Involvement of rho in GTPγS‐induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity
Copyright policy )Involvement of rho in GTPγS‐induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity
In β‐escin‐permeabilized cultured pig aortic smooth muscle cells GTPγS dose‐dependently enhances Ca2+‐induced wortmannin‐sensitive phosphorylation of 20 kDa myosin light chain (MLC20). GTPγS does not potentiate thiophosphorylation of MLC20, but does inhibit its dephosphorylation. Pretreatment with C. botulinum exotoxin C3, which specifically ADP‐ribosylates and inactivates the rho family of the small molecular weight G proteins, completely abolishes the effects of GTPγS. These results indicate that rho is involved in the GTPγS‐induced enhancement of Ca2+‐dependent MLC20 phosphorylation in aortic smooth muscle cells, and strongly suggest that this effect of rho is due to inhibition of protein phosphatase activity toward MLC20.
- University of Tokyo Japan
Escin, Botulinum Toxins, GTPγS, Swine, In Vitro Techniques, Myosins, Muscle, Smooth, Vascular, Smooth muscle, Rho, GTP-Binding Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Phosphoprotein Phosphatases, Animals, Calcium, Phosphorylation, Cells, Cultured, Myosin light chain phosphatase
Escin, Botulinum Toxins, GTPγS, Swine, In Vitro Techniques, Myosins, Muscle, Smooth, Vascular, Smooth muscle, Rho, GTP-Binding Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Phosphoprotein Phosphatases, Animals, Calcium, Phosphorylation, Cells, Cultured, Myosin light chain phosphatase
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