Shift from fetal-type to Alzheimer-type phosphorylated Tau proteins in SKNSH-SY 5Y cells treated with okadaic acid.
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.
Dupont-Wallois
L
L
INSERM U156, Laboratoire de Neurosciences, Lille, France.
Sautière
P E
PE
Cocquerelle
C
C
Bailleul
B
B
Delacourte
A
A
Caillet-Boudin
M L
ML
D000328:Adult; D000544:Alzheimer Disease / Q000378:metabolism*; D001483:Base Sequence; D001921:Brain / Q000378:metabolism; D002460:Cell Line; D004988:Ethers, Cyclic / Q000494:pharmacology*; D005326:Fetal Proteins / Q000187:drug effects / Q000378:metabolism*; D005333:Fetus; D006801:Humans; D008969:Molecular Sequence Data; D019319:Okadaic Acid; D010766:Phosphorylation; D016875:tau Proteins / Q000187:drug effects / Q000378:metabolism*
D004988:Ethers, Cyclic; D005326:Fetal Proteins; D016875:tau Proteins; D019319:Okadaic Acid