MYOSIN PHOSPHORYLATION AND THE CONTROL OF MYOMETRIAL CONTRACTION-RELAXATION

In summary, phosphorylation of the regulatory light chain of myosin by Ca2+/CaM-dependent MLCK plays an important role in smooth muscle contraction. Although there have been major advances in our understanding of the regulation and physiological functions of contractile proteins in smooth muscle in recent years, very little information exists on the functional status of these proteins in human myometrium during pregnancy. The simple view that contractile force in smooth muscle is proportionate to cytoplasmic Ca2+ concentrations (Cai2+) and myosin light chain phosphorylation is now more complex as more experiments provide insights into mechanisms of regulation of the contractile elements. MLCK can be phosphorylated, which desensitizes its activation by Ca2+/CaM, and protein phosphatase activity toward myosin may also be regulated. Examples in smooth muscle tissue are sparse, and the different mechanisms by which these processes may be adapted in uterine smooth muscle during pregnancy are not well-defined. Much research is needed to define further the cellular, biochemical, and molecular basis for these physiological processes involved in the regulation of uterine smooth muscle contraction and relaxation. © 1995 W.B. Saunders Company.