beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein
SCIE
SCOPUS
- Title
- beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein
- Authors
- Lee, D; Paik, SR; Choi, KY
- Date Issued
- 2004-10-08
- Publisher
- ELSEVIER SCIENCE BV
- Abstract
- beta-Synuclein exhibits high sequence homology and structural similarity with alpha-synuclein, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of beta-synuclein and its anti-fibrillar activity in comparison with alpha-synuclein. beta-Synuclein suppressed the heat-induced aggregation of aldolase, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of alpha-synuclein. Heat-induced inactivation of citrate synthase was significantly protected by beta-synuclein. Moreover, beta-synuclein inhibited the amyloid formation of both Abeta(1-40) and alpha-synuclein. It is, therefore, suggested that beta-synuclein can prevent abnormal protein aggregations more effectively than alpha-synuclein by acting as a molecular chaperone. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
- Keywords
- beta-synuclein; chaperone activity; protein aggregation; fibril formation; PARKINSONS-DISEASE; NEURODEGENERATIVE DISORDERS; SYNTHETIC MEMBRANES; LEWY BODY; MICE; GENE; IDENTIFICATION; EXPRESSION; MUTATION; PROTEIN
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/17652
- DOI
- 10.1016/J.FEBSLET.2004.08.075
- ISSN
- 0014-5793
- Article Type
- Article
- Citation
- FEBS LETTERS, vol. 576, no. 1-2, page. 256 - 260, 2004-10-08
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.