Abstract:
:Tau proteins are abnormally phosphorylated in Alzheimer's disease. Pathological Tau proteins named PHF-Tau 55, PHF-Tau 64, and PHF-Tau 69, are the main constituents of the paired helical filaments (PHF). When treating SKNSH-SY 5Y cells with okadaic acid (OA), Tau 55 protein was clearly induced whereas Tau 64 protein was only faintly induced. Here, we show that the absence of Tau 69 could be explained by the fact that adult isoforms containing N-terminal inserts are not detected. Phosphorylation is similar for untreated cellular Tau proteins and fetal Tau proteins, while OA cell treatment transformed fetal-type into Alzheimer-type phosphorylated proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Dupont-Wallois L,Sautière PE,Cocquerelle C,Bailleul B,Delacourte A,Caillet-Boudin MLdoi
10.1016/0014-5793(94)01361-4subject
Has Abstractpub_date
1995-01-03 00:00:00pages
197-201issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(94)01361-4journal_volume
357pub_type
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