Aa. Genazzani et al., UNIQUE INACTIVATION PROPERTIES OF NAADP-SENSITIVE CA2+ RELEASE, The Journal of biological chemistry, 271(20), 1996, pp. 11599-11602
Ca2+ mobilization from intracellular stores constitutes an important m
echanism for generating cytoplasmic Ca2+ signals. Inositol trisphospha
te (InsP(3)) and ryanodine receptors are the two families of intracell
ular Ca2+ release channels that have been identified, which may be reg
ulated by separate intracellular messengers, InsP(3) and cyclic adenos
ine 5'-diphosphate ribose, respectively. A third molecule, nicotinic a
cid adenine dinucleotide phosphate (NAADP), has recently been recogniz
ed as a potent Ca2+ releasing agent in sea urchin eggs and microsomes.
We now report that non-releasing concentrations of NAADP fully and ir
reversibly inactivate the NAADP-sensitive Ca2+ release mechanism. This
phenomenon occurred both in intact sea urchin eggs and in homogenates
and is not shared by either InsP(3) or cyclic adenosine 5'-diphosphat
e ribose, The novel properties of this Ca2+ release mechanism, giving
a one-shot Ca2+ release, may be suited to irreversible cellular events
.