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β‐Synuclein exhibits chaperone activity more efficiently than α‐synuclein
Author(s) -
Lee Daekyun,
Paik Seung R.,
Choi Kwan Yong
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.075
Subject(s) - chaperone (clinical) , chemistry , alpha synuclein , biophysics , microbiology and biotechnology , biology , parkinson's disease , medicine , disease , pathology
β‐Synuclein exhibits high sequence homology and structural similarity with α‐synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of β‐synuclein and its anti‐fibrillar activity in comparison with α‐synuclein. β‐Synuclein suppressed the heat‐induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti‐aggregative activity was remarkably higher than that of α‐synuclein. Heat‐induced inactivation of citrate synthase was significantly protected by β‐synuclein. Moreover, β‐synuclein inhibited the amyloid formation of both Aβ 1–40 and α‐synuclein. It is, therefore, suggested that β‐synuclein can prevent abnormal protein aggregations more effectively than α‐synuclein by acting as a molecular chaperone.