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Article: Comparison of Ca2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate

TitleComparison of Ca2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate
Authors
Issue Date1990
PublisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/
Citation
Molecular Biology Of The Cell, 1990, v. 1 n. 3, p. 279-290 How to Cite?
AbstractWe have previously shown that a metabolite of NAD+ generated by an enzyme present in sea urchin eggs and mammalian tissues can mobilize intracellular Ca2+ in the eggs. Structural determination established it to be a cyclized ADP-ribose, and the name cyclic ADP-ribose (cADPR) has been proposed. In this study, Ca2+ mobilizations induced by cADPR and inositol trisphosphate (IP3) in sea urchin egg homogenates were monitored with Ca2+ indicators and Ca2+-specific electrodes. Both methods showed that cADPR can release Ca2+ from egg homogenates. Evidence indicated that it did not act as a nonspecific Ca2+-ionophore or as a blocker of the microsomal Ca2+-transport; instead, it was likely to be operating through a specific receptor system. This was supported by its half-maximal effective concentration of 18 nM, which was 7 times lower than that of IP3. The receptor for cADPR appeared to be different from that of IP3 because heparin, an inhibitor of IP3 binding, had no effect on the cADPR action. The Ca2+ releases induced by cADPR and IP3 were not additive and had an inverse relationship, indicating overlapping stores were mobilized. Microinjection of cADPR into intact eggs induced transient intracellular Ca2+ changes and activated the cortical reaction. The in vivo effectiveness of cADPR was directly comparable with IP3 and neither required external Ca2+. In addition, both were effective in activating the eggs to undergo multiple nuclear cycles and DNA synthesis. These results suggest that cADPR could function as a second messenger in sea urchin eggs. © 1990 by The American Society for Cell Biology.
Persistent Identifierhttp://hdl.handle.net/10722/171738
ISSN
2015 Impact Factor: 4.037
2015 SCImago Journal Rankings: 3.665

 

DC FieldValueLanguage
dc.contributor.authorDargie, PJen_US
dc.contributor.authorAgre, MCen_US
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:42Z-
dc.date.available2012-10-30T06:16:42Z-
dc.date.issued1990en_US
dc.identifier.citationMolecular Biology Of The Cell, 1990, v. 1 n. 3, p. 279-290en_US
dc.identifier.issn1059-1524en_US
dc.identifier.urihttp://hdl.handle.net/10722/171738-
dc.description.abstractWe have previously shown that a metabolite of NAD+ generated by an enzyme present in sea urchin eggs and mammalian tissues can mobilize intracellular Ca2+ in the eggs. Structural determination established it to be a cyclized ADP-ribose, and the name cyclic ADP-ribose (cADPR) has been proposed. In this study, Ca2+ mobilizations induced by cADPR and inositol trisphosphate (IP3) in sea urchin egg homogenates were monitored with Ca2+ indicators and Ca2+-specific electrodes. Both methods showed that cADPR can release Ca2+ from egg homogenates. Evidence indicated that it did not act as a nonspecific Ca2+-ionophore or as a blocker of the microsomal Ca2+-transport; instead, it was likely to be operating through a specific receptor system. This was supported by its half-maximal effective concentration of 18 nM, which was 7 times lower than that of IP3. The receptor for cADPR appeared to be different from that of IP3 because heparin, an inhibitor of IP3 binding, had no effect on the cADPR action. The Ca2+ releases induced by cADPR and IP3 were not additive and had an inverse relationship, indicating overlapping stores were mobilized. Microinjection of cADPR into intact eggs induced transient intracellular Ca2+ changes and activated the cortical reaction. The in vivo effectiveness of cADPR was directly comparable with IP3 and neither required external Ca2+. In addition, both were effective in activating the eggs to undergo multiple nuclear cycles and DNA synthesis. These results suggest that cADPR could function as a second messenger in sea urchin eggs. © 1990 by The American Society for Cell Biology.en_US
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/en_US
dc.relation.ispartofMolecular Biology of the Cellen_US
dc.titleComparison of Ca2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphateen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-27244462501en_US
dc.identifier.volume1en_US
dc.identifier.issue3en_US
dc.identifier.spage279en_US
dc.identifier.epage290en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDargie, PJ=6602429343en_US
dc.identifier.scopusauthoridAgre, MC=6603547827en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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