Prostaglandin (PG) F2α (30 μM) stimulated both monophosphorylation and diphosphorylation of myosin light chain (MLC) in a smooth muscle cell line (SM-3). The diphosphorylation was significantly decreased by treatment with the protein kinase C inhibitor staurosporine (30 nM, 30 min) from 20.1% of total MLC to 4.5%. The protein kinase C down-regulation treatment of SM-3 cells with phorbol dibutyrate suppressed to 8.7% the MLC diphosphorylation activity in the SM-3 cells. This down-regulation treatment had little effect on the monophosphorylation. We propose that the MLC diphosphorylation in PGF2α-stimulated SM-3 cells in culture may be regulated through mechanisms sensitive to protein kinase C.
