{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T08:04:12Z","timestamp":1760169852577},"reference-count":26,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2001,12,20]],"date-time":"2001-12-20T00:00:00Z","timestamp":1008806400000},"content-version":"vor","delay-in-days":49,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Molecular Recognition"],"published-print":{"date-parts":[[2001,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Studies of oxytocin\u2010induced phosphorylation of myosin light chain (MLC), resulting in myometrial contraction, suggest that extracellular Ca<jats:sup>2+<\/jats:sup> influx is involved in its signal transduction. To explore the possibility that intracellular Ca<jats:sup>2+<\/jats:sup> mobilization by oxytocin may also contribute to MLC phosphorylation, we investigated the relative contributions of these Ca<jats:sup>2+<\/jats:sup> sources to oxytocin signal transduction in myometrium of pregnant rat. In pregnant rat myometrium, oxytocin\u2010induced Ca<jats:sup>2+<\/jats:sup> influx occurs via an L\u2010type voltage\u2010dependent Ca<jats:sup>2+<\/jats:sup> channel. Treatment with verapamil, an antagonist specific for these channels, significantly diminished MLC phosphorylation observed in response to oxytocin administration without affecting the release of Ca<jats:sup>2+<\/jats:sup> from intracellular Ca<jats:sup>2+<\/jats:sup> stores. Furthermore, oxytocin\u2010induced MLC phosphorylation was not observed when extracellular Ca<jats:sup>2+<\/jats:sup> was not present. Our results clearly indicate that extracellular Ca<jats:sup>2+<\/jats:sup> influx, rather than release from Ca<jats:sup>2+<\/jats:sup> storage sites, is essential for oxytocin\u2010induced MLC phosphorylation. 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