A new look at uterine muscle contraction

Mary E. Carsten, Jordan D. Miller
In: American Journal of Obstetrics and Gynecology · 1987 · vol. 157(5) , pp. 1303–1315 · doi:10.1016/s0002-9378(87)80320-4 · PMID:2446500 · W2039905246
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This review details recent findings on uterine muscle contraction, highlighting the shift from thin filament activation to calcium-dependent myosin phosphorylation, the roles of multiple calcium sources, prostaglandin actions, and the involvement of second messengers like phosphoinositides and cyclic AMP.

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Abstract

Recent progress in our understanding of uterine smooth muscle contraction is reviewed. We no longer believe that actin-myosin interaction in the myometrium occurs through activation of the thin filament; but it is triggered by calcium-dependent phosphorylation of myosin in the thick filament. Calcium is now thought to originate from both extracellular and intracellular sources. Calcium can enter the cell through either a voltage- or a hormone-controlled calcium channel. The intracellular source of calcium is the sarcoplasmic reticulum. The effect of oxytocin in human labor is no longer considered the result of increased circulating oxytocin but rather of increased oxytocin receptors. In contrast, the contractile action of some prostaglandins is related to increased prostaglandin formation at human parturition. The step between hormone binding and cellular action is mediated by second messengers. The uterine-relaxing action of cyclic adenosine monophosphate is now thought to be limited to the inhibition of myosin phosphorylation. Recently discovered second messengers for contraction of the myometrium are phosphoinositides; their turnover causes calcium release from the sarcoplasmic reticulum. Guanine nucleotides are thought to be modulators of these two second messengers.

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