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J. Biol. Chem., Vol. 259, Issue 22, 13656-13659, Nov, 1984
PK Ngai and MP Walsh
Caldesmon, a major calmodulin- and actin-binding protein of smooth muscle
(Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Proc. Natl.
Acad. Sci. U. S. A. 78, 5652-5655), has been obtained in highly purified
form from chicken gizzard by a modification of a previously published
procedure (Ngai, P. K., Carruthers, C. A., and Walsh, M. P. (1984) Biochem.
J. 218, 863-870) and was found to cause a significant inhibition of both
superprecipitation and actin-activated myosin Mg2+-ATPase activity in a
system reconstituted from the purified contractile and regulatory proteins
without influencing the phosphorylation state of myosin. This inhibitory
effect was seen both in the presence and absence of tropomyosin. A Ca2+-and
calmodulin- dependent kinase which catalyzed phosphorylation of caldesmon
was identified in chicken gizzard; this kinase is distinct from myosin
light-chain kinase. Caldesmon prepared by calmodulin-Sepharose affinity
chromatography was contaminated with caldesmon kinase activity and was
unable to inhibit actomyosin ATPase activity or superprecipitation.
Phosphatase activity capable of dephosphorylating caldesmon was also
identified in smooth muscle. These results indicate that caldesmon can
inhibit smooth muscle actomyosin ATPase activity in vitro, and this
function may itself be subject to regulation by reversible phosphorylation
of caldesmon.
Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon
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