Nuclear CD38 in retinoic acid-induced HL-60 cells
- Department of Biophysics, Istanbul University, Istanbul Faculty of Medicine, 34390 Capa-Istanbul (Turkey) and Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455 (United States)
- Department of Biophysics, Istanbul University, Istanbul Faculty of Medicine, 34390 Capa-Istanbul (Turkey)
- Department of Microbiology, Istanbul University, Istanbul Faculty of Medicine, Virology and Basic Immunology Unit, 34390 Capa-Istanbul (Turkey)
- Department of Pharmacology, University of Minnesota, Minneapolis, MN 55455 (United States)
The cell surface antigen, CD38, is a 45-kDa transmembrane protein which is predominantly expressed on hematopoietic cells during differentiation. As a bifunctional ectoenzyme, it catalyzes the synthesis of cyclic ADP-ribose (cADPR) from NAD{sup +} and hydrolysis of either NAD{sup +} or cADPR to ADP-ribose. All-trans-retinoic acid (RA) is a potent and specific inducer of CD38 in myeloid cells. In this report, we demonstrate that the nuclei of RA-treated human HL-60 myeloblastic cells reveal enzymatic activities inherent to CD38. Thus, GDP-ribosyl cyclase and NAD{sup +} glycohydrolase activities in the nuclear fraction increased very significantly in response to incubation with RA. With Western blotting, we detected in the nuclear protein fraction from RA-treated cells a {approx}43-kDa protein band which was reactive with the CD38-specific monoclonal antibody OKT10. The expression of CD38 in HL-60 nuclei was also shown with FACScan analysis. RA treatment gave rise to an increase in in vitro ADP ribosylation of the {approx}43-kDa nuclear protein. Moreover, nuclei isolated from RA-treated HL-60 cells revealed calcium release in response to cADPR, whereas a similar response was not observed in control nuclei. These results suggest that CD38 is expressed in HL-60 cell nuclei during RA-induced differentiation.
- OSTI ID:
- 20717519
- Journal Information:
- Experimental Cell Research, Vol. 303, Issue 1; Other Information: DOI: 10.1016/j.yexcr.2004.09.010; PII: S0014-4827(04)00534-8; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0014-4827
- Country of Publication:
- United States
- Language:
- English
Similar Records
Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity
A specific isoform of poly(ADP-ribose) glycohydrolase is targeted to the mitochondrial matrix by a N-terminal mitochondrial targeting sequence