (dEGF/Tc) was purified with size-exclusion chromatography using a PD-10 column, and the average yield of the labeled product was 45 ± 13% (<i>n</i> = 13 labeling reactions) as determined by the amount of <sup>99m</sup>Tc eluting from the column (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). The radiochemical purity of dEGF/Tc was 90–95% as determined with instant thin-layer chromatography (ITLC) (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). The Rf value for the labeled protein on ITLC was not reported. Specific activity of dEGF/Tc was reported to be 5.92–10.36 MBq/70 fmol (0.13–0.28 mCi/70 fmol) (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>).</p><p>To investigate the stability of dEGF/Tc, the labeled protein was injected into mice (<i>n</i> = 2 animals), and then the animals were euthanized 2 min later (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). Blood from the mice was collected and centrifuged to obtain plasma. The plasma was then incubated for 10, 20, and 75 min at 37°C, and the protein-bound radioactivity was determined with ITLC. The radioactivity was reported to be associated with the plasma protein fraction for at least 75 min under these conditions. Stability of dEGF/Tc was also investigated under <i>in vitro</i> conditions by incubating the labeled protein in phosphate-buffered saline (PBS) for up to 3 h at room temperature followed by ITLC and polyacrylamide gel analysis under denaturing conditions. dEGF/Tc was reported to be stable in PBS at room temperature for at least 3 h.</p></div><div id="CysdEGF99mTc.In_Vitro_Studies_Tes"><h2 id="_CysdEGF99mTc_In_Vitro_Studies_Tes_"><i>In Vitro</i> Studies: Testing in Cells and Tissues</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=99mTc+Cys-EGF+in+vitro" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>In another study, Cys-EGF was reported to induce EGFR TK phosphorylation in F98/EGFR(F) cells (rat glioma cells transfected with the human EGFR gene) in a dose-dependent manner (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). Cys-dEGF was also reported to compete with an EGF-Shiga-like toxin subunit A conjugate (<a href="http://www.sibtech.com/?p=targeted_toxins" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">EGF-SLT</a>) for binding to the EGFR (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). EGF-SLT is extremely toxic to MDA23 1luc human breast cancer cells, and the ability of proteins to compete for binding with the EGFR was measured by counting the number of cells surviving after a 72-h exposure to EGF-SLT (1 nM) in the presence of an increasing concentration of Cys-EGF (0–25 nM). It was reported that cell survival increased with an increasing Cys-dEGF concentration under these experimental conditions, which indicates that Cys-dEGF protected the cells from EGF-SLT toxicity.</p></div><div id="CysdEGF99mTc.Animal_Studies"><h2 id="_CysdEGF99mTc_Animal_Studies_">Animal Studies</h2><div id="CysdEGF99mTc.Rodents"><h3>Rodents</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=99m+Tc+Cys+EGF+rodentia" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>Levashova et al. studied the blood clearance and biodistribution of dEGF/Tc in mice (<i>n</i> = 4 animals) bearing MDA23 1luc cell tumors (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). The animals were injected with the radiotracer, and blood was collected at preselected time points for up to 60 min. More than 95% of the radioactivity was reported to clear from blood within 60 min. To determine biodistribution of the labeled protein, the animals were euthanized 3 h after administration of the tracer, all the major organs and the tumors were harvested, and radioactivity incorporated in the harvested organs was counted using a gamma counter. The radioactivity was reported to have accumulated primarily in the liver (24.5 ± 7.4% injected dose/gram tissue (% ID/g)) and kidneys (45.5 ± 1.4% ID/g). Compared with [<sup>99m</sup>Tc]Cys-EGF, both organs were reported to accumulate a higher amount of dEGF/Tc. Also, the outer edges and the center of each tumor were reported to have a similar accumulation of radioactivity after the dEGF/Tc treatment, indicating that the tracer was distributed throughout the tumor mass. No blocking studies were reported.</p><p>The accumulation of dEGF/Tc was investigated in mice bearing either orthotopic MDA23 1luc cell tumors or spontaneous lung carcinoma (<a class="bibr" href="#CysdEGF99mTc.REF.10" rid="CysdEGF99mTc.REF.10">10</a>). The animals (<i>n</i> = 4 mice per model) were injected with the radiolabeled protein and imaged 1 h later with single-photon emission computed tomography (SPECT). Compared with the surrounding normal tissue, accumulation of radioactivity in the tumors was reported to be clearly evident in both tumor types. No blocking studies were reported.