β-Synuclein exhibits chaperone activity more efficiently than α-synuclein

26Citations
Citations of this article
29Readers
Mendeley users who have this article in their library.

Abstract

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. © 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Lee, D., Paik, S. R., & Choi, K. Y. (2004). β-Synuclein exhibits chaperone activity more efficiently than α-synuclein. FEBS Letters, 576(1–2), 256–260. https://doi.org/10.1016/j.febslet.2004.08.075

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free