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Chaperone‐like activity of synucleins
Author(s) -
Souza José M.,
Giasson Benoit I.,
Lee Virginia M.-Y.,
Ischiropoulos Harry
Publication year - 2000
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(00)01563-5
Subject(s) - chaperone (clinical) , chemistry , mutant , alpha synuclein , synuclein , biochemistry , microbiology and biotechnology , protein aggregation , biophysics , biology , medicine , disease , parkinson's disease , pathology , gene
Synucleins are a family of small proteins that are predominantly expressed in neurons. The functions of the synucleins are not entirely understood, but they have been implicated in the pathogenesis of several neurodegenerative diseases. Our data show that α‐, β‐ or γ‐synuclein suppresses the aggregation of thermally denatured alcohol dehydrogenase and chemically denatured insulin. The A53T but not the A30P mutant α‐synuclein was able to inhibit the aggregation of insulin and the chaperone‐like activity of α‐synuclein was lost upon removal of its C‐terminal residues 98–140. These results demonstrate that synucleins with the exception of the A30P mutant possess chaperone‐like activity.