Using human promyelocytic leukemia cells , we demonstrate that all trans-retinoic acid is a potent and specific inducer of CD38 expression in myeloid lineage.
We reported previously that retinoic acid (RA) is a potent and selective inducer of the cell-surface antigen CD38 in myeloid leukemia cells.
Thus , GDP-ribosyl cyclase and NAD (+) glycohydrolase activities in the nuclear fraction increased very significantly in response to incubation with RA.
The nuclear NAD glycohydrolase activity was identified as an ADPRT-catalyzed enzymatic activity by its unreactivity toward ethenoadenine NAD as a substrate added to nuclei or to purified ADPRT.
ADP-ribosyl transferase activity could also be detected when NAD glycohydrolase was separated by hydroxylapatite chromatography.