Anti-CD9 antibodies which bind to the CD9 (p24) antigen are known to induce platelet and pre-B-cell aggregation. We show here that human endothelium expresses the CD9 antigen, and anti-CD9 antibodies incubated with endothelium induce a rapid increase in adhesion of neutrophils to endothelium by an action on the endothelial cell. This augmented adhesion is not mediated by glycoprotein IIb/IIIa or by the leucocyte integrins. Binding of anti-CD9 antibody to CD9 induces shedding of the CD9/anti-CD9 complex off the endothelial cell in a time-dependent manner. It is likely that CD9 binding to its ligand induces an activation event within the endothelial cell, resulting in surface expression of a pre-formed adhesive ligand for the neutrophil, or an activation change to a constitutively expressed ligand to render it functional.