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GMP-140 mediates adhesion of stimulated platelets to neutrophils
SA Hamburger and RP McEver
St Francis Medical Research Institute, Oklahoma City, OK.
In vivo, platelets associate with neutrophils at sites of hemorrhage or
inflammation. In vitro, stimulated platelets bind to neutrophils in a
Ca2(+)-dependent manner. GMP-140, an integral membrane glycoprotein found
in secretory granules of platelets and endothelium, is rapidly translocated
to the cell surface after cellular activation. It shares sequence
similarity with two leukocyte adhesion molecules, ELAM-1 and a lymphocyte
homing receptor. We have recently shown that neutrophils bind to purified
GMP-140 in a Ca2(+)-dependent fashion, and that GMP- 140 participates in
adhesion of neutrophils to activated endothelium. In this study we
demonstrate that GMP-140 also mediates adhesion of neutrophils to
stimulated platelets. Fixed thrombin-activated human platelets, but not
unstimulated platelets, formed rosettes around neutrophils in the presence
of Ca2+. The binding of platelets to neutrophils was inhibited by a
monoclonal antibody to GMP-140 and by purified GMP-140. By promoting close
cell-cell contact, GMP-140 may recruit both platelets and neutrophils to
sites of tissue injury as well as modulate the function of each cell type
by the other.
Volume 75,
Issue 3,
pp. 550-554,
02/01/1990
Copyright © 1990 by The American Society of Hematology

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