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Article: ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium- mobilizing metabolite from NADP +

TitleADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium- mobilizing metabolite from NADP +
Authors
KeywordsSpecies Index: Animalia
Aplysia
Issue Date1995
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1995, v. 270 n. 51, p. 30327-30333 How to Cite?
AbstractADP-ribosyl cyclase catalyzes the cyclization of NAD + to produce cyclic ADP-ribose (cADPR), which is emerging as an endogenous regulator of the Ca 2+-induced Ca 2+ release mechanism in cells. CD38 is a lymphocyte differentiation antigen which has recently been shown to be a bifunctional enzyme that can synthesize cADPR from NAD + as well as hydrolyze cADPR to ADP-ribose. In this study, we show that both the cyclase and CD38 can also catalyze the exchange of the nicotinamide group of NADP + with nicotinic acid (NA). The product is nicotinic acid adenine dinucleotide phosphate (NADP +), a metabolite we have previously shown to be potent in Ca 2+ mobilization (Lee, H. C., and Aarhus, R. (1995) J. Biol. Chem. 270, 2152-2157). The switch of the catalysis to the exchange reaction requires acidic pH and NA. The half-maximal effective concentration of NA is about 5 mM for both the cyclase and CD38. In the absence of NA or at neutral pH, the cyclase converts NADP + to another metabolite, which is identified as cyclic ADP-ribose 2'- phosphate. Under the same conditions, CD38 converts NADP + to ADP-ribose 2'- phosphate instead, which is the hydrolysis product of cyclic ADP-ribose 2'- phosphate. That two different products of ADP-ribosyl cyclase and CD38, cADPR and NAADP +, are both involved in Ca 2+ mobilization suggests a crucial role of these enzymes in Ca 2+ signaling.
Persistent Identifierhttp://hdl.handle.net/10722/132579
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorAarhus, Ren_HK
dc.contributor.authorGraeff, RMen_HK
dc.contributor.authorDickey, DMen_HK
dc.contributor.authorWalseth, TFen_HK
dc.contributor.authorHon Cheung Leeen_HK
dc.date.accessioned2011-03-28T09:26:29Z-
dc.date.available2011-03-28T09:26:29Z-
dc.date.issued1995en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1995, v. 270 n. 51, p. 30327-30333en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132579-
dc.description.abstractADP-ribosyl cyclase catalyzes the cyclization of NAD + to produce cyclic ADP-ribose (cADPR), which is emerging as an endogenous regulator of the Ca 2+-induced Ca 2+ release mechanism in cells. CD38 is a lymphocyte differentiation antigen which has recently been shown to be a bifunctional enzyme that can synthesize cADPR from NAD + as well as hydrolyze cADPR to ADP-ribose. In this study, we show that both the cyclase and CD38 can also catalyze the exchange of the nicotinamide group of NADP + with nicotinic acid (NA). The product is nicotinic acid adenine dinucleotide phosphate (NADP +), a metabolite we have previously shown to be potent in Ca 2+ mobilization (Lee, H. C., and Aarhus, R. (1995) J. Biol. Chem. 270, 2152-2157). The switch of the catalysis to the exchange reaction requires acidic pH and NA. The half-maximal effective concentration of NA is about 5 mM for both the cyclase and CD38. In the absence of NA or at neutral pH, the cyclase converts NADP + to another metabolite, which is identified as cyclic ADP-ribose 2'- phosphate. Under the same conditions, CD38 converts NADP + to ADP-ribose 2'- phosphate instead, which is the hydrolysis product of cyclic ADP-ribose 2'- phosphate. That two different products of ADP-ribosyl cyclase and CD38, cADPR and NAADP +, are both involved in Ca 2+ mobilization suggests a crucial role of these enzymes in Ca 2+ signaling.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subjectSpecies Index: Animaliaen_US
dc.subjectAplysiaen_US
dc.titleADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium- mobilizing metabolite from NADP +en_HK
dc.typeArticleen_HK
dc.identifier.emailGraeff, RM: graeffr@hku.hken_HK
dc.identifier.emailHon Cheung Lee: leehc@hku.hken_HK
dc.identifier.authorityGraeff, RM=rp01464en_HK
dc.identifier.authorityHon Cheung Lee=rp00545en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.270.51.30327en_HK
dc.identifier.pmid8530456-
dc.identifier.scopuseid_2-s2.0-0029616337en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029616337&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume270en_HK
dc.identifier.issue51en_HK
dc.identifier.spage30327en_HK
dc.identifier.epage30333en_HK
dc.identifier.isiWOS:A1995TL67500021-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridAarhus, R=6701339421en_HK
dc.identifier.scopusauthoridGraeff, RM=7003614053en_HK
dc.identifier.scopusauthoridDickey, DM=55292530300en_HK
dc.identifier.scopusauthoridWalseth, TF=7005424273en_HK
dc.identifier.scopusauthoridHon Cheung Lee=26642959100en_HK

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