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Modelling Alzheimer‐specific abnormal Tau phosphorylation independently of GSK3β and PKA kinase activities
Author(s) -
Delobel P,
Flament S,
Hamdane M,
Delacourte A,
Vilain J.P,
Buée L
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02525-5
Subject(s) - gsk 3 , kinase , phosphorylation , epitope , tau protein , cyclin dependent kinase 5 , protein kinase a , xenopus , glycogen synthase , chemistry , microbiology and biotechnology , biochemistry , biology , alzheimer's disease , mitogen activated protein kinase kinase , antibody , medicine , disease , immunology , gene
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 pathology.