Serotonin-stimulated protein phosphorylation in aortic smooth muscle cells |
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Authors: | T. Nakaki B. C. Wise D. M. Chuang R. Kato |
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Affiliation: | (1) Department of Pharmacology, Keio University School of Medicine, 160 Tokyo, (Japan);(2) Laboratory of Preclinical Pharmacology, National Institute of Mental Health, St. Elizabeths Hospital, 20032 Washington, D.C, USA;(3) Present address: Department of Pharmacology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, 160 Tokyo, Japan;(4) Present address: Fidia-Georgetown Institute for the Neurosciences, Georgetown University School of Medicine, 20007 Washington, D.C., USA |
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Abstract: | Summary The effects of serotonin on the formation of inositol phosphates and protein phosphorylation were examined in cultured smooth muscle cells. Serotonin stimulated the formation of [3H]inositol monophosphate, [3H]inositol bisphosphate and [3H]inositol trisphosphate. This effect was prevented by 5-HT2 specific antagonist, 6-methyl-1-(1-methylethyl)ergoline-8-carboxylic acid, 2-hydroxy-1-methylpropyl ester [Z]-2-butenedioate (LY53857). Serotonin stimulated the phosphorylation of many polypeptides, among which a 20 kDa polypeptide was the most prominent. The phosphorylation was also inhibited by LY53857. LY53857 alone produced no effects on protein phosphorylation. The 20 kDa polypeptides were also phosphorylated by the addition of 12-O-tetradecanoylphorbol-13-acetate. These results suggest that serotonin stimulates protein phosphorylation through 5-HT2 receptors and possibly activates protein kinase C in intact vascular smooth muscle cells.Part of the data contained in this paper was presented at the 74th local meeting of the Japanese Society of Pharmacology at Kanagawa. |
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Keywords: | Serotonin protein phosphorylation smooth muscle cells LY53857 inositol trisphosphate |
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