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Ras regulates NFAT3 activity in cardiac myocytes.

M Ichida1, T Finkel

  • 1Laboratory of Molecular Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA.

The Journal of Biological Chemistry
|October 25, 2000
PubMed
Summary
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Ras proteins interact with calcineurin pathways to regulate cardiac myocyte hypertrophy. This Ras-regulated pathway, involving mitogen-activated protein kinase, influences NFAT3 activity in heart cells.

Area of Science:

  • Cardiology
  • Molecular Biology
  • Cell Signaling

Background:

  • Cardiac myocyte hypertrophy involves distinct signal transduction pathways.
  • Key pathways include Ras superfamily small GTPases and calcineurin-NFAT3 signaling.

Purpose of the Study:

  • To investigate the functional interaction between Ras-regulated and calcineurin-regulated pathways in cardiac myocytes.
  • To elucidate the role of Ras proteins in regulating NFAT3 activity and cardiac hypertrophy.

Main Methods:

  • Expression of constitutively active and dominant-negative Ras mutants in neonatal myocytes.
  • Assessing NFAT activity and nuclear translocation of NFAT3 fusion proteins.
  • Utilizing pharmacological inhibitors (cyclosporin A, MEK1 inhibitor) and dominant-negative forms of Raf and ERK2.

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Main Results:

  • Constitutively active Ras (V12ras) increased NFAT activity and NFAT3 nuclear translocation, unlike other small GTPases.
  • Dominant-negative Ras blocked phenylephrine-stimulated NFAT activity and NFAT3 nuclear localization.
  • Ras appears upstream of calcineurin; MEK1/Raf/ERK pathway inhibition blocked NFAT3 activation, while their activation stimulated NFAT activity.

Conclusions:

  • A functional interaction exists between Ras-regulated and calcineurin-regulated pathways in cardiac myocytes.
  • Ras proteins regulate NFAT3 activity, likely via a pathway involving mitogen-activated protein kinase (MAPK).
  • These findings suggest a novel Ras-MAPK-NFAT3 axis in cardiac myocyte hypertrophy.