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,
*
The Wistar Institute of Anatomy and Biology, Philadelphia, PA;
Laboratory of Cell Biology, Department of Genetics, Biology and Medical Chemistry, University of Turin, Turin, Italy; and
Institute of Biology and Genetics, University of Ancona, Ancona, Italy
Human CD38 is a type II transmembrane glycoprotein that regulates
lymphocyte adhesion, proliferation, and cytokine production. The mAb
Moon-1 recognizes a ligand for CD38 (CD38L) and specifically inhibits
CD38-mediated cell adhesion. To analyze the role of CD38 and its ligand
in MHC-nonrestricted T cell activation, we examined the effects of
Moon-1 and the anti-CD38 mAb IB4 on the effector functions of the
IL-2-dependent T cell line TALL-104 (CD3/TCR-
ß+,
CD8+, CD56+) and of LAK cells (90%
CD3+). TALL-104 cells were almost 100% reactive with both
mAbs, whereas the reactivity of LAK cells for IB4 and Moon-1 ranged
from 10 to 60% among different donors. From 78 to 94% of the
cytotoxic CD8+/CD56+ LAK subset was
CD38L+. Like mAb OKT3 (anti-CD3), and at variance with
IB4, Moon-1 drastically enhanced the cytotoxicity of TALL-104 and
CD8+ LAK cells against a resistant tumor target. Granule
exocytosis did not appear to play a role in Moon-1-induced
cytotoxicity. Moreover, neither IB4 nor Moon-1 induced
[Ca2+]i mobilization in LAK and TALL-104
cells. Whereas stimulation of CD3 and CD38 resulted in a dramatic
induction of cytokine (granulocyte-macrophage-CSF, IFN-
, TNF-,
and TNF-ß) release by both TALL-104 and LAK cells, ligation of CD38L
was not followed by cytokine production in TALL-104 cells. Thus,
cytotoxicity and cytokine release are independently regulated, at least
in this system. These data demonstrate that CD38 and its ligand can
regulate some T cell functions using signaling pathways distinct from
those of CD3.
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