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(Received for publication, October 31, 1995; and in revised form, December 7, 1995)
Cyclic adenosine diphosphate ribose (cADPR) is a potent
endogenous calcium-mobilizing agent synthesized from
-NAD by ADP-ribosyl cyclases in sea urchin eggs
and in several mammalian cells (Galione, A., and White, A.(1994) Trends Cell Biol. 4, 431-436). Pharmacological studies
suggest that cADPR is an endogenous modulator of
Ca
-induced Ca
release mediated by
ryanodine-sensitive Ca
release channels. An
unresolved question is whether cADPR can act as a
Ca
-mobilizing intracellular messenger. We show that
exogenous application of nitric oxide (NO) mobilizes Ca
from intracellular stores in intact sea urchin eggs and that it
releases Ca
and elevates cADPR levels in egg
homogenates. 8-Amino-cADPR, a selective competitive antagonist of
cADPR-mediated Ca
release, and nicotinamide, an
inhibitor of ADP-ribosyl cyclase, inhibit the
Ca
-mobilizing actions of NO, while, heparin, a
competitive antagonist of the inositol 1,4,5-trisphosphate receptor,
did not affect NO-induced Ca
release. Since the
Ca
-mobilizing effects of NO can be mimicked by cGMP,
are inhibited by the cGMP-dependent-protein kinase inhibitor, R
-8-pCPT-cGMPS, and in egg homogenates show a
requirement for the guanylyl cyclase substrate, GTP, we suggest a novel
action of NO in mobilizing intracellular calcium from microsomal stores
via a signaling pathway involving cGMP and cADPR. These results suggest
that cADPR has the capacity to act as a Ca-mobilizing
intracellular messenger.
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