Regulation of the actin-myosin interaction of smooth muscle
نویسندگان
چکیده
منابع مشابه
Regulation of the interaction between smooth muscle myosin and actin.
Phosphorylation of the regulatory light chain of smooth muscle myosin efficiently regulates the actin-activated ATPase activity of myosin filaments in solution and actin movement in an in vitro motility assay, independently of thin-filament regulatory proteins. Filaments containing both phosphorylated and dephosphorylated heads move actin at intermediate rates, depending on the relative proport...
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Blebbistatin is a myosin II-specific inhibitor. However, the mechanism and tissue specificity of the drug are not well understood. Blebbistatin blocked the chemotaxis of vascular smooth muscle cells (VSMCs) toward sphingosylphosphorylcholine (IC(50) = 26.1 +/- 0.2 and 27.5 +/- 0.5 microM for GbaSM-4 and A7r5 cells, respectively) and platelet-derived growth factor BB (IC(50) = 32.3 +/- 0.9 and 3...
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A 35--70% ammonium sulfate fraction of smooth muscle actomyosin was prepared from guinea pig vas deferens. This fraction also contains a smooth muscle myosin kinase and a phosphatase that phosphorylates and dephosphorylates, respectively, the 20,000-dalton light chain of smooth muscle myosin. Phosphorylated and dephosphorylated smooth muscle myosin. Phosphorylated and dephosphorylated smooth mu...
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The putative actin-binding interface of myosin is separated by a large cleft that extends into the base of the nucleotide binding pocket, suggesting that it may be important for mediating the nucleotide-dependent changes in the affinity for myosin on actin. We have genetically engineered a truncated version of smooth muscle myosin containing the motor domain and the essential light chain-bindin...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1997
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)44663-5