Bradykinin and des-Arg10-kallidin enhance the adhesion of polymorphonuclear leukocytes to extracellular matrix proteins and endothelial cells.

Abstract

Bradykinin-related peptides (kinins) are well known to contribute to leukocyte recruitment to inflammatory foci; however, a role of these universal pro-inflammatory mediators in the first step of this process, i.e. the leukocyte adhesion to endothelial cells, is not well understood. In this work we found that bradykinin and des-Arg10-kallidin enhance the adhesion of polymorphonuclear bloods cells (PMN) to fibrinogen and fibronectin. Also, the PMN adherence to endothelial cells of HMEC-1 line strongly increased after stimulation by kinins, particularly des-Arg10-kallidin, or when PMN were co-stimulated with bradykinin and interleukin-1β. These effects were attenuated after PMN treatment with a specific inhibitor of carboxypeptidases, which convert kinins to their des-Arg metabolites. The kinin peptides were also able to change the Mac-1 integrin expression on the PMN surface. These results suggest a regulatory effect of kinins on leukocyte adhesion to endothelial wall, providing new aspects of the leukocyte infiltration into inflamed tissues.