CGMP MOBILIZES INTRACELLULAR CA2+ IN SEA-URCHIN EGGS BY STIMULATING CYCLIC ADP-RIBOSE SYNTHESIS
CGMP MOBILIZES INTRACELLULAR CA2+ IN SEA-URCHIN EGGS BY STIMULATING CYCLIC ADP-RIBOSE SYNTHESIS
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DOI：
10.1038/365456a0
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发表时间：
1993-09-30
期刊：
影响因子：
64.8
通讯作者：
WATSON, SP
中科院分区：
文献类型：
--
作者：
GALIONE, A;WHITE, A;WATSON, SP
许多激素或神经递质作用于细胞表面受体，以增加细胞内游离钙浓度，引发广泛的细胞反应1。由于这种Ca 2+的来源通常是内部储存，因此需要额外的信使来传递来自质膜的激素信息。环ADP-核糖（cADPR）已被认为是海胆卵和几种哺乳动物细胞类型中ryanodine受体诱导的Ca 2+释放的内源性激活剂2 - 8，22。cADPR的第二信使作用要求其细胞内水平受到细胞外刺激的控制。在这里，我们证明了3 '，5'-环鸟苷一磷酸（cGMP）通过激活海胆卵和卵匀浆中的合成酶ADP-核糖基环化酶9 -11刺激β-NAD+合成cADPR的新作用。我们认为cADPR可能抑制细胞表面受体或与cGMP产生相关的气体递质产生的信号。
MANY hormones or neurotransmitters act at cell surface receptors to increase the intracellular free calcium concentration, triggering a wide range of cellular responses1. As the source of this Ca2+ is often internal stores, additional messengers are required to convey the hormonal message from the plasma membrane. Cyclic ADP-ribose (cADPR) has been proposed as the endogenous activator of Ca2+-induced Ca2+ release by the ryanodine receptor in sea urchin eggs and in several mammalian cell types2-8,22. A second messenger role for cADPR requires that its intracellular levels be under the control of extracellular stimuli. Here we demonstrate a novel action of 3',5'-cyclic guanosine monophosphate (cGMP) in stimulating the synthesis of cADPR from beta-NAD+ by activating its synthetic enzyme ADP-ribosyl cyclase9-11 in sea urchin eggs and egg homogenates. We suggest that cADPR may transduce signals generated by cell surface receptors or gaseous transmitters linked to cGMP production.