Myosin light chain kinase from vascular smooth muscle inhibits the ATP-dependent interaction between actin and myosin by binding to actin

J Biochem. 1995 Jul;118(1):1-3. doi: 10.1093/oxfordjournals.jbchem.a124862.

Abstract

Myosin light chain kinase (MLCK) was prepared from smooth muscle of bovine aorta. MLCK inhibited the ATP-dependent movement of actin filaments on a glass surface coated with smooth muscle myosin that had been phosphorylated. The inhibitory effect was abolished by calmodulin in the presence of Ca2+ (Ca-CaM). The abolition was also observed when the concentration of actin filaments was increased. The inhibitory effect and its abolition were related to the actin-binding activity of MLCK, that is antagonized by Ca-CaM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Adenosine Triphosphate / antagonists & inhibitors*
  • Animals
  • Calcium / metabolism
  • Calmodulin / metabolism
  • Cattle
  • Muscle, Smooth, Vascular / enzymology*
  • Myosin-Light-Chain Kinase / metabolism*
  • Myosins / metabolism*
  • Protein Binding
  • Surface Properties

Substances

  • Actins
  • Calmodulin
  • Adenosine Triphosphate
  • Myosin-Light-Chain Kinase
  • Myosins
  • Calcium