Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.M908231199
Title: Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus
Authors: Keng Meng Khoo
Han, M.-K.
Park, J.B.
Soo Wan Chae
Kim, U.-H.
Hon Cheung Lee
Boon Huat Bay 
Chan Fong Chang 
Issue Date: 11-Aug-2000
Citation: Keng 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
Abstract: CD38 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.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/107790
ISSN: 00219258
DOI: 10.1074/jbc.M908231199
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