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<p class="publishdate"><span property="dc:date" datatype="xsd:dateTime" content="2016-07-26T00:00:00-04:00" class="date-display-single">July 26, 2016</span></p><div class='syndicate'><h1>Molecule may impact Gaucher, Parkinson’s disease </h1><div class="callout callout-with-border"><h3>At a Glance</h3>
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<li>Scientists identified a molecule that restores the activity of a dysfunctional enzyme tied to both Gaucher disease and Parkinson’s disease.</li>
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<li>These findings suggest a new avenue to explore for treating these disorders.</li>
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<picture title="Small molecule, NCGC607">
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<!--[if IE 9]><video style="display: none;"><![endif]-->
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-large/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=NBjMsnVX&timestamp=1469559995 1x" media="screen and (min-width: 960px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=TLPqRvdB&timestamp=1469559995 1x" media="screen and (min-width: 800px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium-small/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=3QFhaAS3&timestamp=1469559995 1x" media="screen and (min-width: 600px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-small/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=TISgM2ol&timestamp=1469559995 1x" media="screen and (min-width: 480px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-tiny/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=SSowWCYL&timestamp=1469559995 1x" media="screen and (min-width: 0)" />
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<!--[if IE 9]></video><![endif]-->
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<img src="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2016/20160726-gaucher.jpg?itok=TLPqRvdB&timestamp=1469559995" alt="Small molecule, NCGC607" title="Small molecule, NCGC607" />
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||
</picture><span class="caption">The small molecule, NCGC607, can chaperone the dysfunctional enzyme, glucocerebrosidase, into lysosomes (yellow) and restore the enzyme's ability to break down a fatty substance in nerve cells.</span><span class="credit">Darryl Leja, NHGRI</span></div>
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</div><p>Gaucher disease is an inheritable metabolic disorder caused by a malfunctioning enzyme, called glucocerebrosidase, that’s needed to break down, or metabolize, a specific fatty material. Over time, harmful amounts of this substance can accumulate in various cells and tissues in the body. This can damage a person’s bones, liver, and spleen. Children with type 2 Gaucher disease can also have extensive damage to the brain, whereas those with type 1 do not.</p>
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<p>Gaucher disease occurs when a person inherits 2 defective copies of the <em>GBA </em>gene, which codes for glucocerebrosidase. People with even one mutation in <em>GBA</em> also have a higher risk of developing Parkinson’s disease—a disorder characterized by tremors, muscular rigidity, and slowed movements. People with Parkinson’s disease lose the cells involved in movement (dopamine neurons) and accumulate a protein called alpha-synuclein in their brains.</p>
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<p>To better understand the dysfunctional enzyme’s role in Parkinson’s disease, a team led by Dr. Ellen Sidransky at NIH’s National Human Genome Research Institute (NHGRI) compared cells from patients who have Gaucher disease, with and without Parkinson’s disease, and healthy adults. The researchers converted skin cells into dopamine neurons. They then evaluated the enzyme’s activity and the levels of the fatty material and alpha-synuclein. Results were published on July 13, 2016, in the <em>Journal of Neuroscience</em>.</p>
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||
<p>Neurons from patients with type 1 Gaucher disease who also have Parkinson’s disease and those with type 2 Gaucher disease showed reduced enzyme activity and increased levels of alpha-synuclein and the fatty material compared with healthy adult cells. Neurons from patients with type 1 Gaucher disease without Parkinson’s disease showed similar results, but lacked alpha-synuclein accumulation.</p>
|
||
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||
