Hypertension, Vol 20, 129-137, Copyright © 1992 by American Heart Association
CM Rembold
Intracellular calcium concentration ([Ca2+]i)-dependent activation of
myosin light chain kinase and its phosphorylation of the 20-kd light chain
of myosin is generally considered the primary mechanism responsible for
regulation of contractile force in arterial smooth muscle. However, recent
data suggest that the relation between [Ca2+]i and myosin light chain
phosphorylation is variable and depends on the form of stimulation. The
dependence of myosin phosphorylation on [Ca2+]i has been termed the
"[Ca2+]i sensitivity of phosphorylation." The [Ca2+]i sensitivity of
phosphorylation is "high" when relatively small increases in [Ca2+]i induce
a large increase in myosin phosphorylation. Conversely, the [Ca2+]i
sensitivity of phosphorylation is "low" when relatively large increases in
[Ca2+]i are required to induce a small increase in myosin phosphorylation.
There are two proposed mechanisms for changes in the [Ca2+]i sensitivity of
phosphorylation: Ca(2+)-dependent decreases in the [Ca2+]i sensitivity of
phosphorylation induced by phosphorylation of myosin light chain kinase by
Ca(2+)-calmodulin protein kinase II and agonist-dependent increases in the
[Ca2+]i sensitivity of phosphorylation by inhibition of a myosin light
chain phosphatase. I will review the proposed mechanisms responsible for
the regulation of [Ca2+]i and the [Ca2+]i sensitivity of phosphorylation in
arterial smooth muscle.
ARTICLES
Regulation of contraction and relaxation in arterial smooth muscle
Department of Internal Medicine, University of Virginia School of Medicine, Charlottesville.
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