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Related Experiment Videos

Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain

C X Gong1, S Shaikh, J Z Wang

  • 1New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314, USA.

Journal of Neurochemistry
|August 1, 1995
PubMed
Summary
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Protein phosphatase activity dephosphorylating tau is reduced in Alzheimer disease brains. This defect may cause abnormal tau hyperphosphorylation, a hallmark of Alzheimer disease pathology.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Microtubule-associated protein tau (tau) becomes abnormally hyperphosphorylated and aggregates in Alzheimer disease (AD) neurons.
  • Certain protein phosphatases, including PP1, PP2A, and PP2B, can dephosphorylate tau in vitro.

Purpose of the Study:

  • To develop an assay for measuring protein phosphatase activity against specific tau phosphorylation sites (Ser199/Ser202).
  • To investigate the role of protein phosphatases in tau dephosphorylation in normal and Alzheimer disease brains.

Main Methods:

  • Developed a specific assay using hyperphosphorylated tau from AD brains as substrate.
  • Measured protein phosphatase activity toward tau-1 sites (Ser199/Ser202).
  • Compared phosphatase activity between AD and age-matched control brains.

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Main Results:

  • Identified protein phosphatase-2A (PP2A) and 2B (PP2B), and to a lesser extent PP1, as key enzymes for tau dephosphorylation in normal brain.
  • Observed similar Michaelis-Menten constant (Km) values for PP2A and PP2B in tau dephosphorylation.
  • Found a significant decrease of approximately 30% in tau phosphatase activity in AD brains compared to controls.

Conclusions:

  • A defect in protein phosphatase activity is implicated in the abnormal hyperphosphorylation of tau in Alzheimer disease.
  • Reduced tau phosphatase activity may contribute to the neurofibrillary tangle pathology observed in AD.