Abstract
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 β-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.
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Galione, A., White, A., Willmott, N. et al. cGMP mobilizes intracellular Ca2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis. Nature 365, 456–459 (1993). https://doi.org/10.1038/365456a0
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DOI: https://doi.org/10.1038/365456a0
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