</p><p>Autoradiography of cryosections prepared from the MDA23 1luc tumors (<i>n</i> = 2 animals) immediately after SPECT imaging confirmed that accumulated radioactivity after the dEGF/Tc treatment was significantly higher in the tumors than in the normal muscle tissue. No blocking studies were reported.</p></div><div id="CysdEGF99mTc.Other_NonPrimate_Mam"><h3>Other Non-Primate Mammals</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=99m+Tc+Cys+EGF+Non-Primate+Mammals" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div><div id="CysdEGF99mTc.NonHuman_Primates"><h3>Non-Human Primates</h3><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=99m+Tc+Cys+EGF+Non-Human+Primates" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div></div><div id="CysdEGF99mTc.Human_Studies"><h2 id="_CysdEGF99mTc_Human_Studies_">Human Studies</h2><p>[<a href="/sites/entrez?Db=pubmed&Cmd=DetailsSearch&Term=99m+Tc+Cys+EGF+Human+Studies" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">PubMed</a>]</p><p>No references are currently available.</p></div><div id="CysdEGF99mTc.Supplemental_Informa"><h2 id="_CysdEGF99mTc_Supplemental_Informa_">Supplemental Information</h2><p>[<a href="/books/n/micad/disclaimer/?report=reader">Disclaimers</a>]</p><p>No information is currently available.</p></div><div id="CysdEGF99mTc.References"><h2 id="_CysdEGF99mTc_References_">References</h2><dl class="temp-labeled-list"><dl class="bkr_refwrap"><dt>1.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.1">Wu W.K., Tse T.T., Sung J.J., Li Z.J., Yu L., Cho C.H.
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<em>Expression of ErbB receptors and their cognate ligands in gastric and colon cancer cell lines.</em>
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<span><span class="ref-journal">Anticancer Res. </span>2009;<span class="ref-vol">29</span>(1):229–34.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19331154" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19331154</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>2.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.2">Schoenleber S.J., Kurtz D.M., Talwalkar J.A., Roberts L.R., Gores G.J.
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<em>Prognostic role of vascular endothelial growth factor in hepatocellular carcinoma: systematic review and meta-analysis.</em>
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<span><span class="ref-journal">Br J Cancer. </span>2009;<span class="ref-vol">100</span>(9):1385–92.</span> [<a href="/pmc/articles/PMC2694418/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2694418</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/19401698" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19401698</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>3.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.3">Balkwill F.
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<em>Tumour necrosis factor and cancer.</em>
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<span><span class="ref-journal">Nat Rev Cancer. </span>2009;<span class="ref-vol">9</span>(5):361–71.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19343034" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19343034</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>4.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.4">Wilkins-Port C.E., Ye Q., Mazurkiewicz J.E., Higgins P.J.
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<em>TGF-beta1 + EGF-initiated invasive potential in transformed human keratinocytes is coupled to a plasmin/MMP-10/MMP-1-dependent collagen remodeling axis: role for PAI-1.</em>
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<span><span class="ref-journal">Cancer Res. </span>2009;<span class="ref-vol">69</span>(9):4081–91.</span> [<a href="/pmc/articles/PMC2962982/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC2962982</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/19383899" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19383899</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>5.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.5">Baselga J., Arteaga C.L.
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<em>Critical update and emerging trends in epidermal growth factor receptor targeting in cancer.</em>
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<span><span class="ref-journal">J Clin Oncol. </span>2005;<span class="ref-vol">23</span>(11):2445–59.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15753456" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15753456</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>6.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.6">Varella-Garcia M., Mitsudomi T., Yatabe Y., Kosaka T., Nakajima E., Xavier A.C., Skokan M., Zeng C., Franklin W.A., Bunn P.A. Jr, Hirsch F.R.
