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Article: CD38 and ADP-ribosyl cyclase catalyze the synthesis of a dimeric ADP- ribose that potentiates the calcium-mobilizing activity of cyclic ADP-ribose

TitleCD38 and ADP-ribosyl cyclase catalyze the synthesis of a dimeric ADP- ribose that potentiates the calcium-mobilizing activity of cyclic ADP-ribose
Authors
Issue Date1997
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, 1997, v. 272 n. 20, p. 12945-12951 How to Cite?
AbstractCD38, a lymphocyte differentiation antigen, is also a bifunctional enzyme catalyzing the synthesis of cyclic ADP-ribose (cADPR) from NAD+ and its hydrolysis to ADP-ribose (ADPR). An additional enzymatic activity of CD38 shared by monofunctional ADP-ribosyl cyclase from Aplysia californica is the exchange of the base group of NAD+ (nicotinamide) with various nucleophiles. Both human CD38 (either recombinant or purified from erythrocyte membranes) and Aplysia cyclase were found to catalyze the exchange of ADPR with the nicotinamide group of NAD+ leading to the formation of a dimeric ADPR ((ADPR)2). The dimeric structure of the enzymatic product, which was generated by recombinant CD38 and by CD38+ Namalwa cells from as low as 10 μM NAD+, was demonstrated using specific enzyme treatments (dinucleotide pyrophosphatase and 5'-nucleotidase) and mass spectrometry analyses of the resulting products. The linkage between the two ADPR units of (ADPR)2 was identified as that between the N1 of the adenine nucleus of one ADPR unit and the anomeric carbon of the terminal ribose of the second ADPR molecule by enzymatic analyses and by comparison with patterns of cADPR cleavage with Me2SO:tert-butoxide. Although (ADPR)2 itself did not release Ca2+ from sea urchin egg microsomal vesicles, it specifically potentiated the Ca2+ - releasing activity of subthreshold concentrations of cADPR. Therefore, (ADPR)2 is a new product of CD38 that amplifies the Ca2+-mobilizing activity of cADPR.
Persistent Identifierhttp://hdl.handle.net/10722/171637
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDe Flora, Aen_US
dc.contributor.authorGuida, Len_US
dc.contributor.authorFranco, Len_US
dc.contributor.authorZocchi, Een_US
dc.contributor.authorBruzzone, Sen_US
dc.contributor.authorBenatti, Uen_US
dc.contributor.authorDamonte, Gen_US
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:05Z-
dc.date.available2012-10-30T06:16:05Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Biological Chemistry, 1997, v. 272 n. 20, p. 12945-12951en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/171637-
dc.description.abstractCD38, a lymphocyte differentiation antigen, is also a bifunctional enzyme catalyzing the synthesis of cyclic ADP-ribose (cADPR) from NAD+ and its hydrolysis to ADP-ribose (ADPR). An additional enzymatic activity of CD38 shared by monofunctional ADP-ribosyl cyclase from Aplysia californica is the exchange of the base group of NAD+ (nicotinamide) with various nucleophiles. Both human CD38 (either recombinant or purified from erythrocyte membranes) and Aplysia cyclase were found to catalyze the exchange of ADPR with the nicotinamide group of NAD+ leading to the formation of a dimeric ADPR ((ADPR)2). The dimeric structure of the enzymatic product, which was generated by recombinant CD38 and by CD38+ Namalwa cells from as low as 10 μM NAD+, was demonstrated using specific enzyme treatments (dinucleotide pyrophosphatase and 5'-nucleotidase) and mass spectrometry analyses of the resulting products. The linkage between the two ADPR units of (ADPR)2 was identified as that between the N1 of the adenine nucleus of one ADPR unit and the anomeric carbon of the terminal ribose of the second ADPR molecule by enzymatic analyses and by comparison with patterns of cADPR cleavage with Me2SO:tert-butoxide. Although (ADPR)2 itself did not release Ca2+ from sea urchin egg microsomal vesicles, it specifically potentiated the Ca2+ - releasing activity of subthreshold concentrations of cADPR. Therefore, (ADPR)2 is a new product of CD38 that amplifies the Ca2+-mobilizing activity of cADPR.en_US
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_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Chemistry - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Chemistry - Metabolismen_US
dc.subject.meshAplysiaen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCalcium - Chemistry - Metabolismen_US
dc.subject.meshErythrocyte Membrane - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshN-Glycosyl Hydrolases - Chemistry - Metabolismen_US
dc.titleCD38 and ADP-ribosyl cyclase catalyze the synthesis of a dimeric ADP- ribose that potentiates the calcium-mobilizing activity of cyclic ADP-riboseen_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.doi10.1074/jbc.272.20.12945en_US
dc.identifier.pmid9148900-
dc.identifier.scopuseid_2-s2.0-0030977394en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030977394&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume272en_US
dc.identifier.issue20en_US
dc.identifier.spage12945en_US
dc.identifier.epage12951en_US
dc.identifier.isiWOS:A1997WZ38400013-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDe Flora, A=7006450815en_US
dc.identifier.scopusauthoridGuida, L=7006059917en_US
dc.identifier.scopusauthoridFranco, L=35412467500en_US
dc.identifier.scopusauthoridZocchi, E=7003441674en_US
dc.identifier.scopusauthoridBruzzone, S=7004633756en_US
dc.identifier.scopusauthoridBenatti, U=7005696019en_US
dc.identifier.scopusauthoridDamonte, G=7003906406en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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