Effect of calponin on actin-activated myosin ATPase activity.

doi:10.1093/OXFORDJOURNALS.JBCHEM.A123289

Paper

Effect of calponin on actin-activated myosin ATPase activity.

Published Nov 1, 1990 · M. Abe, K. Takahashi, K. Hiwada

Journal of biochemistry

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116

Citations

8

Influential Citations

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Abstract

Calponin inhibited the actin-activated myosin MgATPase activity in a dose-dependent manner without affecting the phosphorylation level of myosin light chain. This inhibition was Ca2(+)-independent. The decrease in enzymatic activity of myosin was correlated with binding of calponin to actin-tropomyosin filaments. Caldesmon showed a further inhibition of the calponin-induced inhibition of MgATPase activity of the thiophosphorylated myosin. Calponin-induced inhibition of the myosin MgATPase activity was reversed by the addition of calmodulin only in the presence of Ca2+. These results suggest that calponin acts as an inhibitory component of smooth muscle thin filaments.

In Vitro Study

Highly Cited

Study Snapshot

Calponin acts as an inhibitory component of smooth muscle thin filaments, inhibiting actin-activated myosin MgATPase activity without affecting phosphorylation levels of myosin light chain.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Paper

Effect of calponin on actin-activated myosin ATPase activity.

References

Citations

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