Myosin light chain kinase from vascular smooth muscle inhibits the ATP-dependent interaction between actin and myosin by binding to actin.
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.
Sato
M
M
Department of Pharmacology, Gunma University School of Medicine.
Ye
L H
LH
Kohama
K
K
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000037:antagonists & inhibitors*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D002417:Cattle; D009131:Muscle, Smooth, Vascular / Q000201:enzymology*; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D011485:Protein Binding; D013499:Surface Properties
D000199:Actins; D002147:Calmodulin; D000255:Adenosine Triphosphate; D009219:Myosin-Light-Chain Kinase; D009218:Myosins; D002118:Calcium