Des-Arg9 bradykinin modulates DNA synthesis, phospholipase C, and protein kinase C in cultured mesangial cells. Distinction from effects of bradykinin.
作者： M. Issandou , J.M. Darbon
DOI: 10.1016/S0021-9258(18)54817-1
关键词:
摘要: The effects of the neuropeptide bradykinin (BK) and its natural proteolytic fragment Des-Arg9 (DBK) on DNA synthesis phospholipase C activation were investigated in cultured mesangial cells. DBK, acting through a distinct receptor, induced serum-starved effect DBK was dose dependent (ED50 = 0.6 microM) strongly potentiated by insulin. Under same conditions, BK had no effect. Down-regulation protein kinase long term pretreatment with 12-O-tetradecanoylphorbol-13-acetate (TPA) markedly reduced DBK-induced synthesis. In way, co-incubation inhibitor staurosporine potently attenuated response to suggesting role mitogenesis. Analysis phosphoproteins from 32P-labeled cells two-dimensional gel electrophoresis revealed that like TPA but not BK, net increase phosphorylation an acidic cellular migrating apparent Mr 80,000 (termed 80K), identified as major specific substrate C. Phosphorylation 80K or completely abolished depleted also 28,000 protein. Moreover, stimulated 18,000 normal well C-depleted large sustained diacylglycerol production inositol phosphate accumulation over 10-min incubation. only minor both parameters. These results demonstrate modulates
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