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Article: Identification of cyclic ADP-ribose-binding proteins by photoaffinity labeling

TitleIdentification of cyclic ADP-ribose-binding proteins by photoaffinity labeling
Authors
Issue Date1993
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, 1993, v. 268 n. 35, p. 26686-26691 How to Cite?
AbstractWe have synthesized 8-azido-cyclic ADP-ribose (8N3-cADPR) and [32P]8- azido-cyclic ADP-ribose ([32P]8N3-cADPR) in order to characterize cyclic ADP-ribose-(cADPR) binding sites in sea urchin egg homogenates. 8N3-cADPR was an antagonist of cADPR since it did not induce Ca2+ release from egg microsomes but did inhibit the ability of cADPR to do so. The effect of 8N3- cADPR was reversible and could be overcome by high concentrations of cADPR, suggesting that both were acting on the same site. This was supported by the fact that 8N3-cADPR effectively competed for [32P]cADPR binding to microsomes. Reciprocally, binding of [32P]8N3-cADPR could also be selectively displaced by cADPR and 8N3-cADPR, but not by ADP-ribose. These results indicate that 8N3-cADPR binds specifically to the cADPR-binding sites and inhibits cADPR from releasing Ca2+. Photolysis of microsomes preincubated with [32P]8N3-cADPR resulted in specific labeling of proteins of 140 and 100 kDa, which could be prevented by 8N3-cADPR or nanomolar concentrations of cADPR, but not by micromolar concentrations of ADP-ribose, AMP, ADP, ATP, cyclic AMP or inositol 1,4,5-trisphosphate. Caffeine, an agonist of Ca2+-induced Ca2+ release, preferentially inhibited the labeling of the 100 kDa as compared to the 140-kDa protein. These results suggest that cADPR may not interact directly with the ryanodine receptor, but may instead, exert its effect through intermediate proteins.
Persistent Identifierhttp://hdl.handle.net/10722/171593
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWalseth, TFen_US
dc.contributor.authorAarhus, Ren_US
dc.contributor.authorKerr, JAen_US
dc.contributor.authorHon Cheung Leeen_US
dc.date.accessioned2012-10-30T06:15:52Z-
dc.date.available2012-10-30T06:15:52Z-
dc.date.issued1993en_US
dc.identifier.citationJournal Of Biological Chemistry, 1993, v. 268 n. 35, p. 26686-26691en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/171593-
dc.description.abstractWe have synthesized 8-azido-cyclic ADP-ribose (8N3-cADPR) and [32P]8- azido-cyclic ADP-ribose ([32P]8N3-cADPR) in order to characterize cyclic ADP-ribose-(cADPR) binding sites in sea urchin egg homogenates. 8N3-cADPR was an antagonist of cADPR since it did not induce Ca2+ release from egg microsomes but did inhibit the ability of cADPR to do so. The effect of 8N3- cADPR was reversible and could be overcome by high concentrations of cADPR, suggesting that both were acting on the same site. This was supported by the fact that 8N3-cADPR effectively competed for [32P]cADPR binding to microsomes. Reciprocally, binding of [32P]8N3-cADPR could also be selectively displaced by cADPR and 8N3-cADPR, but not by ADP-ribose. These results indicate that 8N3-cADPR binds specifically to the cADPR-binding sites and inhibits cADPR from releasing Ca2+. Photolysis of microsomes preincubated with [32P]8N3-cADPR resulted in specific labeling of proteins of 140 and 100 kDa, which could be prevented by 8N3-cADPR or nanomolar concentrations of cADPR, but not by micromolar concentrations of ADP-ribose, AMP, ADP, ATP, cyclic AMP or inositol 1,4,5-trisphosphate. Caffeine, an agonist of Ca2+-induced Ca2+ release, preferentially inhibited the labeling of the 100 kDa as compared to the 140-kDa protein. These results suggest that cADPR may not interact directly with the ryanodine receptor, but may instead, exert its effect through intermediate proteins.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.meshAdenosine Diphosphate Ribose - Analogs & Derivatives - Chemical Synthesis - Metabolismen_US
dc.subject.meshAffinity Labelsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshOvumen_US
dc.subject.meshPhotochemistryen_US
dc.subject.meshProteins - Analysisen_US
dc.subject.meshSea Urchinsen_US
dc.titleIdentification of cyclic ADP-ribose-binding proteins by photoaffinity labelingen_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.pmid8253802-
dc.identifier.scopuseid_2-s2.0-0027508133en_US
dc.identifier.volume268en_US
dc.identifier.issue35en_US
dc.identifier.spage26686en_US
dc.identifier.epage26691en_US
dc.identifier.isiWOS:A1993MK42500098-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWalseth, TF=7005424273en_US
dc.identifier.scopusauthoridAarhus, R=6701339421en_US
dc.identifier.scopusauthoridKerr, JA=7401909403en_US
dc.identifier.scopusauthoridHon Cheung Lee=26642959100en_US

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