Protein Kinase FA/Glycogen Synthase Kinase‐3α After Heparin Potentiation Phosphorylates τ on Sites Abnormally Phosphorylated in Alzheimer's Disease Brain

@article{Yang1994ProteinKF,
  title={Protein Kinase FA/Glycogen Synthase Kinase‐3$\alpha$ After Heparin Potentiation Phosphorylates $\tau$ on Sites Abnormally Phosphorylated in Alzheimer's Disease Brain},
  author={Shiaw‐Der Yang and Jau-Song Yu and Shine-Gwo Shiah and Jun‐Jae Huang},
  journal={Journal of Neurochemistry},
  year={1994},
  volume={63}
}
Abstract: Previously, we identified protein kinase FA/glycogen synthase kinase‐3α (GSK‐3α) as a brain microtubule‐associated τ kinase that phosphorylates Ser235 and Ser404 of τ and causes its electrophoretic mobility shift in gels, a unique property characteristic of paired helical filament‐associated pathological τ (PHF‐τ) in Alzheimer's disease brains. In this study, we found that the activity of kinase FA/GSK‐3α towards phosphorylation of brain τ could be stimulated approximately fourfold by… 

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TLDR
Results provide initial evidence that protein kinase FA/GSK‐3 may represent one of the Ser‐Pro motif‐directed kinases involved in the abnormal phosphorylation of pathological PHF‐ in Alzheimer's disease brain.

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TLDR
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TLDR
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TLDR
Results provide initial evidence that the ATP·Mg-dependent protein phosphatase activating factor (FA) is a potent and unique MAP kinase, and may represent one of the major factors involved in phosphorylation of brain microtubules.
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