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FEBS Lett 2002 Apr 10;5161-3:151-5. doi: 10.1016/s0014-5793(02)02525-5.
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Modelling Alzheimer-specific abnormal Tau phosphorylation independently of GSK3beta and PKA kinase activities.

Delobel P , Flament S , Hamdane M , Delacourte A , Vilain JP , Buée L .

In Alzheimer''s disease, neurofibrillary degeneration results from the aggregation of abnormally phosphorylated Tau proteins into paired helical filaments. These Tau variants displayed specific epitopes that are immunoreactive with anti-phospho-Tau antibodies such as AT100. As shown in in vitro experiments, glycogen synthase kinase 3 beta (GSK3beta) and protein kinase A (PKA) may be key kinases in these phosphorylation events. In the present study, Tau was microinjected into Xenopus oocytes. Surprisingly, in this system, AT100 was generated without any GSK3beta and PKA contribution during the progesterone or insulin-induced maturation process. Our results demonstrate that a non-modified physiological process in a cell model can generate the most specific Alzheimer epitope of Tau pathology.

PubMed ID: 11959122
Article link: FEBS Lett

Species referenced: Xenopus
Genes referenced: gsk3b ins mapt
GO keywords: oocyte maturation [+]

Disease Ontology terms: Alzheimer's disease [+]