Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase.

@article{Garver1995TauPI,
  title={Tau phosphorylation in brain slices: pharmacological evidence for convergent effects of protein phosphatases on tau and mitogen-activated protein kinase.},
  author={Timothy D. Garver and George A. Oyler and Kristina A. Harris and Rathnagiri Polavarapu and Zahi Damuni and Ronald A Lehman and Melvin L. Billingsley},
  journal={Molecular pharmacology},
  year={1995},
  volume={47 4},
  pages={745-56}
}
Tau is a neuron-specific, microtubule-associated protein that forms paired helical filaments (PHFs) of Alzheimer's disease when aberrantly phosphorylated. We have attempted to elucidate the protein kinases and phosphatases that regulate tau phosphorylation. Incubation of rat, human, and rhesus monkey temporal neocortex slices with the phosphatase inhibitor okadaic acid induced epitopes of tau similar to those found in PHFs. Okadaic acid (1-20 microM) induced variant forms of tau at 60-68 kDa… CONTINUE READING
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