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J. Biol. Chem., Vol. 275, Issue 32, 24807-24817, August 11, 2000
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From the 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.
Localization of the Cyclic ADP-ribose-dependent
Calcium Signaling Pathway in Hepatocyte Nucleus*
§,
,,, and Clinical Research Unit, Tan Tock Seng
Hospital, 11 Jalan Tan Tock Seng, S308433, Singapore, the
§ Department of Biochemistry, Faculty of Medicine, National
University of Singapore, 10 Kent Ridge Crescent, S119260, Singapore,
the ¶ Department of Biochemistry, Institute of Medical Sciences,
the Department of Pharmacology, Institute of Cardiovascular
Research, Chonbuk National University Medical School,
Chonju 561-182 Korea, the ** Department of Physiology, University
of Minnesota, Minneapolis, Minnesota 55455, and the
Department of Anatomy, Faculty of
Medicine, National University of Singapore, 10 Kent Ridge Crescent,
S119260, Singapore
*
This work was supported by the National University of
Singapore Academic Research Grants RP960325 and RP960376. The work on the three-dimensional reconstruction was supported by a National Institutes of Health Grant HD17484 (to H. C. L.). The calcium mobilization work and funds for K. M. Khoo's stay in Korea to perform the initial part of that work was supported by a Genetic Engineering Research Grant from the Korean Ministry of Education (to
U. H. K.) and a Korean STEPI Grant 97-N1-02-02-A-04 (to
U.-H. K. and S. W. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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