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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Accession number;03A0101997
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| Title;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. |
| Author;
OH J-H
(Univ. Manchester, Manchester, Gbr)
YOU S-K
(Yonsei Univ., Seoul, Kor)
HWANG M-K
(Yonsei Univ., Seoul, Kor)
AHN D-S
(Yonsei Univ., Seoul, Kor)
KWON S-C
(Yonsei Univ., Seoul, Kor)
TAGGART M J
(Univ. Manchester, Manchester, Gbr)
LEE Y-H
(Yonsei Univ., Seoul, Kor)
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Journal Title;J Vet Med Sci
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Journal Code:F0905A
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ISSN:0916-7250
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VOL.65;NO.1;PAGE.43-50(2003)
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| Figure&Table&Reference;FIG.5, REF.26 |
| Pub. Country;Japan |
| Language;English |
| Abstract;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 [Ca2+]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 agonistinduced 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. (author abst.) |
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