P3–298:  In vivo  efficacy of GSK3β inhibitors in the postnatal rat model of tau hyperphosphorylation | Zendy

Selenica Maj-Linda | Zendy; Lundbeck H. | Zendy

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P3–298: In vivo efficacy of GSK3β inhibitors in the postnatal rat model of tau hyperphosphorylation

Author(s) -

Selenica Maj-Linda,

Lundbeck H.

Publication year - 2006

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.2006.05.1567

Subject(s) - hyperphosphorylation , dentate gyrus , gsk 3 , hippocampus , western blot , in vivo , immunohistochemistry , tau protein , phosphorylation , blot , glycogen synthase , gsk3b , chemistry , endocrinology , medicine , cortex (anatomy) , alzheimer's disease , microbiology and biotechnology , pharmacology , biology , neuroscience , biochemistry , disease , gene

chromatography using monoclonal antibody (mAb) BT-2, which binds all -versions independent of their posttranslational modifications, and analyzed its N-glycosylation state after two-dimensional gel electrophoresis (2-DE) using sensitive immunoand lectin-blot analyses. Blots from crude resulted mostly in Nand O-glycosylated neurofilaments that incidentally comigrated with in SDS-PAGE, but were separated by the pH-gradient in 2-DE. Thus N-glycosylated versions present in the affinity purified were enriched by a lectin-based affinity chromatography. The eluate was separated by 2-DE and probed with an antimAb and lectins. Taken together, appears to be Oand N-glycosylated at a low level. This raises the question, if the glycosylation levels detected in PHFare really diseasespecific or if it is only related to different aggregation characteristics unand N-glycosylated species.

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