cGMP mobilizes intracellular Ca2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis

Nature. 1993 Sep 30;365(6445):456-9. doi: 10.1038/365456a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / analogs & derivatives*
  • Adenosine Diphosphate Ribose / biosynthesis
  • Aniline Compounds
  • Animals
  • Calcium / metabolism*
  • Cyclic ADP-Ribose
  • Cyclic GMP / metabolism*
  • Fluorometry
  • In Vitro Techniques
  • Microsomes / metabolism
  • NAD / metabolism
  • Ovum
  • Ruthenium Red
  • Sea Urchins
  • Signal Transduction
  • Xanthenes


  • Aniline Compounds
  • Xanthenes
  • NAD
  • Ruthenium Red
  • Cyclic ADP-Ribose
  • Adenosine Diphosphate Ribose
  • Fluo-3
  • Cyclic GMP
  • Calcium