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Interplay between glycogen synthase kinase‐3β and tau in the cerebellum of Hsp27 transgenic mouse
Author(s) -
Wang Shan,
Toth Melinda Erzsebet,
Bereczki Erika,
Santha Miklos,
Guan ZhiZhong,
Winblad Bengt,
Pei JinJing
Publication year - 2011
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.22660
Subject(s) - gsk 3 , protein phosphatase 2 , glycogen synthase , phosphorylation , gsk3b , hsp27 , cerebellum , transgene , phosphatase , biology , genetically modified mouse , dephosphorylation , protein kinase a , ribosomal s6 kinase , microbiology and biotechnology , heat shock protein , chemistry , biochemistry , protein kinase b , hsp70 , endocrinology , p70 s6 kinase 1 , gene
The association between heat shock protein 27 (Hsp27) and hyperphosphorylated tau has gained attention for more than a decade, but it has never been explored in vivo. In the present study, we found that tau phosphorylated at S396/404 (PHF‐1) and S262 sites was significantly increased in the cerebellum of Hsp27 transgenic mice, which was concomitant with increased glycogen synthase kinase‐3β (GSK3β) phosphorylated at Y216 and decreased GSK3β phosphorylated at S9. Neither 70‐kDa ribosomal protein S6 kinase (p70S6K; total p70S6K, p70S6K at T389, and p70S6K at T421/S424) nor protein phosphatase PP2A (total PP2A, PP2A at Y307, methylated or demethylated PP2A) was changed. This suggests that the increased tau phosphorylation at S396/404 and S262 sites may be induced by Hsp27 through enhancement of GSK3β activity in the mouse cerebellum. © 2011 Wiley‐Liss, Inc.