CD38 is constitutively expressed in the nucleus of human hematopoietic cells.

CD38 is a type II glycoprotein that acts both as a bifunctional enzyme, responsible for the synthesis and hydrolysis of cyclic ADP-ribose, and as a signal-transducing surface receptor. Although CD38 was originally described as a plasma membrane molecule, several reports indicate that CD38 is expressed in the nucleus, even in cells known to be CD38 surface-negative. In this study, firstly we investigated the presence of nuclear CD38 by immunofluorescence and confocal microscopy using a panel of hematopoietic cell lines that exhibit different levels of CD38 plasma membrane expression. Our second aim was to explore the relationship between the nuclear and plasma membrane forms of CD38 in human cell lines which represent discrete early maturation stages of the human lymphoid and myeloid compartments. Our results indicate that CD38 is constitutively present in the nucleus of cells belonging to distinct lineages. Furthermore, nuclear CD38 appears to be independent of the plasma membrane pool. The presence of nuclear CD38 during different stages of hematopoietic differentiation suggests that it may play a role in the control of nuclear Ca(2+) homeostasis and NAD levels.