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Article: Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose

TitlePotentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose
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. 1, p. 293-299 How to Cite?
AbstractCyclic ADP-ribose (cADPR) is a naturally occurring metabolite of NAD+ that is as potent as inositol 1,4,5-trisphosphate (IP3) in mobilizing Ca2+ in sea urchin eggs. Previous pharmacological evidence suggests that cADPR acts through a system similar to the Ca2+-induced Ca2+ release (CICR). Here I showed that in the presence of low concentrations of cADPR addition of Ca2+ to egg homogenates stimulated further release of Ca2+ in a concentration-dependent manner. In the absence of cADPR, no induced release was seen, and the added Ca2+ was, instead, sequestered by a thapsigargin- sensitive transport system. High concentrations of strontium (>50 μM) could also induce Ca2+ release. The effective concentrations of Sr2+, however, were reduced 10-20-fold in the presence of low concentrations of cADPR. Barium, at up to 0.4 mM, did not stimulate Ca2+ release with or without cADPR. The potentiation between divalent cations and cADPR was mutual since the Ca2+ releasing activity of cADPR was also increased in the presence of strontium. Ionomycin and thapsigargin both released Ca2+ but neither potentiated Ca2+ release induced by divalent cations. Caffeine also released Ca2+ in a concentration-dependent manner, and its potency was greatly increased by low concentrations of cADPR, while no such simulation was seen with IP3. Conversely, low concentrations of caffeine that were not sufficient to release Ca2+ increased the effectiveness of cADPR 10-fold. Isocaffeine, an isomer of caffeine, was four to five times less effective, demonstrating the specificity of the caffeine effect. These results suggest that cADPR can function as an endogenous regulator of CICR in eggs.
Persistent Identifierhttp://hdl.handle.net/10722/171594
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHon Cheung Leeen_US
dc.date.accessioned2012-10-30T06:15:53Z-
dc.date.available2012-10-30T06:15:53Z-
dc.date.issued1993en_US
dc.identifier.citationJournal Of Biological Chemistry, 1993, v. 268 n. 1, p. 293-299en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/171594-
dc.description.abstractCyclic ADP-ribose (cADPR) is a naturally occurring metabolite of NAD+ that is as potent as inositol 1,4,5-trisphosphate (IP3) in mobilizing Ca2+ in sea urchin eggs. Previous pharmacological evidence suggests that cADPR acts through a system similar to the Ca2+-induced Ca2+ release (CICR). Here I showed that in the presence of low concentrations of cADPR addition of Ca2+ to egg homogenates stimulated further release of Ca2+ in a concentration-dependent manner. In the absence of cADPR, no induced release was seen, and the added Ca2+ was, instead, sequestered by a thapsigargin- sensitive transport system. High concentrations of strontium (>50 μM) could also induce Ca2+ release. The effective concentrations of Sr2+, however, were reduced 10-20-fold in the presence of low concentrations of cADPR. Barium, at up to 0.4 mM, did not stimulate Ca2+ release with or without cADPR. The potentiation between divalent cations and cADPR was mutual since the Ca2+ releasing activity of cADPR was also increased in the presence of strontium. Ionomycin and thapsigargin both released Ca2+ but neither potentiated Ca2+ release induced by divalent cations. Caffeine also released Ca2+ in a concentration-dependent manner, and its potency was greatly increased by low concentrations of cADPR, while no such simulation was seen with IP3. Conversely, low concentrations of caffeine that were not sufficient to release Ca2+ increased the effectiveness of cADPR 10-fold. Isocaffeine, an isomer of caffeine, was four to five times less effective, demonstrating the specificity of the caffeine effect. These results suggest that cADPR can function as an endogenous regulator of CICR in eggs.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 - Pharmacologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBarium - Pharmacologyen_US
dc.subject.meshCaffeine - Pharmacologyen_US
dc.subject.meshCalcium - Metabolism - Pharmacologyen_US
dc.subject.meshCations, Divalenten_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshDrug Synergismen_US
dc.subject.meshFemaleen_US
dc.subject.meshKineticsen_US
dc.subject.meshOvum - Drug Effects - Metabolismen_US
dc.subject.meshSea Urchinsen_US
dc.subject.meshSpectrometry, Fluorescenceen_US
dc.subject.meshStrontium - Pharmacologyen_US
dc.titlePotentiation of calcium- and caffeine-induced calcium release by cyclic ADP-riboseen_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.pmid8416936-
dc.identifier.scopuseid_2-s2.0-0027518440en_US
dc.identifier.volume268en_US
dc.identifier.issue1en_US
dc.identifier.spage293en_US
dc.identifier.epage299en_US
dc.identifier.isiWOS:A1993KE60300045-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridHon Cheung Lee=26642959100en_US

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