Induction of CD38/NADase and its monoclonal antibody-induced tyrosine phosphorylation in human leukemia cell lines.

We previously reported that CD38 characterized as an ecto-enzyme of NAD+ glycohydrolase (NADase) was specifically induced by retinoic acid (RA) in human promyelocytic leukemia HL-60 cells and that anti-CD38 monoclonal antibody (mAb) induced tyrosine phosphorylation of cellular proteins in the RA-differentiated cells. In the present study, we found that CD38/NADase was induced in human monocytic leukemia THP-1 cells not only by RA but also by dibutyryl cAMP, which had no effect on the induction of CD38 in HL-60 cells. Similarly in the RA-differentiated HL-60 cells, tyrosine phosphorylation by anti-CD38 mAb was also observed in the CD38-expressing THP-1 cells, regardless of whether CD38 was induced by RA or dibutyryl cAMP. Such tyrosine phosphorylation was, however, not observed in human lymphoblastic leukemia Jurkat cells which had been treated by RA to produce CD38. Thus, the induction of CD38/NADase appeared to be not limited for RA-dependent differentiation and not always linked to protein-tyrosine phosphorylation in human leukemic cell lines.