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- W2075959495 abstract "Noradrenaline increased phosphorylase a activity through activation of α1B-adrenoceptors in rat hepatocytes. Such effect was inhibited by chloroquine (Ki≈55 nM) and only slightly reduced by high concentrations of primaquine. Chloroquine did not inhibit the activation of phosphorylase a induced by vasopressin or angiotensin II. Binding competition experiments using [3H]prazosin showed that both chloroquine and primaquine interact with α1B-adrenoceptors, but only at very high concentrations. This indicates that the ability of chloroquine to block the α1B-adrenergic action was not due to antagonism at the receptor level. Noradrenaline increased phosphatidylinositol resynthesis and inositol trisphosphate production; these effects were inhibited by chloroquine and phorbol 12-myristate 13-acetate. Staurosporine and Ro 31-8220 (3-[1-[3-(amidinothio)propyl-1H-indol-3-yl]-3-(1-methyl-1H-indol-3-yl)maleimide), reduced the inhibitions induced by the active phorbol ester and the antimalarial drug on adrenergic-stimulated phosphatidylinositol resynthesis. Similarly, staurosporine blocked the inhibitory actions of chloroquine and phorbol 12-myristate 13-acetate on noradrenaline-stimulated inositol trisphosphate production. These data suggest the possibility that protein kinases, such as protein kinase C, could be involved in the actions of chloroquine." @default.
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- W2075959495 date "1998-01-01" @default.
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- W2075959495 title "Chloroquine inhibits α1B-adrenergic action in hepatocytes" @default.
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- W2075959495 doi "https://doi.org/10.1016/s0014-2999(97)01493-3" @default.
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