Phosphorylation of caldesmon by ERK MAP kinases in smooth muscle.

@article{Hedges2000PhosphorylationOC,
  title={Phosphorylation of caldesmon by ERK MAP kinases in smooth muscle.},
  author={Jason C. Hedges and Brian C Oxhorn and Misty Carty and Leonard P Adam and Ilia A. Yamboliev and William T. Gerthoffer},
  journal={American journal of physiology. Cell physiology},
  year={2000},
  volume={278 4},
  pages={
          C718-26
        }
}
Phosphorylation of h-caldesmon has been proposed to regulate airway smooth muscle contraction. Both extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases phosphorylate h-caldesmon in vitro. To determine whether both enzymes phosphorylate caldesmon in vivo, phosphorylation-site-selective antibodies were used to assay phosphorylation of MAP kinase consensus sites. Stimulation of cultured tracheal smooth muscle cells with ACh or platelet-derived growth factor… CONTINUE READING

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p38 MAP kinase expression and activation in smooth muscle

  • JC Hedges, IA Yamboliev, WT. Gerthoffer
  • Am J Physiol Cell Physiol 275:
  • 1998
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