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Article: NAADP: a universal Ca2+ trigger.

TitleNAADP: a universal Ca2+ trigger.
Authors
Issue Date2008
Citation
Science Signaling, 2008, v. 1 n. 44, p. re10 How to Cite?
AbstractCells possess multiple calcium ion (Ca2+) stores and multiple messenger molecules to mobilize them. These include d-myo-inositol 1,4,5-trisphosphate (IP(3)), cyclic adenosine diphosphoribose (cADPR), and the most recently identified Ca2+-mobilizing messenger, nicotinic acid adenine dinucleotide phosphate (NAADP), which acts on a wide spectrum of cells, from plant cells to mammalian cells. Accumulating evidence indicates that NAADP targets both acidic (lysosome-like) Ca2+ stores and endoplasmic reticular stores. Recent studies in invertebrate and mammalian cells suggest that NAADP provides an initiating Ca2+ signal, which is amplified by cADPR- or IP(3)-dependent mechanisms (or both) through Ca2+-induced Ca2+ release. Diverse stimuli activate a rapid rise of endogenous NAADP concentration, resulting in severalfold increases of NAADP over basal values within seconds. The enzyme CD38 can catalyze both the synthesis and hydrolysis of NAADP, making it ideal for effecting the rapid metabolism of NAADP. The crystal structure of CD38 and the structures of its various substrate complexes have now been determined, clarifying the mechanism of its multifunctional catalysis. We anticipate that these advances will lead to the unmasking of all the key components of the Ca2+ signaling pathway mediated by NAADP.
Persistent Identifierhttp://hdl.handle.net/10722/59672
ISSN
2012 Impact Factor: 7.648
2015 SCImago Journal Rankings: 4.850
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorGuse, AHen_HK
dc.contributor.authorLee, HCen_HK
dc.date.accessioned2010-05-31T03:54:58Z-
dc.date.available2010-05-31T03:54:58Z-
dc.date.issued2008en_HK
dc.identifier.citationScience Signaling, 2008, v. 1 n. 44, p. re10en_HK
dc.identifier.issn1937-9145en_HK
dc.identifier.urihttp://hdl.handle.net/10722/59672-
dc.description.abstractCells possess multiple calcium ion (Ca2+) stores and multiple messenger molecules to mobilize them. These include d-myo-inositol 1,4,5-trisphosphate (IP(3)), cyclic adenosine diphosphoribose (cADPR), and the most recently identified Ca2+-mobilizing messenger, nicotinic acid adenine dinucleotide phosphate (NAADP), which acts on a wide spectrum of cells, from plant cells to mammalian cells. Accumulating evidence indicates that NAADP targets both acidic (lysosome-like) Ca2+ stores and endoplasmic reticular stores. Recent studies in invertebrate and mammalian cells suggest that NAADP provides an initiating Ca2+ signal, which is amplified by cADPR- or IP(3)-dependent mechanisms (or both) through Ca2+-induced Ca2+ release. Diverse stimuli activate a rapid rise of endogenous NAADP concentration, resulting in severalfold increases of NAADP over basal values within seconds. The enzyme CD38 can catalyze both the synthesis and hydrolysis of NAADP, making it ideal for effecting the rapid metabolism of NAADP. The crystal structure of CD38 and the structures of its various substrate complexes have now been determined, clarifying the mechanism of its multifunctional catalysis. We anticipate that these advances will lead to the unmasking of all the key components of the Ca2+ signaling pathway mediated by NAADP.en_HK
dc.languageengen_HK
dc.relation.ispartofScience signalingen_HK
dc.titleNAADP: a universal Ca2+ trigger.en_HK
dc.typeArticleen_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid18984909-
dc.identifier.scopuseid_2-s2.0-61549132959en_HK
dc.identifier.hkuros154343en_HK
dc.identifier.volume1en_HK
dc.identifier.issue44en_HK
dc.identifier.spagere10en_HK
dc.identifier.epagere10en_HK
dc.identifier.isiWOS:000207497200001-
dc.identifier.scopusauthoridGuse, AH=34975071300en_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK

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