NDLI: Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle.

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Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle.

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Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Eccleston, J. F. Gong, M. C. Browne, J. P. Somlyo, A. P. Iizuka, K. Hall, A. Somlyo, A. V. Nixon, G. Kobayashi, S. Sugai, M.
Description	Author Affiliation: Gong MC ( Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22908, USA.);
Abstract	The purpose of this study was to identify guanine nucleotide-binding proteins (G proteins) involved in the agonist- and guanosine 5'-[gamma-thio]triphosphate (GTP[gamma-S])-induced increase in the Ca2+ sensitivity of 20-kDa myosin light chain (MLC20) phosphorylation and contraction in smooth muscle. A constitutively active, recombinant val14p21rhoA.GTP expressed in the baculovirus/Sf9 system, but not the protein expressed without posttranslational modification in Escherichia coli, induced at constant Ca2+ (pCa 6.4) a slow contraction associated with increased MLC20 phosphorylation from 19.8% to 29.5% (P < 0.05) in smooth muscle permeabilized with beta-esein. The effect of val14p21rhoA.GTP was inhibited by ADP-ribosylation of the protein and was absent in smooth muscle extensively permeabilized with Triton X-100. ADP-ribosylation of endogenous p21rho with epidermal cell differentiation inhibitor (EDIN) inhibited Ca2+ sensitization induced by GTP [in rabbit mesenteric artery (RMA) and rabbit ileum smooth muscles], by carbachol (in rabbit ileum), and by endothelin (in RMA), but not by phenylephrine (in RMA), and only slowed the rate without reducing the amplitude of contractions induced in RMA by 1 microM GTP[gamma-S] at constant Ca2+ concentrations. AlF(4-)-induced Ca2+ sensitization was inhibited by both guanosine 5'-[beta-thio]diphosphate (GDP[beta-S]) and by EDIN. EDIN also inhibited, to a lesser extent, contractions induced by Ca2+ alone (pCa 6.4) in both RMA and rabbit ileum. ADP-ribosylation of trimeric G proteins with pertussis toxin did not inhibit Ca2+ sensitization. We conclude that p21rho may play a role in physiological Ca2+ sensitization as a cofactor with other messengers, rather than as a sole direct inhibitor of smooth muscle MLC20 phosphatase.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Pharmacology GTP-Binding Proteins Metabolism Muscle, Smooth, Vascular Physiology Muscle, Smooth Animals Carbachol Cell Line Cell Membrane Permeability Cloning, Molecular Endothelins Enterotoxins Biosynthesis Isolation & Purification Guanosine 5'-O-(3-Thiotriphosphate) Guanosine Triphosphate Ileum In Vitro Techniques Mesenteric Arteries Drug Effects Pertussis Toxin Phenylephrine Rabbits Recombinant Proteins Spodoptera Staphylococcus Aureus Virulence Factors, Bordetella RhoA GTP-Binding Protein Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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