The phosphorylation state of MAP-kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide

FEBS Lett. 1996 Jul 8;389(3):285-8. doi: 10.1016/0014-5793(96)00605-9.


Micromolar concentrations of hydrogen peroxide induced the phosphorylation of mitogen-activated protein (MAP) kinases and a lethal response in growth-arrested smooth muscle cells (A7r5). The H202-induced phosphorylation of MAP-kinases was markedly lower in the presence of protein tyrosine kinase (PTK) inhibitors or in protein kinase C (PKC) down-regulated cells. Similarly, the toxicity of H202 was diminished by concomitant addition of either PKC or PTK inhibitors and was also lower in PKC down-regulated cells. These results are consistent with the possibility that phosphorylation of MAP-kinases is a critical event in the toxic response of cultured smooth muscle cells to H202.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Catechols / pharmacology
  • Cell Death / drug effects
  • Cell Division / drug effects
  • Clone Cells
  • Down-Regulation
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Hydrogen Peroxide / pharmacology*
  • Muscle, Smooth / cytology*
  • Muscle, Smooth / drug effects
  • Naphthalenes / pharmacology
  • Nitriles / pharmacology
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Rats
  • Tyrphostins*


  • Catechols
  • Enzyme Inhibitors
  • Naphthalenes
  • Nitriles
  • Tyrphostins
  • calphostin complex
  • Hydrogen Peroxide
  • Protein-Tyrosine Kinases
  • Protein Kinase C
  • Calcium-Calmodulin-Dependent Protein Kinases
  • tyrphostin A23