J Biol Chem 1996 May 17;27120:11599-602. doi: 10.1074/jbc.271.20.11599.

Unique inactivation properties of NAADP-sensitive Ca2+ release.

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Ca2+ mobilization from intracellular stores constitutes an important mechanism for generating cytoplasmic Ca2+ signals. Inositol trisphosphate (InsP3) and ryanodine receptors are the two families of intracellular Ca2+ release channels that have been identified, which may be regulated by separate intracellular messengers, InsP3, and cyclic adenosine 5''-diphosphate ribose, respectively. A third molecule, nicotinic acid adenine dinucleotide phosphate (NAADP), has recently been recognized as a potent Ca2+ releasing agent in sea urchin eggs and microsomes. We now report that non-releasing concentrations of NAADP fully and irreversibly 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 InsP3 or cyclic adenosine 5''-diphosphate ribose. The novel properties of this Ca2+ release mechanism, giving a one-shot Ca2+ release, may be suited to irreversible cellular events.

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Genes referenced: LOC100887844 LOC115919080 LOC576539