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Article: Multiplicity of Ca2+ messengers and Ca2+ stores: A perspective from cyclic ADP-ribose and NAADP

TitleMultiplicity of Ca2+ messengers and Ca2+ stores: A perspective from cyclic ADP-ribose and NAADP
Authors
KeywordsADP-ribosyl cyclase
Ca2+ signaling
CD38
Cyclic ADP-ribose (cADPR)
Mobilization of Ca2+ stores
NAADP
Issue Date2004
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/cmm/index.htm
Citation
Current Molecular Medicine, 2004, v. 4 n. 3, p. 227-237 How to Cite?
AbstractIt is generally believed that multiple Ca2+ stores are present in cells, a notion that has now been made substantive by the discovery of multiple Ca2+ mobilizing messengers. Cyclic ADP-ribose (cADPR and nicotinic acid dinucleotide phosphate (NAADP) are two such messengers that are derived from NAD and NADP, respectively. A wide variety of cells, from plants to mammals, including human, have been shown to be responsive to these two novel Ca2+ messengers. Not only are their structures and mechanisms of action different, their targeted Ca2+ stores are also distinct and separable. This article explores the implications of the multiplicity of Ca2+ stores in cellular signaling. Special emphasis will be put on the recent progress in the understanding of the physiological functions of NAADP. © 2004 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/171734
ISSN
2023 Impact Factor: 2.2
2023 SCImago Journal Rankings: 0.531
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, HCen_US
dc.date.accessioned2012-10-30T06:16:41Z-
dc.date.available2012-10-30T06:16:41Z-
dc.date.issued2004en_US
dc.identifier.citationCurrent Molecular Medicine, 2004, v. 4 n. 3, p. 227-237en_US
dc.identifier.issn1566-5240en_US
dc.identifier.urihttp://hdl.handle.net/10722/171734-
dc.description.abstractIt is generally believed that multiple Ca2+ stores are present in cells, a notion that has now been made substantive by the discovery of multiple Ca2+ mobilizing messengers. Cyclic ADP-ribose (cADPR and nicotinic acid dinucleotide phosphate (NAADP) are two such messengers that are derived from NAD and NADP, respectively. A wide variety of cells, from plants to mammals, including human, have been shown to be responsive to these two novel Ca2+ messengers. Not only are their structures and mechanisms of action different, their targeted Ca2+ stores are also distinct and separable. This article explores the implications of the multiplicity of Ca2+ stores in cellular signaling. Special emphasis will be put on the recent progress in the understanding of the physiological functions of NAADP. © 2004 Bentham Science Publishers Ltd.en_US
dc.languageengen_US
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/cmm/index.htmen_US
dc.relation.ispartofCurrent Molecular Medicineen_US
dc.subjectADP-ribosyl cyclase-
dc.subjectCa2+ signaling-
dc.subjectCD38-
dc.subjectCyclic ADP-ribose (cADPR)-
dc.subjectMobilization of Ca2+ stores-
dc.subjectNAADP-
dc.subject.meshAnimalsen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCatalysisen_US
dc.subject.meshCyclic Adp-Ribose - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshNadp - Analogs & Derivatives - Metabolismen_US
dc.titleMultiplicity of Ca2+ messengers and Ca2+ stores: A perspective from 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.doi10.2174/1566524043360753en_US
dc.identifier.pmid15101681-
dc.identifier.scopuseid_2-s2.0-1942485783en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1942485783&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume4en_US
dc.identifier.issue3en_US
dc.identifier.spage227en_US
dc.identifier.epage237en_US
dc.identifier.isiWOS:000220810500002-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.issnl1566-5240-

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