Titlebook: Regulation of the Contractile Cycle in Smooth Muscle; Takeshi Nakano (Professor),David J. Hartshorne (Pr Conference proceedings 1995 Sprin

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Cross-Bridge Cycle in Phasic and Tonic Smooth Muscle,the cross-bridge cycle is presented. (5) The affinity of cross-bridges for MgADP is much higher in tonic than in phasic smooth muscles. (6) Creatine phosphate (CP) accelerates relaxation induced by flash photolysis of Diazo-2 in isometrically contracted, permeabilized smooth muscle. We suggest that

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Regulation of Ca2+-Dependent Phosphorylation of 20-kDa Myosin Light Chain by the Small Molecular Wethe botulinum exoenzyme C., which specifically ADP-ribosylates and inactivates the rho family proteins, completely abolishes GTPγS-induced enhancement of Ca.-dependent MLC. phosphorylation. Under the same condition C. completely ADP-ribosylates cellular proteins with a relative molecular weight of 2

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Molecular Dissection of Regulatory Light Chain Function in Vertebrate Smooth Muscle Myosins,emonstrate that the origin of the third subdomain specifies the regulatory capability of the RLC. A series of smooth muscle myosin RLC mutants with deletions in the fourth subdomain show that the C-terminal helix in this subdomain is essential for regulation. Although the skeletal and scallop RLCs n

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Autoinhibition of Myosin Light Chain Kinase,bition. These results required reevaluation of the pseudosubstrate hypothesis. Based on a model showing the interaction of the pseudosubstrate sequence with the catalytic core, Y. interacts with a hydrophobic pocket in the catalytic core. We propose that this interaction is enough to inhibit the enz

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Regulation of Myosin Light Chain Kinase Activity in Smooth Muscle,us of the calmodulin-binding domain. This phosphorylation increases the concentration of Ca./calmodulin required for activation and hence physiologically increases the Ca z concentration required for light chain phosphorylation. However, in smooth muscle cells the concentration of Ca. necessary for

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Pharmacomechanical Coupling Through Regulation of Myosin Light Chain Phosphatase,osin light chain phosphatase, through dissociation of the catalytic from the targeting subunits, are illustrated, and studies showing the inhibition of voltage-gated Ca“ current by arachidonic acid are summarized. It is suggested that G protein-coupled protein phosphatase inhibition plays a signific

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Smooth Muscle Myosin Phosphatase,er and skeletal muscle, and higher concentrations of the 130-kDa component were found in samples of smooth muscle. Intact myosin phosphatase was purified from chicken gizzard with the MoAb as probe. The purified holoenzyme was a heterotrimer that consisted of PP1bc (38kDa) and regulatory subunits of

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Modulation of Vascular Smooth Muscle Contraction by Calponin Phosphorylation, of .P incorporation into the calponin in association with the development of force. These results suggest that calponin phosphorylation by protein kinase C plays a potential role in the modulation of smooth muscle contraction by agonists.