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We have studied the effect of overexpressing either wild-type or an Alzheimer's disease mutant Presenilin 1 (PS1) on tau phosphorylation in transfected Chinese hamster ovary (CHO) and COS cells. Tau transfected into these cells is predominantly non-phosphorylated at many PHF-tau sites but co-transfection with the tau kinase glycogen synthase kinase-3 beta (GSK-3 beta) induces phosphorylation that generates epitopes for several phosphorylation-dependent antibodies. Co-transfection of tau with either wild-type or mutant PS1 did not alter tau phosphorylation as detected by five different antibodies. Likewise, co-transfection of the PS1s did not influence GSK-3 beta-mediated tau phosphorylation. The implications of these results for the pathogenesis of Alzheimer's disease are discussed.


Journal article


Neurosci Lett

Publication Date





71 - 74


Alzheimer Disease, Animals, Antibody Specificity, Blotting, Western, CHO Cells, COS Cells, Calcium-Calmodulin-Dependent Protein Kinases, Cricetinae, Gene Expression, Glycogen Synthase Kinases, Membrane Proteins, Mutagenesis, Nerve Degeneration, Neurofibrillary Tangles, Phosphorylation, Point Mutation, Presenilin-1, Transfection, tau Proteins