<p>The team next tested a small “chaperone” molecule called NCGC607 on the neurons. The molecule, which they had identified in previous work, improves the activity of glucocerebrosidase. The chaperone restored the enzyme’s ability to gain entry into lysosomes—the cell compartment where fatty materials are broken down—and increased enzyme activity. After treatment, dopamine neurons from patients with type 2 and type 1 Gaucher disease with Parkinson’s disease also showed less buildup of the fatty material and alpha-synuclein. These findings suggest that using a molecular chaperone to aid the dysfunctional enzyme may be a useful strategy for treating both diseases.</p>
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||
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<p>“This research demonstrates how insights from a rare disorder such as Gaucher disease can have direct relevance to the treatment of common disorders like Parkinson’s disease,” says NHGRI scientific director Dr. Daniel Kastner. More research is needed to determine whether using such a small molecule could be useful for treating either disease.</p></div><h2 class="label-above">Related Links</h2><ul class="spaced print-urls"><li><a href="https://www.nih.gov/news-events/nih-research-matters/rare-disease-gene-linked-parkinsons-disease" target="_top">Rare Disease Gene Linked to Parkinson’s Disease</a></li><li><a href="https://newsinhealth.nih.gov/issue/nov2014/feature2" target="_top">Parkinson’s Disease: Understanding a Complicated Condition</a></li><li><a href="https://www.genome.gov/25521505/" target="_top">Learning About Gaucher Disease</a></li><li><a href="http://www.ninds.nih.gov/disorders/gauchers/gauchers.htm" target="_top">Gaucher Disease</a></li><li><a href="http://www.ninds.nih.gov/disorders/lipid_storage_diseases/detail_lipid_storage_diseases.htm" target="_top">Lipid Storage Diseases Fact Sheet</a></li><li><a href="https://www.genome.gov/10001217/" target="_top">Learning About Parkinson's Disease</a></li><li><a href="http://www.niehs.nih.gov/health/topics/conditions/parkinson/index.cfm" target="_top">Parkinson’s Disease </a></li><li><a href="http://nihseniorhealth.gov/parkinsonsdisease/whatisparkinsonsdisease/01.html" target="_top">What Is Parkinson's Disease?</a></li></ul><p class="footnote"><strong class="label-inline">References: </strong><a href="http://www.ncbi.nlm.nih.gov/pubmed/27413154">A New Glucocerebrosidase Chaperone Reduces α-Synuclein and Glycolipid Levels in iPSC-Derived Dopaminergic Neurons from Patients with Gaucher Disease and Parkinsonism. </a>Aflaki E, Borger DK, Moaven N, Stubblefield BK, Rogers SA, Patnaik S, Schoenen FJ, Westbroek W, Zheng W, Sullivan P, Fujiwara H, Sidhu R, Khaliq ZM, Lopez GJ, Goldstein DS, Ory DS, Marugan J, Sidransky E. <em>J Neurosci.</em> 2016 Jul 13;36(28):7441-52. doi: 10.1523/JNEUROSCI.0636-16.2016. PMID: 27413154.</p><p class="footnote"><strong class="label-inline">Funding: </strong>NIH’s National Human Genome Research Institute (NHGRI), National Institute of Neurological Disorders and Stroke (NINDS), and National Center for Advancing Translational Sciences (NCATS).</p>
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<p><a href="https://www.nih.gov/news-events/nih-research-matters/research-context-can-we-slow-aging">Research in Context: Can we slow aging?</a></p>
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<p><a href="https://www.nih.gov/news-events/nih-research-matters/brain-changes-observed-during-pregnancy">Brain changes observed during pregnancy</a></p>
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<p><a href="https://www.nih.gov/news-events/nih-research-matters/risk-future-burden-dementia-united-states">Risk and future burden of dementia in the United States </a></p>
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<p><a href="https://www.nih.gov/news-events/nih-research-matters/complete-wiring-map-adult-fruit-fly-brain">Complete wiring map of an adult fruit fly brain</a></p>
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<p><strong>Editor:</strong> Harrison Wein, Ph.D.</p>
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<p><strong>Assistant Editors:</strong> Vicki Contie and Brian Doctrow, Ph.D.</p>
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<p><strong><em>NIH Research Matters </em></strong>is a weekly update of NIH research highlights reviewed by NIH’s experts. It's published by the <a href="/institutes-nih/nih-office-director/office-communications-public-liaison">Office of Communications and Public Liaison</a> in the <a href="/institutes-nih/nih-office-director">NIH Office of the Director</a>.</p>
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