Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation

Yasuko Kureishi, Sei Kobayashi, Mutsuki Amano, Kazushi Kimura, Hideo Kanaide, Takeshi Nakano, Kozo Kaibuchi, Masaaki Ito

研究成果: Article査読

493 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)12257-12260
ページ数4
ジャーナルJournal of Biological Chemistry
272
19
DOI
出版ステータスPublished - 09-05-1997
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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