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P1‐372: Regulation of the Hsp90 chaperone complex by HDAC6
Author(s) -
Cook Casey N.,
Dunmore Judy,
Gendron Tania,
Deture Michael,
Petrucelli Leonard
Publication year - 2010
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2010.05.926
Subject(s) - hsp90 , hdac6 , chaperone (clinical) , microbiology and biotechnology , acetylation , tauopathy , downregulation and upregulation , gene knockdown , transfection , biology , chemistry , biochemistry , cell culture , heat shock protein , histone , histone deacetylase , neurodegeneration , genetics , medicine , disease , gene , pathology
higher molecular weight under non-reducing condition of SDS-PAGE. Immunogold electron microscopical analysis showed that the soluble 64 kDa tau fraction contained tau-positive granules and short filaments. Conclusions: Cytosplasmic hyperphosphorylated tau species that differ from either normal soluble tau or sarkosyl insoluble tau are pre-aggregation conformers and may play an important role in tau pathogenesis in rTg4510 mouse.