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J Biol Chem, Vol. 274, Issue 6, 3744-3752, February 5, 1999

Rho-associated Kinase of Chicken Gizzard Smooth Muscle

Jianhua FengDagger , Masaaki ItoDagger , Yasuko KureishiDagger , Kazuhito IchikawaDagger , Mutsuki Amano, Naoki IsakaDagger , Katsuya Okawaparallel , Akihiro Iwamatsuparallel , Kozo Kaibuchi, David J. Hartshorne**, and Takeshi NakanoDagger

From the Dagger  First Department of Internal Medicine, Mie University School of Medicine, Tsu, 514-8507, Japan, the  Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-0101, Japan, the parallel  Central Laboratories for Key Technology, Kirin Brewery Co. Ltd., Yokohama 326, Japan, and the ** Muscle Biology Group, Shantz Building, University of Arizona, Tucson, Arizona 85721

Rho-associated kinase (Rho-kinase) from chicken gizzard smooth muscle was purified to apparent homogeneity (160 kDa on SDS-polyacrylamide gel electrophoresis) and identified as the ROKalpha isoform. Several substrates were phosphorylated. Rates with myosin phosphatase target subunit 1 (MYPT1), myosin, and the 20-kDa myosin light chain were higher than other substrates. Thiophosphorylation of MYPT1 inhibited myosin phosphatase activity. Phosphorylation of myosin at serine 19 increased actin-activated Mg+-ATPase activity, i.e. similar to myosin light chain kinase. Myosin phosphorylation was increased at higher ionic strengths, possibly by formation of 6 S myosin. Phosphorylation of the isolated light chain and myosin phosphatase was decreased by increasing ionic strength. Rho-kinase was stimulated 1.5-2-fold by guanosine 5'-O-3-(thio)triphosphate·RhoA, whereas limited tryptic hydrolysis caused a 5-6-fold activation, independent of RhoA. Several kinase inhibitors were screened and most effective were Y-27632, staurosporine, and H-89. Several lipids caused slight activation of Rho-kinase, but arachidonic acid (30-50 µM) induced a 5-6-fold activation, independent of RhoA. These results suggest that Rho-kinase of smooth muscle may be involved in the contractile process via phosphorylation of MYPT1 and myosin. Activation by arachidonic acid presents a possible regulatory mechanism for Rho-kinase.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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