Adhesion of activated platelets to polymorphonuclear leukocytes.

Polymorphonuclear leukocytes (PMNL) are components of the blood which as such interact extensively with other blood cells, with endothelial cells or with plasma. Here, we consider the interaction between PMNL and platelets which is efficient during adhesion of platelets to PMNL and which can be studied in vitro using the rosette formation assay. The adhesion of activated platelets to PMNL seems to be mediated mainly by a protein of platelets (CD62) and its counterreceptor on PMNL, but also other platelet receptors are involved. Here we demonstrate the participation of the glycoprotein IIb-IIIa complex (CD41a) in the adhesion of activated platelets to PMNL due to the following findings: a) inhibition of adhesion by monoclonal antibodies raised against CD41a, b) inhibition of adhesion by peptides such as RGDS and echistatin, c) inhibition of adhesion by dissociation of CD41a with EGTA and d) inhibition of adhesion using platelets from a thrombasthenic patient which have almost no CD41a in the surface membrane but a normal expression of CD62 upon activation. The adhesion of activated platelets to PMNL via CD41a seems to be mediated by fibrinogen due to the following findings: a) addition of fibrinogen to ADP-stimulated and fixed platelets increases significantly the rosette formation and b) the incubation of unstimulated platelets with fibrinogen and an antibody raised against glycoprotein IIIa which stimulates fibrinogen binding to the platelet surface results in an enlarged rosette formation.