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(Received for publication, March 4, 1997)
,
From the First Department of Internal Medicine, Mie University
School of Medicine, Tsu, Mie 514, Japan, the Small GTPase Rho plays pivotal roles in the
Ca2+ sensitization of smooth muscle. However, the
GTP-bound active form of Rho failed to exert
Ca2+-sensitizing effects in extensively Triton
X-100-permeabilized smooth muscle preparations, due to the loss of the
important diffusible cofactor (Gong, M. C., Iizuka, K., Nixon, G.,
Browne, J. P., Hall, A., Eccleston, J. F., Sugai, M., Kobayashi, S.,
Somlyo, A. V., and Somlyo, A. P. (1996) Proc. Natl. Acad. Sci.
U. S. A. 93, 1340-1345). Here we demonstrate the contractile
effects of Rho-associated kinase (Rho-kinase), recently identified as a
putative target of Rho, on the Triton X-100-permeabilized smooth muscle
of rabbit portal vein. Introduction of the constitutively active form
of Rho-kinase into the cytosol of Triton X-100-permeabilized smooth muscle provoked a contraction and a proportional increase in levels of
monophosphorylation of myosin light chain in both the presence and the
absence of cytosolic Ca2+. These effects of constitutively
active Rho-kinase were wortmannin (a potent myosin light chain kinase
inhibitor)-insensitive. Immunoblot analysis revealed that the amount of
native Rho-kinase was markedly lower in Triton X-100-permeabilized
tissue than in intact tissue. Our results demonstrate that
Rho-kinase directly modulates smooth muscle contraction through myosin
light chain phosphorylation, independently of the
Ca2+-calmodulin-dependent myosin light chain kinase
pathway.
First
Department of Physiology, Yamaguchi University School of Medicine, Ube,
Yamaguchi 755, Japan, the ¶ Division of Signal Transduction, Nara
Institute of Science and Technology, Ikoma, Nara 630-01, Japan, and the
§ Division of Molecular Cardiology, Research Institute of
Angiocardiology, Faculty of Medicine, Kyushu University,
Fukuoka 812, Japan
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