Sasaki Y, Seto M, Komatsu K
Life Science Research Center, Asahi Chemical Industry, Co. Ltd., Miyazaki, Japan.
FEBS Lett. 1990 Dec 10;276(1-2):161-4. doi: 10.1016/0014-5793(90)80532-n.
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.
前列腺素（PG）F2α（30微摩尔）刺激了平滑肌细胞系（SM-3）中肌球蛋白轻链（MLC）的单磷酸化和双磷酸化。用蛋白激酶C抑制剂星形孢菌素（30纳摩尔，30分钟）处理后，双磷酸化从总MLC的20.1%显著降低至4.5%。用佛波酯对SM-3细胞进行蛋白激酶C下调处理后，SM-3细胞中的MLC双磷酸化活性被抑制至8.7%。这种下调处理对单磷酸化影响很小。我们认为，培养的PGF2α刺激的SM-3细胞中的MLC双磷酸化可能通过对蛋白激酶C敏感的机制进行调节。
