DIRECT MODIFICATION OF THE MEMBRANE ADENYLATE-CYCLASE SYSTEM BY ISLET-ACTIVATING PROTEIN DUE TO ADP-RIBOSYLATION OF A MEMBRANE-PROTEIN
DIRECT MODIFICATION OF THE MEMBRANE ADENYLATE-CYCLASE SYSTEM BY ISLET-ACTIVATING PROTEIN DUE TO ADP-RIBOSYLATION OF A MEMBRANE-PROTEIN
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DOI：
10.1073/pnas.79.10.3129
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发表时间：
1982-01-01
期刊：
影响因子：
--
通讯作者：
UI, M
中科院分区：
文献类型：
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作者：
KATADA, T;UI, M
如果孵育混合物中补充了NAD和ATP，则通过与胰岛活化蛋白（来自百日咳博德特氏菌的百日咳毒素之一）孵育，增强了从[大鼠] C6神经胶质瘤细胞制备的洗涤膜中腺苷酸环化酶[ATP焦磷酸裂解酶（环化），EC 4.6.1.1]的GTP和异丙肾上腺素活化。加入后立即观察到蛋白质的作用，并随着蛋白质浓度或孵育时间的增加而逐渐增加。同时，不同标记NAD的ADP-核糖部分的放射性掺入MW为41，000的膜蛋白中。显然，胰岛活化蛋白增强受体介导的GTP诱导的膜腺苷酸环化酶的活化，这是膜蛋白的ADP-核糖基化的结果，可能是受体-腺苷酸环化酶系统的一个组分。
GTP and isoproterenol activation of adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] in washed membranes prepared from [rat] C6 glioma cells was enhanced by incubation with islet-activating protein, one of the pertussis toxins [from Bordetella pertussis], if the incubation mixture was supplemented with NAD and ATP. The action of the protein was observed immediately after its addition and increased progressively in magnitude as the protein concentration or the incubation time increased. There was simultaneous incorporation of radioactivity from the ADP-ribose moiety of variously labeled NAD into the membrane protein with a MW of 41,000. Apparently islet-activating protein enhances receptor-mediated GTP-induced activation of membrane adenylate cyclase as a result of ADP-ribosylation of a membrane protein, probably 1 component of the receptor-adenylate cyclase system.