title: Diphosphorylation of myosin light chain in smooth muscle cells in culture. Possible involvement of protein kinase C.
abstract: Prostaglandin (PG) F2 alpha (30 microM) 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 PGF2 alpha-stimulated SM-3 cells in culture may be regulated through mechanisms sensitive to protein kinase C.
authors: Life Science Research Center, Asahi Chemical Industry, Co. Ltd., Miyazaki, Japan.
authors: Y
authors: Y
authors: Sasaki
authors: M
authors: M
authors: Seto
authors: K
authors: K
authors: Komatsu
mesh_terms: D000818:Animals; D001011:Aorta / Q000378:metabolism; D002460:Cell Line; D015237:Dinoprost / Q000494:pharmacology; D007700:Kinetics; D009131:Muscle, Smooth, Vascular / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010750:Phosphoproteins / Q000302:isolation & purification; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits; D013997:Time Factors
chemical_list: D010750:Phosphoproteins; D015237:Dinoprost; D011493:Protein Kinase C; D009218:Myosins