The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson’s disease
Identifieur interne : 000324 ( Pmc/Corpus ); précédent : 000323; suivant : 000325The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson’s disease
Auteurs : Samantha Pemberton ; Ronald MelkiSource :
- Communicative & Integrative Biology [ 1942-0889 ] ; 2012.
Abstract
We recently described the effect of the constitutively expressed chaperone, Hsc70 protein, on α‑Synuclein aggregation, a phenomenon associated with Parkinson disease. In vitro, Hsc70 binds to soluble α‑Syn and slows down its assembly into fibrils. Hsc70 also binds fibrillar α‑Syn, 5-fold tighter than soluble α‑Syn. This interaction reduces the cytotoxicity associated with naked α‑Syn fibrils. Herein, we discuss the feasibility of engineering a “minichaperone” which could be used against α‑Syn assembly propagation in Parkinson disease: taking what is necessary and sufficient within Hsc70 to protect against the damaging repercussions of high molecular weight α‑Syn species’ passage from one neuron to another in the brain.
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PubMed: 22482021
PubMed Central: 3291325
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<front><div type="abstract" xml:lang="en"><p>We recently described the effect of the constitutively expressed chaperone, Hsc70 protein, on α‑Synuclein aggregation, a phenomenon associated with Parkinson disease. In vitro, Hsc70 binds to soluble α‑Syn and slows down its assembly into fibrils. Hsc70 also binds fibrillar α‑Syn, 5-fold tighter than soluble α‑Syn. This interaction reduces the cytotoxicity associated with naked α‑Syn fibrils. Herein, we discuss the feasibility of engineering a “minichaperone” which could be used against α‑Syn assembly propagation in Parkinson disease: taking what is necessary and sufficient within Hsc70 to protect against the damaging repercussions of high molecular weight α‑Syn species’ passage from one neuron to another in the brain.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Commun Integr Biol</journal-id>
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<title-group><article-title>The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson’s disease</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Pemberton</surname>
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<contrib contrib-type="author" corresp="yes"><name><surname>Melki</surname>
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<aff>Laboratoire d’Enzymologie et Biochimie Structurales; CNRS; Gif-sur-Yvette, France</aff>
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<author-notes><corresp>Correspondence to: Ronald Melki; Email: <email>Ronald.Melki@lebs.cnrs-gif.fr</email>
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<volume>5</volume>
<issue>1</issue>
<fpage>94</fpage>
<lpage>95</lpage>
<permissions><copyright-statement>Copyright © 2012 Landes Bioscience</copyright-statement>
<copyright-year>2012</copyright-year>
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<abstract><p>We recently described the effect of the constitutively expressed chaperone, Hsc70 protein, on α‑Synuclein aggregation, a phenomenon associated with Parkinson disease. In vitro, Hsc70 binds to soluble α‑Syn and slows down its assembly into fibrils. Hsc70 also binds fibrillar α‑Syn, 5-fold tighter than soluble α‑Syn. This interaction reduces the cytotoxicity associated with naked α‑Syn fibrils. Herein, we discuss the feasibility of engineering a “minichaperone” which could be used against α‑Syn assembly propagation in Parkinson disease: taking what is necessary and sufficient within Hsc70 to protect against the damaging repercussions of high molecular weight α‑Syn species’ passage from one neuron to another in the brain.</p>
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<kwd-group kwd-group-type="author"><title>Keywords: </title>
<kwd>alpha synuclein</kwd>
<kwd>chaperones</kwd>
<kwd>heat shock protein</kwd>
<kwd>Hsc70</kwd>
<kwd>Parkinson’s disease</kwd>
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