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Article: Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes

TitleProduction and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes
Authors
Issue Date1993
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 1993, v. 191 n. 2, p. 639-645 How to Cite?
AbstractHemoglobin-free membranes from human erythrocytes are able to convert β- NAD+ to cyclic ADP-ribose, a calcium mobilizer as potent as inositol 1,4,5- trisphosphate. Identification of cyclic ADP-ribose was based on HPLC analyses and its Ca2+-mobilizing activity on sea urchin egg microsomes. Erythrocyte membranes also hydrolyze cyclic ADP-ribose to ADP-ribose. By comparing the cyclic ADP-ribose-synthesizing and hydrolyzing activities on unsealed and right-side-out resealed ghosts, it can be concluded that both are localized at the extracellular side of the membrane. This is confirmed by the demonstration of both enzyme activities on the surface of intact human red cells. Identification of the two enzymes involved in cyclic ADP-ribose metabolism might suggest some physiological role of this nucleotide in red cells.
Persistent Identifierhttp://hdl.handle.net/10722/171575
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHon Cheung Leeen_US
dc.contributor.authorZocchi, Een_US
dc.contributor.authorGuida, Len_US
dc.contributor.authorFranco, Len_US
dc.contributor.authorBenatti, Uen_US
dc.contributor.authorDe Flora, Aen_US
dc.date.accessioned2012-10-30T06:15:45Z-
dc.date.available2012-10-30T06:15:45Z-
dc.date.issued1993en_US
dc.identifier.citationBiochemical And Biophysical Research Communications, 1993, v. 191 n. 2, p. 639-645en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/171575-
dc.description.abstractHemoglobin-free membranes from human erythrocytes are able to convert β- NAD+ to cyclic ADP-ribose, a calcium mobilizer as potent as inositol 1,4,5- trisphosphate. Identification of cyclic ADP-ribose was based on HPLC analyses and its Ca2+-mobilizing activity on sea urchin egg microsomes. Erythrocyte membranes also hydrolyze cyclic ADP-ribose to ADP-ribose. By comparing the cyclic ADP-ribose-synthesizing and hydrolyzing activities on unsealed and right-side-out resealed ghosts, it can be concluded that both are localized at the extracellular side of the membrane. This is confirmed by the demonstration of both enzyme activities on the surface of intact human red cells. Identification of the two enzymes involved in cyclic ADP-ribose metabolism might suggest some physiological role of this nucleotide in red cells.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_US
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Biosynthesis - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cden_US
dc.subject.meshAntigens, Cd38en_US
dc.subject.meshAntigens, Differentiation - Metabolismen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshErythrocyte Membrane - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrolysisen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMicrosomes - Metabolismen_US
dc.subject.meshN-Glycosyl Hydrolases - Metabolismen_US
dc.subject.meshNad - Metabolismen_US
dc.subject.meshOvumen_US
dc.subject.meshSea Urchinsen_US
dc.titleProduction and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytesen_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.doi10.1006/bbrc.1993.1265en_US
dc.identifier.pmid8461019-
dc.identifier.scopuseid_2-s2.0-0027240645en_US
dc.identifier.volume191en_US
dc.identifier.issue2en_US
dc.identifier.spage639en_US
dc.identifier.epage645en_US
dc.identifier.isiWOS:A1993KT12800046-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridHon Cheung Lee=26642959100en_US
dc.identifier.scopusauthoridZocchi, E=7003441674en_US
dc.identifier.scopusauthoridGuida, L=7006059917en_US
dc.identifier.scopusauthoridFranco, L=35412467500en_US
dc.identifier.scopusauthoridBenatti, U=7005696019en_US
dc.identifier.scopusauthoridDe Flora, A=7006450815en_US

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