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• W1982898889 abstract "We have previously shown that vasopressin (VP) induces breakdown of membrane phosphoinositides in adrenal glomerulosa cells. In the present study we demonstrate that the accumulation of inositol phosphates (IP) measured in the presence of arginine vasopressin (AVP) is reduced if the cells are incubated in a calcium-free medium. This effect cannot be accounted for by modification of VP binding, reduction of inositol lipid labeling, or stimulation of inositol, 1,4,5,-triphosphate 5-monophosphatase. It mainly affects phospholipase-C activity, since this enzyme is highly sensitive to calcium. Ionomycine and nifedipine, which, respectively, increase and decrease the intracellular calcium concentration, also, respectively, stimulate and inhibit IP accumulation. In membranes prepared from pertussis toxin (IAP)-treated cells, AVP stimulates inositol monophosphate accumulation to the same extent as in membranes derived from untreated cells. However, in intact cells, IAP decreases the inositol monophosphate accumulation. This decrease probably involves calcium influx, since we show that AVP stimulates a unidirectional calcium influx, which is completely blocked by IAP treatment. In rat adrenal glomerulosa cells, the AVP-stimulated secretion of aldosterone is mainly under the control of calcium, since a full inhibition of its secretion is observed under conditions in which the calcium influxes are completely suppressed despite a sustained accumulation of IP (calcium depletion or IAP treatment). Together, these results signify that VP acts on rat glomerulosa cells by two distinct mechanisms: calcium influx, which is IAP sensitive, and phosphoinositide turnover, which is IAP insensitive." @default.
• W1982898889 created "2016-06-24" @default.
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• W1982898889 date "1990-03-01" @default.
• W1982898889 modified "2023-10-01" @default.
• W1982898889 title "Involvement of Distinct G-Proteins in the Action of Vasopressin on Rat Glomerulosa Cells" @default.
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• W1982898889 doi "https://doi.org/10.1210/endo-126-3-1699" @default.
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