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* MediCity Research Laboratory, Turku University and National Public Health Institute, Department in Turku, Turku, Finland; and
VTT Biotechnology and Food Research, Espoo, Finland
1Correspondence: MediCity Research Laboratory, Tykistökatu 6A, FIN-20520 Turku, Finland. E-mail: marko.salmi{at}utu.fi
Granulocyte extravasation from the blood into tissues is a
prerequisite for a proper inflammatory response. It is regulated by a
multistep adhesion cascade consisting of successive contacts between
leukocyte surface receptors and their endothelial ligands on vessels.
Vascular adhesion protein 1 (VAP-1) is an endothelial surface
glycoprotein with two functions. It is an enzyme (monoamine oxidase)
and an adhesion molecule for lymphocytes. Its function in binding of
granulocytes or in leukocyte trafficking into sites of inflammation
in vivo has remained unknown. Here we show that
treatment of rabbits with anti-VAP-1 monoclonal antibodies abrogates
70% of granulocyte extravasation into a site of an experimental
inflammation. Using intravital microscopy, VAP-1 blockade is shown to
increase the velocity of the rolling granulocytes and the frequency of
their jerky skippings during the rolling. In addition, the number of
firmly bound leukocytes decreased by 44% when VAP-1 was rendered
nonfunctional. Our results suggest that VAP-1 functions as a molecular
brake early in the adhesion cascade and consequently decreases the firm
adherence; it may also directly influence the transmigration step.
These data elucidate a new interplayer in the granulocyte extravasation
process and provide a novel physiological function for a member of the
monoamine oxidase family.—Tohka, S., Laukkanen, M.-L., Jalkanen, S.,
Salmi, M. Vascular adhesion protein 1 (VAP-1) functions as a molecular
brake during granulocyte rolling and mediates their recruitment
in vivo.
Key Words: inflammation • rolling • extravasation • migration • monoamine oxidases
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