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P-selectin mediates Ca(2+)-dependent adhesion of activated platelets to
many different types of leukocytes: detection by flow cytometry
LG de Bruijne-Admiraal, PW Modderman, AE Von dem Borne and A Sonnenberg
Department of Immunohematology, Central Laboratory of the Netherlands Red
Cross Blood Transfusion Service, Amsterdam.
Previous studies have shown that thrombin-activated platelets interact
through the P-selectin with neutrophils and monocytes. To identify other
types of leukocytes capable of such an interaction, eosinophils, basophils,
and lymphocytes were isolated from whole blood. Binding of these cells to
activated platelets was examined in a double immunofluorescence assay and
the results show that activated platelets not only bind to neutrophils and
monocytes, but also to eosinophils, basophils, and subpopulations of T
lymphocytes. Using monoclonal antibodies (MoAbs) specific for subsets of T
cells, we could further demonstrate that the T cells which bind activated
platelets are natural killer (NK) cells and an undefined subpopulation of
CD4+ and CD8+ cells. All these interactions were dependent on divalent
cations and were completely inhibited by an MoAb against P-selectin. Thus,
P- selectin mediates the binding of activated platelets to many different
types of leukocytes. Studies with leukocytes treated with proteases or
neuraminidase have shown that the structures recognized by P-selectin are
glycoproteins carrying sialic acid residues. Because the loss of binding of
activated platelets to neuraminidase-treated neutrophils was almost
complete, but only partial to treated eosinophils, basophils, and
monocytes, the latter cell types may have different P-selectin ligands in
addition to those present on neutrophils. We found that two previously
identified ligands for P-selectin, the oligosaccharides Le(x) and
sialyl-Le(x), had little or no inhibitory effect on adhesion of activated
platelets to leukocytes and that binding was not inhibited by MoAbs against
these oligosaccharides. In addition, there was no correlation between the
expression of Le(x) on several cell types and their capacity to bind
activated platelets. In contrast, the expression of sialyl-Le(x) on cells
was almost perfectly correlated with their ability to bind activated
platelets. Thus, while Le(x) cannot be a major ligand for P-selectin, a
possible role for sialyl-Le(x) in P- selectin-mediated adhesion processes
cannot be dismissed. Finally, activated platelets were found to bind
normally to monocytes and neutrophils of patients with paroxysmal nocturnal
hemoglobulinuria (PNH) and to neutrophils from which phosphatidyl inositol
(PI)-linked proteins had been removed by glycosylphosphatidyl
inositol-specific phospholipase C (GPI-PLC) digestion. This suggests that
at least part of the P-selectin ligands on these cells are not
GPI-anchored.
Volume 80,
Issue 1,
pp. 134-142,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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