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Book Chapter: Determination of ADP-Ribosyl Cyclase Activity, Cyclic ADP-Ribose, and Nicotinic Acid Adenine Dinucleotide Phosphate in Tissue Extracts

TitleDetermination of ADP-Ribosyl Cyclase Activity, Cyclic ADP-Ribose, and Nicotinic Acid Adenine Dinucleotide Phosphate in Tissue Extracts
Authors
Issue Date2013
PublisherSpringer
Citation
Determination of ADP-Ribosyl Cyclase Activity, Cyclic ADP-Ribose, and Nicotinic Acid Adenine Dinucleotide Phosphate in Tissue Extracts. In Gehring, C (Ed.), Cyclic nucleotide signaling in plants: methods and protocols, p. 39-56. New York: Springer, 2013 How to Cite?
AbstractCyclic ADP-ribose (cADPR) is a novel second messenger that releases calcium from intracellular stores. Although first shown to release calcium in the sea urchin egg, cADPR has been shown since to be active in a variety of cells and tissues, from plant to human. cADPR stimulates calcium release via ryanodine receptors although the mechanism is still not completely understood. cADPR is produced enzymatically from NAD by ADP-ribosyl cyclases; several of these proteins have been identified including one isolated from Aplysia californica, two types found in mammals (CD38 and CD157), and three forms in sea urchin. A cyclase activity has been measured in extracts from Arabidopsis thaliana although the protein is still unidentified. Nicotinic acid adenine dinucleotide phosphate (NAADP) is another novel messenger that releases calcium from internal stores and is produced by these same enzymes by an exchange reaction. NAADP targets lysosomal stores whereas cADPR releases calcium from the endoplasmic reticulum. Due to their importance in cell signaling, cADPR and NAADP have been the focus of numerous investigations over the last 25 years. This chapter describes several assay methods for the measurements of cADPR and NAADP concentration and cyclase activity in extracts from cells.
Persistent Identifierhttp://hdl.handle.net/10722/191022
ISBN
Series/Report no.Methods in molecular biology, v. 1016.; Springer protocols (Series)

 

DC FieldValueLanguage
dc.contributor.authorGraeff, RMen_US
dc.contributor.authorLee, HCen_US
dc.date.accessioned2013-09-17T16:07:41Z-
dc.date.available2013-09-17T16:07:41Z-
dc.date.issued2013en_US
dc.identifier.citationDetermination of ADP-Ribosyl Cyclase Activity, Cyclic ADP-Ribose, and Nicotinic Acid Adenine Dinucleotide Phosphate in Tissue Extracts. In Gehring, C (Ed.), Cyclic nucleotide signaling in plants: methods and protocols, p. 39-56. New York: Springer, 2013en_US
dc.identifier.isbn9781627034401-
dc.identifier.urihttp://hdl.handle.net/10722/191022-
dc.description.abstractCyclic ADP-ribose (cADPR) is a novel second messenger that releases calcium from intracellular stores. Although first shown to release calcium in the sea urchin egg, cADPR has been shown since to be active in a variety of cells and tissues, from plant to human. cADPR stimulates calcium release via ryanodine receptors although the mechanism is still not completely understood. cADPR is produced enzymatically from NAD by ADP-ribosyl cyclases; several of these proteins have been identified including one isolated from Aplysia californica, two types found in mammals (CD38 and CD157), and three forms in sea urchin. A cyclase activity has been measured in extracts from Arabidopsis thaliana although the protein is still unidentified. Nicotinic acid adenine dinucleotide phosphate (NAADP) is another novel messenger that releases calcium from internal stores and is produced by these same enzymes by an exchange reaction. NAADP targets lysosomal stores whereas cADPR releases calcium from the endoplasmic reticulum. Due to their importance in cell signaling, cADPR and NAADP have been the focus of numerous investigations over the last 25 years. This chapter describes several assay methods for the measurements of cADPR and NAADP concentration and cyclase activity in extracts from cells.-
dc.languageengen_US
dc.publisherSpringeren_US
dc.relation.ispartofCyclic nucleotide signaling in plants: methods and protocolsen_US
dc.relation.ispartofseriesMethods in molecular biology, v. 1016.; Springer protocols (Series)-
dc.subject.meshADP-ribosyl Cyclase - metabolism-
dc.subject.meshCyclic ADP-Ribose - metabolism-
dc.subject.meshNADP - analogs and derivatives - metabolism-
dc.subject.meshTissue Extracts - metabolism-
dc.titleDetermination of ADP-Ribosyl Cyclase Activity, Cyclic ADP-Ribose, and Nicotinic Acid Adenine Dinucleotide Phosphate in Tissue Extractsen_US
dc.typeBook_Chapteren_US
dc.identifier.emailGraeff, RM: graeffr@hku.hken_US
dc.identifier.emailLee, HC: leehc@hku.hken_US
dc.identifier.authorityGraeff, RM=rp01464en_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.identifier.doi10.1007/978-1-62703-441-8_4-
dc.identifier.pmid23681571-
dc.identifier.hkuros222845en_US
dc.identifier.spage39en_US
dc.identifier.epage56en_US
dc.publisher.placeNew York-

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