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P3‐008: Deregulation of PP2A and hyperphosphorylation of tau protein following onset of diabetes in NOD mice
Author(s) -
El Khoury Noura B.,
Papon MarieAmelie,
Marcouiller François,
Julien Carl,
Morin Françoise,
Petry Franck,
Whittington Robert,
Planel Emmanuel
Publication year - 2012
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.2012.05.1226
Subject(s) - hyperphosphorylation , nod , endocrinology , medicine , phosphorylation , tau protein , diabetes mellitus , insulin , nod mice , protein phosphatase 2 , biology , phosphatase , alzheimer's disease , disease , microbiology and biotechnology
protease. Tau constructs with amino acid substitutions have been produced and are being assayed to determine the active site amino acids. Conclusions: Tau protease activity is dependent on oligomerization causing self-fragmentation, as well as cleavage of other proteins that may be indicative of a direct pathological of tau in AD. The disease relevance of this activity is being studied as this may represent an important mechanism in the development of pathology and a druggable target for the development of therapeutics and biomarkers.