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J. Biol. Chem. 275 (12): 8301-8306
© 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
J Biol Chem, Vol. 275, Issue 12, 8301-8306, March 24, 2000
Nicotinic Acid Adenine Dinucleotide Phosphate-induced
Ca2+ Release
INTERACTIONS AMONG DISTINCT Ca2+ MOBILIZING
MECHANISMS IN STARFISH OOCYTES*
Luigia
Santella ,
Keiichiro
Kyozuka§,
Armando A.
Genazzani¶,
Laura
De Riso , and
Ernesto
Carafoli **
From the Laboratory of Cell Biology Stazione
Zoologica "A. Dohrn" Villa Comunale, I-80121, Napoli, Italy, the
§ Asamushi Marine Biological Station, Asamushi, Aomori
039-3501, Japan, the ¶ Department of Pharmacology, Tennis Court
Road, Cambridge, CB2 1QJ United Kingdom, and the Department of
Biochemistry, University of Padova, 35121 Padova, Italy
An intracellular mechanism activated by nicotinic
acid adenine dinucleotide phosphate (NAADP+)
contributes to intracellular Ca2+ release alongside
inositol 1,4,5-trisphosphate (Ins-P3) and ryanodine receptors. The NAADP+-sensitive mechanism has been shown to
be operative in sea urchin eggs, ascidian eggs, and pancreatic acinar
cells. Furthermore, most mammalian cell types can synthesize
NAADP+, with nicotinic acid and NADP+ as
precursors. In this contribution, NAADP+-induced
Ca2+ release has been investigated in starfish oocytes.
Uncaging of injected NAADP+ induced Ca2+
mobilization in both immature oocytes and in oocytes matured by the
hormone 1-methyladenine (1-MA). The role of extracellular Ca2+ in NAADP+-induced Ca2+
mobilization, which was minor in immature oocytes, was instead essential in mature oocytes. Thus, the NAADP+-sensitive
Ca2+ pool, which is known to be distinct from those
sensitive to inositol 1,4,5-trisphosphate or cyclic ADPribose,
apparently migrated closer to (or became part of) the plasma membrane
during the maturation process. Inhibition of both Ins-P3
and ryanodine receptors, but not of either alone, substantially
inhibited NAADP+-induced Ca2+ mobilization in
both immature and mature oocytes. The data also suggest that
NAADP+-induced Ca2+ mobilization acted as a
trigger for Ca2+ release via Ins-P3 and
ryanodine receptors.
*
This work was made possible by the financial contributions
of the Japan Society for the promotion of Science and the National Research Council of Italy (to L. S.), of the Italian Ministry of
Scientific Research (M.U.R.S.T., P.R.I.N. 1998, to E. C.), of the
National Research Council of Italy (Target Project of Biochemistry), and of the European Molecular Biology Organization (to A. A. G.). The
support of Telethon (Grant 963) is also gratefully acknowledged.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
**
To whom correspondence should be addressed: Dept. of Biochemistry,
University of Padova, Viale G. Colombo 3, 35121, Padova, Italy. Tel.:
0039-049-8276137; Fax: 0039-049-8276125.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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