TY - JOUR
T1 - Myosin phosphorylation and the control of myometrial contraction/relaxation
AU - Word, R. Ann
N1 - Funding Information:
From the Department of Obstetrics and Gynecology, The University of Texas Southwestern Medical Center at Dallas, "IX. Supported by National Institutes of Health grant nos. HD11149 and HL26043. Address reprint requests to R. Ann Word, MD, Department of Obstetrics and Gynecology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX 75235-9032. Copyright 9 1995 by W.B. Saunders Company O146-0005/95/1901-0002505.00/0
PY - 1995/2
Y1 - 1995/2
N2 - 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.
AB - 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.
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U2 - 10.1016/S0146-0005(95)80043-3
DO - 10.1016/S0146-0005(95)80043-3
M3 - Article
C2 - 7754409
AN - SCOPUS:0028944015
SN - 0146-0005
VL - 19
SP - 3
EP - 14
JO - Seminars in Perinatology
JF - Seminars in Perinatology
IS - 1
ER -