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- W1570546061 abstract "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." @default.
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- W1570546061 date "1990-12-10" @default.
- W1570546061 modified "2023-09-27" @default.
- W1570546061 title "Diphosphorylation of myosin light chain in smooth muscle cells in culture" @default.
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- W1570546061 doi "https://doi.org/10.1016/0014-5793(90)80532-n" @default.
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