Rho/ROCK pathway contributes to the activation of extracellular signal-regulated kinase/GATA-4 during myocardial cell hypertrophy

J Biol Chem. 2002 Mar 8;277(10):8618-25. doi: 10.1074/jbc.M107924200. Epub 2001 Dec 5.

Abstract

The low molecular weight GTPase Rho mediates a variety of cytoskeleton-dependent cell functions and stretch- and G(q) protein-induced hypertrophic responses in cardiac myocytes. Although ROCK, one of Rho's effectors, has been suggested to mediate hypertrophic signals, the relationship of Rho/ROCK with downstream signals is unknown. A zinc finger transcription factor, GATA-4, is activated by extracellular signal-regulated kinase 1/2 and is required for the up-regulation of the endothelin-1 gene during myocardial cell hypertrophy. However, it is unknown whether Rho/ROCK signals are linked to downstream GATA-4. By transient transfection assays using a dominant-negative mutant and an activated derivative of ROCK-I, we showed that ROCK-I participates in GATA-4-dependent endothelin-1 transcription. Inhibition of the Rho/ROCK pathway by Y-27632, a selective inhibitor of ROCK, suppressed phenylephrine-stimulated phosphorylation of extracellular signal-regulated kinase 1/2 and increased the DNA binding activity of cardiac GATA-4. Interestingly, latrunculin B, which inhibits actin polymerization, also prevents phenylephrine-induced responses. These findings demonstrate that the Rho/ROCK pathway is linked to downstream GATA-4 via the activation of extracellular signal-regulated kinases during myocardial cell hypertrophy. The results also suggest that changes in actin dynamics provide a convergence point for Rho/ROCK to the downstream signals during this process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Actins / metabolism
  • Amides / pharmacology
  • Animals
  • Blotting, Northern
  • Bridged Bicyclo Compounds, Heterocyclic / pharmacology
  • COS Cells
  • Cells, Cultured
  • DNA-Binding Proteins / metabolism*
  • Enzyme Activation
  • GATA4 Transcription Factor
  • Hypertrophy
  • Immunohistochemistry
  • Intracellular Signaling Peptides and Proteins
  • Luciferases / metabolism
  • Mice
  • Microscopy, Fluorescence
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases / metabolism*
  • Mutation
  • Myocardium / cytology*
  • Phenylephrine / pharmacology
  • Phosphorylation
  • Plasmids / metabolism
  • Protein Binding
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Serine-Threonine Kinases / physiology
  • Pyridines / pharmacology
  • Rats
  • Thiazoles / pharmacology
  • Thiazolidines
  • Transcription Factors / metabolism*
  • Transcription, Genetic
  • Transfection
  • Zinc Fingers
  • rho-Associated Kinases

Substances

  • Actins
  • Amides
  • Bridged Bicyclo Compounds, Heterocyclic
  • DNA-Binding Proteins
  • GATA4 Transcription Factor
  • Intracellular Signaling Peptides and Proteins
  • Pyridines
  • Thiazoles
  • Thiazolidines
  • Transcription Factors
  • Y 27632
  • Phenylephrine
  • Luciferases
  • Protein Serine-Threonine Kinases
  • rho-Associated Kinases
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • latrunculin B