| Literature DB >> 2150518 |
M Abe1, K Takahashi, K Hiwada.
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.Entities:
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Year: 1990 PMID: 2150518 DOI: 10.1093/oxfordjournals.jbchem.a123289
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387