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Oxidized glutathione stimulated the amyloid formation of α‐synuclein
Author(s) -
Paik Seung R.,
Lee Daekyun,
Cho Hyun-Ju,
Lee Eui-Nam,
Chang Chung-Soon
Publication year - 2003
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/s0014-5793(03)00081-4
Subject(s) - glutathione , chemistry , oxidative stress , amyloid (mycology) , kinetics , alpha synuclein , dissociation (chemistry) , stimulation , pathogenesis , biochemistry , biophysics , endocrinology , parkinson's disease , medicine , biology , enzyme , disease , inorganic chemistry , physics , quantum mechanics
α‐Synuclein is the major filamentous constituent of Lewy bodies found in Parkinson's disease (PD). The amyloid formation of α‐synuclein was significantly facilitated by oxidized glutathione (GSSG) as the lag period of the aggregation kinetics was shortened by 2.5‐fold from its absence. Reduced glutathione (GSH), on the other hand, did not influence the lag phase although it increased the final amyloid formation. The GSSG stimulation was specific for not only α‐synuclein but also its intactness. The preferred GSSG interaction of α‐synuclein to GSH was also demonstrated with dissociation constants of 0.53 and 43.5 mM, respectively. It is suggested that the oxidative stress favoring the GSSG generation from GSH could result in the augmented amyloid formation of α‐synuclein, which ought to be related to the pathogenesis of PD.