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Article: Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP

TitleMechanisms of calcium signaling by cyclic ADP-ribose and NAADP
Authors
Issue Date1997
Citation
Physiological Reviews, 1997, v. 77 n. 4, p. 1133-1164 How to Cite?
AbstractCells possess various mechanisms for transducing external signals to intracellular responses. The discovery of inositol 1,4,5-trisphosphate (IP 3) as a messenger for mobilizing internal Ca 2+ stores has centralized Ca 2+ mobilization among signaling mechanisms. Results reviewed in this article establish that, in addition to IP 3, the internal Ca 2+ stores can be mobilized by at least two other molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), via totally independent mechanisms. Cyclic ADP-ribose is a newly discovered cyclic nucleotide derived from NAD, but, unlike adenosine 3',5'-cyclic monophosphate, its main signaling function is modulation of Ca 2+-induced Ca 2+ release, a major mechanism of Ca 2+ mobilization in addition to the IP 3 pathway. Evidence shows that cADPR may in fact be responsible for mediating the Ca 2+-mobilizing activity of the gaseous messenger nitric oxide. Cells responsive to cADPR are widespread and include species from plant to mammal, indicating the generality of cADPR as a signaling molecule. In addition to cADPR, NAADP, a metabolite of NADP, can also mobilize Ca 2+ stores. The release mechanism and the stores on which NAADP acts are distinct from cADPR and IP 3. Nicotinic acid adenine dinucleotide phosphate may play a role in generating Ca 2+ oscillations, since liberation of NAADP in live cells by photolyzing its caged analog produces long-lasting Ca 2+ oscillations. These two new Ca 2+ agonists are intimately related, since the same metabolic enzymes can, under appropriate conditions, synthesize either one, suggesting a unified mechanism may regulate both pathways. Elucidation of these two new Ca 2+ mobilization pathways is likely to have an important impact on our understanding of cellular signaling mechanisms.
Persistent Identifierhttp://hdl.handle.net/10722/171722
ISSN
2015 Impact Factor: 30.924
2015 SCImago Journal Rankings: 17.564
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:36Z-
dc.date.available2012-10-30T06:16:36Z-
dc.date.issued1997en_US
dc.identifier.citationPhysiological Reviews, 1997, v. 77 n. 4, p. 1133-1164en_US
dc.identifier.issn0031-9333en_US
dc.identifier.urihttp://hdl.handle.net/10722/171722-
dc.description.abstractCells possess various mechanisms for transducing external signals to intracellular responses. The discovery of inositol 1,4,5-trisphosphate (IP 3) as a messenger for mobilizing internal Ca 2+ stores has centralized Ca 2+ mobilization among signaling mechanisms. Results reviewed in this article establish that, in addition to IP 3, the internal Ca 2+ stores can be mobilized by at least two other molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), via totally independent mechanisms. Cyclic ADP-ribose is a newly discovered cyclic nucleotide derived from NAD, but, unlike adenosine 3',5'-cyclic monophosphate, its main signaling function is modulation of Ca 2+-induced Ca 2+ release, a major mechanism of Ca 2+ mobilization in addition to the IP 3 pathway. Evidence shows that cADPR may in fact be responsible for mediating the Ca 2+-mobilizing activity of the gaseous messenger nitric oxide. Cells responsive to cADPR are widespread and include species from plant to mammal, indicating the generality of cADPR as a signaling molecule. In addition to cADPR, NAADP, a metabolite of NADP, can also mobilize Ca 2+ stores. The release mechanism and the stores on which NAADP acts are distinct from cADPR and IP 3. Nicotinic acid adenine dinucleotide phosphate may play a role in generating Ca 2+ oscillations, since liberation of NAADP in live cells by photolyzing its caged analog produces long-lasting Ca 2+ oscillations. These two new Ca 2+ agonists are intimately related, since the same metabolic enzymes can, under appropriate conditions, synthesize either one, suggesting a unified mechanism may regulate both pathways. Elucidation of these two new Ca 2+ mobilization pathways is likely to have an important impact on our understanding of cellular signaling mechanisms.en_US
dc.languageengen_US
dc.relation.ispartofPhysiological Reviewsen_US
dc.subject.meshAdp-Ribosyl Cyclaseen_US
dc.subject.meshAdenosine Diphosphate Ribose - Agonists - Analogs & Derivatives - Antagonists & Inhibitors - Chemistry - Metabolism - Physiologyen_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 - Metabolismen_US
dc.subject.meshCalcium - Physiologyen_US
dc.subject.meshCalmodulin - Physiologyen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshHl-60 Cellsen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Glycoproteinsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNad+ Nucleosidase - Metabolismen_US
dc.subject.meshNadp - Analogs & Derivatives - Biosynthesis - Chemistry - Physiologyen_US
dc.subject.meshNitric Oxide - Pharmacologyen_US
dc.subject.meshPc12 Cellsen_US
dc.subject.meshRatsen_US
dc.subject.meshSea Urchinsen_US
dc.subject.meshSignal Transductionen_US
dc.subject.meshTretinoin - Pharmacologyen_US
dc.titleMechanisms of calcium signaling by cyclic ADP-ribose and NAADPen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid9354813-
dc.identifier.scopuseid_2-s2.0-0345609814en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0345609814&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume77en_US
dc.identifier.issue4en_US
dc.identifier.spage1133en_US
dc.identifier.epage1164en_US
dc.identifier.isiWOS:A1997YC32000006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US

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