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Article: Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38

TitleFormation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38
Authors
Howard, MGrimaldi, JCBazan, JFLund, FESantosArgumedo, LParkhouse, RMEWalseth, TFHon Cheung Lee
Issue Date1993
PublisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.org
Citation
Science, 1993, v. 262 n. 5136, p. 1056-1059 How to Cite?
DOI: http://dx.doi.org/10.1126/science.8235624
AbstractCD38 is a 42-kilodalton glycoprotein expressed extensively on B and T lymphocytes. CD38 exhibits a structural homology to Aplysia adenosine diphosphate (ADP)-ribosyl cyclase. This enzyme catalyzes the synthesis of cyclic ADP-ribose (cADPR), a metabolite of nicotinamide adenine dinucleotide (NAD+) with calcium-mobilizing activity. A complementary DNA encoding the extracellular domain of murine CD38 was constructed and expressed, and the resultant recombinant soluble CD38 was purified to homogeneity. Soluble CD38 catalyzed the formation and hydrolysis of cADPR when added to NAD+. Purified cADPR augmented the proliferative response of activated murine B cells, potentially implicating the enzymatic activity of CD38 in lymphocyte function.
Persistent Identifierhttp://hdl.handle.net/10722/171598
ISSN
0036-8075
2022 Impact Factor: 56.9
2020 SCImago Journal Rankings: 12.556
ISI Accession Number ID
WOS:A1993MG18700036

 

DC FieldValueLanguage
dc.contributor.authorHoward, Men_US
dc.contributor.authorGrimaldi, JCen_US
dc.contributor.authorBazan, JFen_US
dc.contributor.authorLund, FEen_US
dc.contributor.authorSantosArgumedo, Len_US
dc.contributor.authorParkhouse, RMEen_US
dc.contributor.authorWalseth, TFen_US
dc.contributor.authorHon Cheung Leeen_US
dc.date.accessioned2012-10-30T06:15:55Z-
dc.date.available2012-10-30T06:15:55Z-
dc.date.issued1993en_US
dc.identifier.citationScience, 1993, v. 262 n. 5136, p. 1056-1059en_US
dc.identifier.issn0036-8075en_US
dc.identifier.urihttp://hdl.handle.net/10722/171598-
dc.description.abstractCD38 is a 42-kilodalton glycoprotein expressed extensively on B and T lymphocytes. CD38 exhibits a structural homology to Aplysia adenosine diphosphate (ADP)-ribosyl cyclase. This enzyme catalyzes the synthesis of cyclic ADP-ribose (cADPR), a metabolite of nicotinamide adenine dinucleotide (NAD+) with calcium-mobilizing activity. A complementary DNA encoding the extracellular domain of murine CD38 was constructed and expressed, and the resultant recombinant soluble CD38 was purified to homogeneity. Soluble CD38 catalyzed the formation and hydrolysis of cADPR when added to NAD+. Purified cADPR augmented the proliferative response of activated murine B cells, potentially implicating the enzymatic activity of CD38 in lymphocyte function.en_US
dc.languageengen_US
dc.publisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.orgen_US
dc.relation.ispartofScienceen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Metabolism - Pharmacologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Isolation & Purification - Metabolismen_US
dc.subject.meshB-Lymphocytes - Drug Effects - Metabolismen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshLymphocyte Activationen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshN-Glycosyl Hydrolases - Metabolismen_US
dc.subject.meshNad - Metabolismen_US
dc.subject.meshRecombinant Proteins - Metabolismen_US
dc.titleFormation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38en_US
dc.typeArticleen_US
dc.identifier.emailHon Cheung Lee:leehc@hku.hken_US
dc.identifier.authorityHon Cheung Lee=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1126/science.8235624-
dc.identifier.pmid8235624-
dc.identifier.scopuseid_2-s2.0-0027763586en_US
dc.identifier.volume262en_US
dc.identifier.issue5136en_US
dc.identifier.spage1056en_US
dc.identifier.epage1059en_US
dc.identifier.isiWOS:A1993MG18700036-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridHoward, M=7402455148en_US
dc.identifier.scopusauthoridGrimaldi, JC=35821610600en_US
dc.identifier.scopusauthoridBazan, JF=7006614128en_US
dc.identifier.scopusauthoridLund, FE=7006541851en_US
dc.identifier.scopusauthoridSantosArgumedo, L=7003756424en_US
dc.identifier.scopusauthoridParkhouse, RME=7102481729en_US
dc.identifier.scopusauthoridWalseth, TF=7005424273en_US
dc.identifier.scopusauthoridHon Cheung Lee=26642959100en_US
dc.identifier.issnl0036-8075-

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