The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson’s disease
Identifieur interne : 000E87 ( Ncbi/Checkpoint ); précédent : 000E86; suivant : 000E88The 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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