Abstract
In β-escin-permeabilized cultured pig aortic smooth muscle cells GTPγS dose-dependently enhances Ca 2+-induced wortmannin-sensitive phosphorylation of 20 kDa myosin light chain (MLC 20). GTPγS does not potentiate thiophosphorylation of MLC 20, but does inhibit its dephosphorylation. Pretreatment with C. botulinum exotoxin C 3, 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 Ca 2+-dependent MLC 20 phosphorylation in aortic smooth muscle cells, and strongly suggest that this effect of rho is due to inhibition of protein phosphatase activity toward MLC 20.
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