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Article

Distinct cleavage patterns of normal and pathologic forms of alpha-synuclein by calpain I in vitro.

Journal of neurochemistry - 1 Aug 2003

Mishizen-Eberz Amanda J, Guttmann Rodney P, Giasson Benoit I, Day George A, Hodara Roberto, Ischiropoulos Harry, Lee Virginia M-Y, Trojanowski John Q, Lynch David R

Abstract excerpt

Parkinson's disease (PD) is characterized by fibrillary neuronal inclusions called Lewy bodies (LBs) consisting largely of alpha-synuclein (alpha-syn), the protein mutated in some patients with familial PD. The mechanisms of alpha-syn fibrillization and LB formation are unknown, but may involve aberrant degradation or turnover. We examined the ability of calpain I to cleave alpha-syn in vitro. Calpain I cleaved...

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Identifiers

PMID: 12887682
DOI: 10.1046/j.1471-4159.2003.01878.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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