Inhibition of rho-associated kinase reduces MLC20 phosphorylation and contractility of intact myometrium and attenuates agonist-induced Ca〔2+〕 sensitization of force of permeabilized rat myometrium

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  • OH Jae-Hwan
    Department of Surgery, Gachon Medical School, Gil Medical Center
  • YOU Sung-Kyung
    Department of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University
  • HWANG Mi-Kyung
    Department of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University
  • AHN Duck-Sun
    Department of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University
  • KWON Seong-chun
    Department of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University
  • TAGGART Michael J.
    Department of Medicine, Manchester Royal Infirmary The Maternal & Fetal Health Research Centre, St Mary's Hospital, University of Manchester
  • LEE Young-Ho
    Department of Physiology, College of Medicine, BK 21 Project for Medical Sciences, Yonsei University

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  • Inhibition of Rho-Associated Kinase Reduces MLC20 Phosphorylation and Contractility of Intact Myometrium and Attenuates Agonist-Induced Ca2+ Sensitization of Force of Permeabilized Rat Myometrium.

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The role of rhoA/rho-associated kinase (ROK) signaling pathways in agonist-induced contraction of the rat myometrium was investigated. We measured the [Ca2+]i-force relationship, phosphorylation of myosin regulatory light chains (MLC20) in intact tissue and the Ca2+-sensitization of force in permeabilized myometrial cells of rat. In measurements of the relationship between [Ca2+]i and tension in intact tissue, Y-27632, a ROK inhibitor, significantly attenuated the carbachol-induced contraction without changing [Ca 2+]i. Phosphorylation of MLC20 was increased by carbachol and this increased phosphorylation was blocked by treatment of tissue with Y-27632. In tension measurements of single hyperpermeable cells, carbachol evoked sustained contraction at constant pCa 6.7 and these agonist-induced contractions were decreased by treatment with Y-27632. These results suggest that activation of a ROK-mediated signaling pathway(s) plays an important role in agonist-induced alterations in MLC20 phosphorylation and force of rat myometrium.<br>

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