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<em>EGFR and HER2 genomic gain in recurrent non-small cell lung cancer after surgery: impact on outcome to treatment with gefitinib and association with EGFR and KRAS mutations in a Japanese cohort.</em>
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<span><span class="ref-journal">J Thorac Oncol. </span>2009;<span class="ref-vol">4</span>(3):318–25.</span> [<a href="/pmc/articles/PMC3379811/" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pmc">PMC free article<span class="bk_prnt">: PMC3379811</span></a>] [<a href="https://pubmed.ncbi.nlm.nih.gov/19247083" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19247083</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>7.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.7">Chung K.Y., Shia J., Kemeny N.E., Shah M., Schwartz G.K., Tse A., Hamilton A., Pan D., Schrag D., Schwartz L., Klimstra D.S., Fridman D., Kelsen D.P., Saltz L.B.
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<em>Cetuximab shows activity in colorectal cancer patients with tumors that do not express the epidermal growth factor receptor by immunohistochemistry.</em>
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<span><span class="ref-journal">J Clin Oncol. </span>2005;<span class="ref-vol">23</span>(9):1803–10.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/15677699" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 15677699</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>8.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.8">Bell D.W., Lynch T.J., Haserlat S.M., Harris P.L., Okimoto R.A., Brannigan B.W., Sgroi D.C., Muir B., Riemenschneider M.J., Iacona R.B., Krebs A.D., Johnson D.H., Giaccone G., Herbst R.S., Manegold C., Fukuoka M., Kris M.G., Baselga J., Ochs J.S., Haber D.A.
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<em>Epidermal growth factor receptor mutations and gene amplification in non-small-cell lung cancer: molecular analysis of the IDEAL/INTACT gefitinib trials.</em>
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<span><span class="ref-journal">J Clin Oncol. </span>2005;<span class="ref-vol">23</span>(31):8081–92.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/16204011" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 16204011</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>9.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.9">Johns T.G., Perera R.M., Vernes S.C., Vitali A.A., Cao D.X., Cavenee W.K., Scott A.M., Furnari F.B.
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<em>The efficacy of epidermal growth factor receptor-specific antibodies against glioma xenografts is influenced by receptor levels, activation status, and heterodimerization.</em>
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<span><span class="ref-journal">Clin Cancer Res. </span>2007;<span class="ref-vol">13</span>(6):1911–25.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17363548" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17363548</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>10.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.10">Levashova Z., Backer M.V., Horng G., Felsher D., Backer J.M., Blankenberg F.G.
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<em>SPECT and PET imaging of EGF receptors with site-specifically labeled EGF and dimeric EGF.</em>
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<span><span class="ref-journal">Bioconjug Chem. </span>2009;<span class="ref-vol">20</span>(4):742–9.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/19320434" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 19320434</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>11.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.11">Levashova Z., Backer M., Backer J.M., Blankenberg F.G.
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<em>Direct site-specific labeling of the Cys-tag moiety in scVEGF with technetium 99m.</em>
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<span><span class="ref-journal">Bioconjug Chem. </span>2008;<span class="ref-vol">19</span>(5):1049–54.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/18407683" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 18407683</span></a>]</div></dd></dl><dl class="bkr_refwrap"><dt>12.</dt><dd><div class="bk_ref" id="CysdEGF99mTc.REF.12">Backer M.V., Levashova Z., Patel V., Jehning B.T., Claffey K., Blankenberg F.G., Backer J.M.
