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><journal-meta><journal-id journal-id-type="nlm-ta">Commun Integr Biol</journal-id><journal-id journal-id-type="iso-abbrev">Commun Integr Biol</journal-id><journal-id journal-id-type="publisher-id">CIB</journal-id><journal-title-group><journal-title>Communicative & Integrative Biology</journal-title></journal-title-group><issn pub-type="epub">1942-0889</issn><publisher><publisher-name>Landes Bioscience</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22482021</article-id><article-id pub-id-type="pmc">3291325</article-id><article-id pub-id-type="publisher-id">2011CIB0185</article-id><article-id pub-id-type="pii">18483</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article Addendum</subject></subj-group></article-categories><title-group><article-title>The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson’s disease</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Pemberton</surname><given-names>Samantha</given-names></name></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Melki</surname><given-names>Ronald</given-names></name></contrib><aff>Laboratoire d’Enzymologie et Biochimie Structurales; CNRS; Gif-sur-Yvette, France</aff></contrib-group><author-notes><corresp>Correspondence to: Ronald Melki; Email: <email>Ronald.Melki@lebs.cnrs-gif.fr</email></corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>1</month><year>2012</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<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></permissions><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></abstract><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></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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