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Interplay between glycogen synthase kinase-3β and tau in the cerebellum of Hsp27 transgenic mouse

✍ Scribed by Shan Wang; Melinda Erzsebet Toth; Erika Bereczki; Miklos Santha; Zhi-Zhong Guan; Bengt Winblad; Jin-Jing Pei

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
723 KB
Volume
89
Category
Article
ISSN
0360-4012

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✦ Synopsis

Abstract

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.

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