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- Scopus: eid_2-s2.0-0027508133
- PMID: 8253802
- WOS: WOS:A1993MK42500098
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Article: Identification of cyclic ADP-ribose-binding proteins by photoaffinity labeling
Title | Identification of cyclic ADP-ribose-binding proteins by photoaffinity labeling |
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Authors | |
Issue Date | 1993 |
Publisher | American 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? |
Abstract | We 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 Identifier | http://hdl.handle.net/10722/171593 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Walseth, TF | en_US |
dc.contributor.author | Aarhus, R | en_US |
dc.contributor.author | Kerr, JA | en_US |
dc.contributor.author | Hon Cheung Lee | en_US |
dc.date.accessioned | 2012-10-30T06:15:52Z | - |
dc.date.available | 2012-10-30T06:15:52Z | - |
dc.date.issued | 1993 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 1993, v. 268 n. 35, p. 26686-26691 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171593 | - |
dc.description.abstract | We 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.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Adenosine Diphosphate Ribose - Analogs & Derivatives - Chemical Synthesis - Metabolism | en_US |
dc.subject.mesh | Affinity Labels | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Binding Sites | en_US |
dc.subject.mesh | Calcium - Metabolism | en_US |
dc.subject.mesh | Cyclic Adp-Ribose | en_US |
dc.subject.mesh | Ovum | en_US |
dc.subject.mesh | Photochemistry | en_US |
dc.subject.mesh | Proteins - Analysis | en_US |
dc.subject.mesh | Sea Urchins | en_US |
dc.title | Identification of cyclic ADP-ribose-binding proteins by photoaffinity labeling | en_US |
dc.type | Article | en_US |
dc.identifier.email | Hon Cheung Lee:leehc@hku.hk | en_US |
dc.identifier.authority | Hon Cheung Lee=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.pmid | 8253802 | - |
dc.identifier.scopus | eid_2-s2.0-0027508133 | en_US |
dc.identifier.volume | 268 | en_US |
dc.identifier.issue | 35 | en_US |
dc.identifier.spage | 26686 | en_US |
dc.identifier.epage | 26691 | en_US |
dc.identifier.isi | WOS:A1993MK42500098 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Walseth, TF=7005424273 | en_US |
dc.identifier.scopusauthorid | Aarhus, R=6701339421 | en_US |
dc.identifier.scopusauthorid | Kerr, JA=7401909403 | en_US |
dc.identifier.scopusauthorid | Hon Cheung Lee=26642959100 | en_US |
dc.identifier.issnl | 0021-9258 | - |