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Blood, 1 May 2004, Vol. 103, No. 9, pp. 3388-3395.
Prepublished online as a Blood First Edition Paper on January 15, 2004; DOI 10.1182/blood-2003-09-3275.
Submitted September 24, 2003
Accepted December 16, 2003
Granulocyte transmigration through endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1)
Kaisa Koskinen, Petri J Vainio, David J Smith, Marjo Pihlavisto, Seppo Yla-Herttuala, Sirpa Jalkanen, and Marko Salmi*
MediCity Research Laboratory, and Dept of Medical Microbiology, Turku University, Turku, Finland; National Public Health Institute, Turku, Finland
Biotie Therapies Corp, Turku, Finland
A.I. Virtanen Institute and Department of Medicine, University of Kuopio, Kuopio, Finland
* Corresponding author; email: marko.salmi{at}utu.fi.
Polymorphonuclear leukocytes (PMN) migrate from the blood into areas of inflammation by binding to the endothelial cells of blood vessels via adhesion molecules. Vascular adhesion protein-1 (VAP-1) is one of the molecules mediating leukocyte-endothelial cell interactions. It is also an endothelial cell-surface enzyme (amine oxidase) that produces reactive oxygen species during the catalytic reaction. To study the role of the enzymatic activity of VAP-1 in PMN extravasation we used an enzymatically inactive VAP-1 mutant, specific amine oxidase inhibitors (including a novel small molecule compound) and anti-VAP-1 antibodies in several flow-dependent models. The enzyme inhibitors diminished PMN rolling on and transmigration through human endothelial cells under conditions of laminar shear stress in vitro. Notably, the enzyme inactivating point mutation abolished the capacity of VAP-1 to mediate transmigration. Moreover, the new VAP-1 inhibitor effectively prevented the extravasation of PMN in an animal model of inflammation. These data show that the oxidase activity of VAP-1 controls PMN exit from the blood during the relatively poorly understood transmigration step.
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