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Adhesive functions of platelets lacking glycoprotein IV (CD36)
NN Tandon, CF Ockenhouse, NJ Greco and GA Jamieson
American Red Cross, Cell Biology Laboratory, Rockville, MD 20855.
Glycoprotein IV (GPIV; CD36 or GPIIIb) is a cell surface glycoprotein that
has been proposed as mediating a number of physiologically important
processes such as the adhesion of platelets to thrombospondin (TSP) and
collagen, the cytoadherence of Plasmodium falciparum-infected erythrocytes,
and the TSP-dependent interaction of monocytes with platelets and
macrophages. Because platelets of the Naka-negative phenotype have recently
been shown to lack detectable GPIV, their availability offered the
opportunity to test directly these hypotheses regarding its adhesive
functions. It has been found that Naka-negative platelets and monocytes do
not support cytoadherence of P falciparum- infected erythrocytes.
Naka-negative platelets are deficient in the initial stages of their
adhesion to fibrillar collagen and this defect is most marked under
Mg(2+)-free conditions. Finally, the ability of Naka-negative platelets to
bind TSP before or after activation is unimpaired as compared with normal
controls. These results do not support a role for GPIV as the TSP receptor.
Volume 78,
Issue 11,
pp. 2809-2813,
12/01/1991
Copyright © 1991 by The American Society of Hematology
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