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Expression of cyclic ADP-ribose-synthetizing CD38 molecule on human
platelet membrane
G Ramaschi, M Torti, ET Festetics, F Sinigaglia, F Malavasi and C Balduini
Department of Biochemistry , University of Pavia, Italy.
CD38 is a cell surface molecule widely used as a marker for immature and
activated lymphocytes. It has been recently shown that CD38 displays three
enzymatic activities: hydrolysis of NAD+ to ADP-ribose, synthesis of cyclic
ADP-ribose from NAD+, and hydrolysis of cyclic ADP- ribose to ADP-ribose.
Thus, CD38 plays a key role in the synthesis of cyclic ADP-ribose, a
calcium-mobilizing compound. We investigate here the expression and
cellular localization of CD38 in human platelets using a specific
monoclonal antibody. Results showed that CD38 is expressed by human
platelet membranes. Moreover, we show that platelet CD38 possesses NAD
glycohydrolase, ADP-ribose cyclase, and cyclic ADP- ribose hydrolase
activities. This finding indicates that the calcium- mobilizing agent
cyclic ADP-ribose can be synthetized by human platelets and raises the
question about the possible role of CD38 expression and enzymatic
activities in the signal transduction pathways leading to platelet
activation.
Volume 87,
Issue 6,
pp. 2308-2313,
03/15/1996
Copyright © 1996 by The American Society of Hematology
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