Myosin light chain and caldesmon phosphorylation in arterial muscle stimulated with endothelin-1

Leonard P. Adam, Lorraine Milio, Blair Brengle, David R. Hathaway

Research output: Contribution to journalArticlepeer-review

Abstract

Endothelin-1 contracts porcine carotid arterial smooth muscle with an ED50 of 10 nm. Contraction is associated with phosphorylation of the 20 000 dalton-regulatory light chain subunits of vascular myosin. Phosphopeptide mapping of light chains isolated from 32PO4-loaded muscle strips stimulated by endothelin-1 (5 × 10-8 m) and comparison with maps generated from light chains phosphorylated in vitro or muscles stimulated with KCl (110 mm) or angiotensin-II (5 × 10-8 m) indicates that Ca2+-calmodulin activation of myosin light chain kinase is a biochemical pathway stimulated by all three agonists. However, a small amount of phosphate (17%) was detected in a light chain peptide phosphorylated by protein kinase C. Endothelin-1 also stimulated phosphorylation of the thin filament protein, caldesmon, (from 0.35 mol PO4/mol caldesmon to 0.52 mol PO4/mol). Collectively, these results provide evidence that the effects of endothelin-1 on force generation and maintenance in vascular muscle may be dependent upon myosin light chain phosphorylation by Ca2+ calmodulin-requiring myosin light chain kinase and upon a thin filament mechanism that is modulated by phosphorylation of caldesmon.

Original languageEnglish (US)
Pages (from-to)1017-1023
Number of pages7
JournalJournal of Molecular and Cellular Cardiology
Volume22
Issue number9
DOIs
StatePublished - Sep 1990
Externally publishedYes

Keywords

  • Angiotensin
  • Caldesmon
  • Endothelin
  • Myosin light chains
  • Smooth muscle

ASJC Scopus subject areas

  • Molecular Biology
  • Cardiology and Cardiovascular Medicine

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