Human vascular adhesion protein-1 (VAP-1) is a dualfunction molecule with adhesive and enzymatic properties. In addition to synthesis in endothelial cells1 In endothelial cells, VAP-1 is localized both in conspicuous cytoplasmic granules and on the luminal surface. Under physiological conditions, the synthesis of VAP-1 is most prominent in high endothelial venules (HEVs) of peripheral lymph node-type lymphatic organs, but it is also inducible in vessels at other locations in the setting of inflammation.2 In endothelial cells VAP-1 is expressed as a homodimer of two 90-kd subunits. VAP-1 isolated from HEVs is an abundantly sialylated glycoprotein, and the sialic acid decorations are a prerequisite to the adhesive function of VAP-1.

Human P-selectin, ICAM-1 and VAP-1 appear to be the most promising targets when antiadhesive interventions preventing leukocyte-mediated tissue destruction after myocardial ischemia are planned.