[Detection of Alzheimer type pathological epitopes on Tau proteins of neuroblastoma cells after treatment with okadaic acid].
In Alzheimer's disease, Tau proteins are abnormally phosphorylated. In this paper, we describe a cellular model producing such pathological Tau proteins. After differentiation by NGF and treatment with okadaic acid (an inhibitor of phosphatases 1 and 2 A), neuroblastoma SKNSH-SY 5Y cells produced Tau proteins with an increased apparent molecular weight and a more acidic isoelectric point when compared to Tau proteins from control cells. These modified tau proteins bore Alzheimer-type epitopes detectable by antibodies specific to phosphorylated Alzheimer epitopes. This model is the first step toward a pharmacological approach of neuroprotection.
Sautière
P E
PE
INSERM U156, Laboratoire de Neurosciences, Lille, France.
Caillet-Boudin
M L
ML
Wattez
A
A
Buée-Scherrer
V
V
Delacourte
A
A
D000544:Alzheimer Disease / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D004988:Ethers, Cyclic / Q000494:pharmacology*; D006801:Humans; D009447:Neuroblastoma / Q000473:pathology*; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors* / Q000494:pharmacology*; D014407:Tumor Cells, Cultured / Q000187:drug effects / Q000276:immunology; D016875:tau Proteins / Q000276:immunology*
D000939:Epitopes; D004988:Ethers, Cyclic; D016875:tau Proteins; D019319:Okadaic Acid; D010749:Phosphoprotein Phosphatases