Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M908231199
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dc.titleLocalization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus
dc.contributor.authorKeng Meng Khoo
dc.contributor.authorHan, M.-K.
dc.contributor.authorPark, J.B.
dc.contributor.authorSoo Wan Chae
dc.contributor.authorKim, U.-H.
dc.contributor.authorHon Cheung Lee
dc.contributor.authorBoon Huat Bay
dc.contributor.authorChan Fong Chang
dc.date.accessioned2014-11-10T09:52:31Z
dc.date.available2014-11-10T09:52:31Z
dc.date.issued2000-08-11
dc.identifier.citationKeng Meng Khoo, Han, M.-K., Park, J.B., Soo Wan Chae, Kim, U.-H., Hon Cheung Lee, Boon Huat Bay, Chan Fong Chang (2000-08-11). Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus. Journal of Biological Chemistry 275 (32) : 24807-24817. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M908231199
dc.identifier.issn00219258
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/107790
dc.description.abstractCD38 is a type II transmembrane glycoprotein found on both hematopoietic and non-hematopoietic cells. It is known for its involvement in the metabolism of cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate, two nucleotides with calcium mobilizing activity independent of inositol trisphosphate. It is generally believed that CD38 is an integral protein with ectoenzymatic activities found mainly on the plasma membrane. Here we show that enzymatically active CD38 is present intracellularly on the nuclear envelope of rat hepatocytes. CD38 isolated from rat liver nuclei possessed both ADP-ribosyl cyclase and NADase activity. Immunofluorescence studies on rat liver cryosections and isolated nuclei localized CD38 to the nuclear envelope of hepatocytes. Subcellular localization via immunoelectron microscopy showed that CD38 is located on the inner nuclear envelope. The isolated nuclei sequestered calcium in an ATP-dependent manner. cADPR elicited a rapid calcium release from the loaded nuclei, which was independent of inositol trisphosphate and was inhibited by 8-amino-cADPR, a specific antagonist of cADPR, and ryanodine. However, nicotinic acid adenine dinucleotide phosphate failed to elicit any calcium release from the nuclear calcium stores. The nuclear localization of CD38 shown in this study suggests a novel role of CD38 in intracellular calcium signaling for non-hematopoietic cells.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.M908231199
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentANATOMY
dc.description.doi10.1074/jbc.M908231199
dc.description.sourcetitleJournal of Biological Chemistry
dc.description.volume275
dc.description.issue32
dc.description.page24807-24817
dc.description.codenJBCHA
dc.identifier.isiut000088683300078
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