Nuclear CD38 in retinoic acid-induced HL-60 cells

Leman Yalcintepe, Isil Albeniz, Suzan Adin-Cinar, Demir Tiryaki, Engin Bermek, Richard M Graeff, Hon Cheung Lee

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14 Scopus citations


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+ and hydrolysis of either NAD+ 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+ 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 ∼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 ∼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.

Original languageEnglish (US)
Pages (from-to)14-21
Number of pages8
JournalExperimental Cell Research
Issue number1
StatePublished - Feb 1 2005

Bibliographical note

Funding Information:
This work was supported by the Research Fund of the University of Istanbul (project G-148/20082003).


  • ADP ribosylation
  • CD38
  • cGDP-ribose


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