Modelling Alzheimer‐specific abnormal Tau phosphorylation independently of GSK3β and PKA kinase activities
- 12 March 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 516 (1-3) , 151-155
- https://doi.org/10.1016/s0014-5793(02)02525-5
Abstract
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 β (GSK3β) 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 GSK3β 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 pathologyKeywords
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