EFFECTS OF CALDESMON, CALPONIN, AND TROPOMYOSIN ON THE MG^2＋ -ATPase ACTIVITIES OF SMOOTH MUSCLE MYOSIN

Objective To test whether in the absence of actin, actin-binding proteins such as caldesmon, calponin, and tropomyosin interact with the myosin of unphosphorylation, Ca^2 -dependent phosphorylation (CDP), and Ca^2 -independent phosphorylation (CIP) and stimulate myosin Mg^2 -ATPase activities. Methods Mg^2 -ATPase activities were measured to evaluate the effects of caldesmon, calponin, and tropomyosin on the myosin in unphosphorylation, CDP by myosin light chain kinase (MLCK), and CIP by MLCK. (1) At different incubation-time, i.e., 5, 10, 20, 40, and 60 minutes, the highest Mg^2 -ATPase activity was observed when myosin was in the state of CDP, the medium was CIP of myosin, and the lowest was the unphosphorylated myosin. (2) In the absence of caldesmon, calponin, and tropomyosin, the Mg^2 -ATPase activities from high to low were in the following order: CDP, CIP, and unphosphorylated myosin. However, in the presence of caldesmon, calponin, and tropomyosin, the order of relative value of Mg^2 -ATPase activities from high to low was unphosphorylated, CIP, and CDP of myosin respectively compared to the corresponding controls. Conelusions The results propose that caldesmon, calponin, and tropomyosin are capable of stimulating Mg^2 -ATPase activity of smooth muscle myosin in Ca^2 -independent manner, since Ca^2 is not obligating for the stimulating effects of the three proteins. The common characteristic of the three proteins is that when myosin activities are low, their activations are relatively strong and this property might be involved in smooth muscle tension keeping.

EFFECTS OF CALDESMON, CALPONIN, AND TROPOMYOSIN ON THE MG2+ -ATPase ACTIVITIES OF SMOOTH MUSCLE MYOSIN

Objective To test whether in the absence ofactin, actin-binding proteins such as caldesmon, calponin, and tropomyosin interact with the myosin of unphosphorylation, Ca2 -dependent phosphorylation (CDP), and Ca2 -independent phosphorylation (CIP) and stimulate myosin Mg2 -ATPase activities.Methods Mg2 -ATPase activities were measured to evaluate the effects of caldesmon, calponin, and tropomyosin on the myosin in unphosphorylation, CDP by myosin light chain kinase (MLCK), and CIP by MLCK.Results (1) At different incubation-time, i.e., 5, 10, 20, 40, and 60 minutes, the highest Mg2 -ATPase activity was observed when myosin was in the state of CDP, the medium was CIP of myosin, and the lowest was the unphosphorylated myosin. (2) In the absence of caldesmon, calponin, and tropomyosin, the Mg2 -ATPase activities from high to low were in the following order: CDP, CIP, and unphosphorylated myosin. However, in the presence of caldesmon, calponin, and tropomyosin, the order of relative value of Mg2 -ATPase activities from high to low was unphosphorylated, CIP, and CDP of myosin respectively compared to the corresponding controls.Conclusions The results propose that caldesmon, calponin, and tropomyosin are capable of stimulating Mg2 -ATPase activity of smooth muscle myosin in Ca2 -independent manner, since Ca2 is not obligating for the stimulating effects of the three proteins. The common characteristic of the three proteins is that when myosin activities are low, their activations are relatively strong and this property might be involved in smooth muscle tension keeping.