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Tau hyperphosphorylation affects Smad 2/3 translocation.

S Baig1, Z van Helmond, S Love

  • 1Dementia Research Group, Institute of Clinical Neurosciences, Department of Clinical Science at North Bristol, University of Bristol, Frenchay Hospital, Bristol BS16 1LE, UK. shabnam.baig@bristol.ac.uk

Neuroscience
|June 27, 2009
PubMed
Summary
This summary is machine-generated.

Transforming growth factors beta (TGFbeta) signaling is disrupted in Alzheimer's disease (AD) by hyperphosphorylated tau. This tau pathology impedes neuroprotective TGFbeta actions, potentially worsening neurodegeneration.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Transforming growth factors beta (TGFbeta) regulate cellular activities via the Smad pathway.
  • Elevated TGFbeta in Alzheimer's disease (AD) suggests a neuroprotective role.
  • Tau hyperphosphorylation in AD disrupts TGFbeta-Smad signaling.

Purpose of the Study:

  • To investigate if tau hyperphosphorylation affects Smad2/3 localization in neurons.
  • To determine the impact of AD-relevant tau phosphorylation on TGFbeta-Smad signaling.

Main Methods:

  • Primary rat cortical cells were treated with okadaic acid to induce tau hyperphosphorylation.
  • Cells were also treated with synthetic oligomeric amyloid-beta (Aβ(1-42)) as an AD model.
  • Localization of phosphorylated Smad2/3 (pSmad2/3) was assessed in relation to tau phosphorylation.

Main Results:

  • Okadaic acid treatment caused tau hyperphosphorylation and disrupted pSmad2/3 nuclear translocation.
  • Amyloid-beta treatment confirmed that tau phosphorylation impedes pSmad2/3 nuclear entry.
  • pSmad2/3 co-localized with hyperphosphorylated tau in the cytoplasm.

Conclusions:

  • Tau hyperphosphorylation in AD sequesters pSmad2/3 in the cytoplasm, blocking nuclear translocation.
  • This disruption impedes the neuroprotective functions of TGFbeta signaling in AD neurons.
  • Impaired TGFbeta-Smad pathway signaling may contribute to neurodegeneration in Alzheimer's disease.