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Many hormones or neurotransmitters act at cell surface receptors to increase the intracellular free calcium concentration, triggering a wide range of cellular responses. 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 Ca(2+)-induced Ca2+ release by the ryanodine receptor in sea urchin eggs and in several mammalian cell types. 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 cyclase 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.

Original publication

DOI

10.1038/365456a0

Type

Journal article

Journal

Nature

Publication Date

30/09/1993

Volume

365

Pages

456 - 459

Keywords

Adenosine Diphosphate Ribose, Aniline Compounds, Animals, Calcium, Cyclic ADP-Ribose, Cyclic GMP, Fluorometry, In Vitro Techniques, Microsomes, NAD, Ovum, Ruthenium Red, Sea Urchins, Signal Transduction, Xanthenes