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*
Laboratory of Immunology and Vascular Biology, La Jolla Institute for Experimental Medicine, La Jolla, CA 92037;
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92937; and
Department of Medicine, University of California at San Diego, La Jolla, CA 92122
The comparative ability of the complement anaphylatoxins C3a and
C5a to mediate leukocyte adhesion and transendothelial migration
in vivo and in vitro was investigated. Superfusion of
IL-1ß-stimulated rabbit mesentery with C3a resulted in a rapid and
stable adhesion of rolling eosinophils, but not neutrophils, to
postcapillary venules. However, C3a failed to evoke subsequent
transmigration of the adherent eosinophils. In contrast, C5a induced
both the rapid activation-dependent firm adhesion and transmigration of
eosinophils and neutrophils through venular endothelium. C3a induced
selective shedding of L-selectin and an increase in
Mß2 integrin expression on eosinophils but
not neutrophils, while C5a induced shedding of L-selectin and
up-regulation of Mß2 integrin on both
eosinophils and neutrophils. Both C3a- and C5a-dependent adhesion to
venular endothelium was blocked by ex vivo treatment of eosinophils
with anti-4 and anti-ß2 integrin
mAbs. In vitro, both C3a (but not C3adesArg) and C5a
(including C5adesArg)-dependent transmigration of
eosinophils across IL-1ß-stimulated endothelial monolayer was
mediated by 4ß1 and
Mß2 integrins. Overall these studies
suggest that C3a is eosinophil-specific chemotactic mediator that
influences selectively eosinophil adhesion but not transmigration in
vivo. C5a in contrast is a complete activator of integrin-dependent
adhesion as well as transmigration of eosinophils and
neutrophils.
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