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<em>Molecular imaging of VEGF receptors in angiogenic vasculature with single-chain VEGF-based probes.</em>
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<span><span class="ref-journal">Nat Med. </span>2007;<span class="ref-vol">13</span>(4):504–9.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/17351626" ref="pagearea=cite-ref&targetsite=entrez&targetcat=link&targettype=pubmed">PubMed<span class="bk_prnt">: 17351626</span></a>]</div></dd></dl></dl></div><div id="bk_toc_contnr"></div></div></div><div class="fm-sec"><h2 id="_NBK23369_pubdet_">Publication Details</h2><h3>Author Information and Affiliations</h3><div class="contrib half_rhythm"><span itemprop="author">Arvind Chopra</span>, PhD<div class="affiliation small">National Center for Biotechnology Information, NLM, NIH, Bethesda, MD 20894<div><span class="email-label">Email: </span><a href="mailto:dev@null" data-email="vog.hin.mln.ibcn@dacim" class="oemail">vog.hin.mln.ibcn@dacim</a></div></div></div><h3>Publication History</h3><p class="small">Created: <span itemprop="datePublished">May 18, 2009</span>; Last Update: <span itemprop="dateModified">July 15, 2009</span>.</p><h3>Copyright</h3><div><div class="half_rhythm"><a href="/books/about/copyright/">Copyright Notice</a></div></div><h3>Publisher</h3><p><a href="http://www.ncbi.nlm.nih.gov/" ref="pagearea=page-banner&targetsite=external&targetcat=link&targettype=publisher">National Center for Biotechnology Information (US)</a>, Bethesda (MD)</p><h3>NLM Citation</h3><p>Chopra A. 99mTc-Labeled cysteine-tagged dimeric epidermal growth factor. 2009 May 18 [Updated 2009 Jul 15]. In: Molecular Imaging and Contrast Agent Database (MICAD) [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013. <span class="bk_cite_avail"></span></p></div><div class="small-screen-prev"><a href="/books/n/micad/Tc-citro-folate/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M75,30 c-80,60 -80,0 0,60 c-30,-60 -30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Prev</text></svg></a></div><div class="small-screen-next"><a href="/books/n/micad/CysEGF99mTc/?report=reader"><svg xmlns="http://www.w3.org/2000/svg" viewBox="0 0 100 100" preserveAspectRatio="none"><path d="M25,30c80,60 80,0 0,60 c30,-60 30,0 0,-60"></path><text x="20" y="28" textLength="60" style="font-size:25px">Next</text></svg></a></div></article><article data-type="table-wrap" id="figobCysdEGF99mTcT1"><div id="CysdEGF99mTc.T1" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK23369/table/CysdEGF99mTc.T1/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__CysdEGF99mTc.T1_lrgtbl__"><table><tbody><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Chemical name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"><sup>99m</sup>Tc-Labeled cysteine-tagged dimeric epidermal growth factor<br /></td><td rowspan="9" colspan="1" style="text-align:left;vertical-align:middle;"></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Abbreviated name:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">[<sup>99m</sup>Tc]Cys-dEGF</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Synonym:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"></td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Agent Category:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Ligand</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Target:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Epidermal growth factor receptor (EGFR)</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Target Category:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Receptor</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Method of detection:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Single-photon emission computed tomography (SPECT); planar imaging</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Source of signal / contrast:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;"><sup>99m</sup>Tc</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Activation:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">No</td></tr><tr><td rowspan="1" colspan="1" style="text-align:right;vertical-align:top;">
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<b>Studies:</b>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">
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<ul class="simple-list"><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" />
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<i>In vitro</i>
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</div></li><li class="half_rhythm"><div>
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<img alt="Checkbox" src="/corehtml/pmc/css/bookshelf/2.26/img/studies.checkbox.png" /> Rodents
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</div></li></ul>
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</td><td rowspan="1" colspan="1" style="text-align:left;vertical-align:top;">Click here for the <a href="/nuccore/166362727?report=genbank" ref="pagearea=body&targetsite=external&targetcat=link&targettype=uri">protein and nucleotide sequence</a> of human epidermal growth factor.</td></tr></tbody></table></div></div></article></div><div id="jr-scripts"><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/libs.min.js"> </script><script src="/corehtml/pmc/jatsreader/ptpmc_3.22/js/jr.min.js"> </script></div></div>
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