Inhibition of myosin light chain phosphorylation in cultured smooth muscle cells by HA1077, a new type of vasodilator

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Abstract

When cultured smooth muscle cells were stimulated sequentially by concanavalin A and fetal calf serum, the cells rounded up, and there was an accompanying mono- and diphosphorylation of the 20 kDa myosin light chain. HA1077, a new type of vasodilator, inhibited both the cell rounding and the light chain phosphorylation in a concentration dependent manner. Since HA1077 inhibits myosin light chain kinase, in vitro, we propose that this vasodilator presumably inhibits cell rounding by limiting myosin light chain phosphorylation.

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    The inactive t-CA-4-P (0.1-10 µM) failed to induce any significant actin reorganization (data not shown). To determine whether the actin response to CA-4-P was due to the activation of Rho and Rho-kinase, cells were pretreated with the selective Rho inhibitor C3 exoenzyme from Clostridium botulinum33 (24 hours, 10 µg/mL; Figure 2C,D) or Rho-kinase inhibitors Y-2763230 (30 minutes, 10 µM; Figure 2E,F) and HA107742 (30 minutes, 10 µM; Figure2G,H) before CA-4-P addition. All inhibitors reduced microfilament assembly in resting cells to a small extent and completely blocked CA-4-P–mediated actin stress fiber formation.

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