Modification of cardiac membrane adenylate cyclase activity and Gs alpha by NAD and endogenous ADP-ribosyltransferase.
Modification of cardiac membrane adenylate cyclase activity and Gs alpha by NAD and endogenous ADP-ribosyltransferase.
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NAD 和内源 ADP-核糖基转移酶对心脏膜腺苷酸环化酶活性和 Gs α 的修饰。
DOI:
10.1006/jmcc.1994.1028
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发表时间:
1994
影响因子:
5
通讯作者:
Jacobson,MK
中科院分区:
文献类型:
--
作者:
Quist,EE;Coyle,DL;Vasan,R;Satumtira,N;Jacobson,EL;Jacobson,MK
The mechanism by which NAD stimulates cardiac adenylate cyclase was investigated. In highly purified canine cardiac sarcolemma, NAD stimulated adenylate cyclase activity in the presence of agents which activate GS(i.e. 5 mM AlF4-, 10 μM GTPγS. 10 μM GppNHp or isoproterenol plus 2 nM GTPγS). Furthermore the EC50of isoproterenol of stimulate adenylate cyclase was reduced in the presence of NAD. In membranes incubated with [32P]-NAD, AlF4-, 10 μM GTPγS or isoproterenol plus 2 nM GTPγS produced a selective increase in the radiolabeling of a single 45-kDA protein which was identified as GSαby immunoprecipitation. Cholera toxin catalysed radiolabeling of the same protein. Neutral hydroxylamine released [32P]-ADP-ribose from GSαprelabeled in the presence of AlF4-and [32P]-NAD indicating that an arginine residue on GSαwas modified by an endogenous ADP-ribosyltransferase. ADP-ribosyltransferase inhibitors, novobiocin, vitamin K1or 3-aminobenzamide, inhibited AlF4-stimulated ADP-ribosylation of GSαand NAD potentiation of adenylate cyclase with similar efficacies. The activity responsible for NAD potentiation of adenylate cyclase and ADP-ribosylation of GSαwas not removed under hypotonic or hypotonic conditions and therefore appears to be tightly membrane bound. Collectively, these observations indicate that canine cardiac sarcolemma possess and ADP-ribosyltransferase which may constitutively catalyse transfer of an ADP-ribose to activated GSα.