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* Liver Research Laboratories, University of Birmingham Institute of Clinical Science, Medical Research Council Center for Immune Regulation, Edgbaston, Birmingham, United Kingdom; and
Medicity Research Laboratories, University of Turku, Turku, Finland
Vascular adhesion protein-1 (VAP-1) is an amine oxidase and
adhesion receptor that is expressed by endothelium in the human liver.
The hepatic sinusoids are perfused by blood at low flow rates, and
sinusoidal endothelium lacks selectin expression and has low levels of
CD31, suggesting that VAP-1 may play a specific role in lymphocyte
recruitment to the liver. In support of this we now report the
constitutive expression of VAP-1 on human hepatic sinusoidal
endothelial cells (HSEC) in vitro and demonstrate that VAP-1 supports
adhesion and transmigration of lymphocytes across these cells under
physiological shear stress. These are the first studies to report the
function of VAP-1 on primary human endothelial cells. Under static
conditions lymphocyte adhesion to unstimulated HSEC was dependent on
VAP-1 and ICAM-2, whereas adhesion to TNF-
-stimulated HSEC was
dependent on ICAM-1, VCAM-1, and VAP-1. Under conditions of flow,
blocking VAP-1 reduced lymphocyte adhesion to TNF--treated HSEC by
50% and significantly reduced the proportion of adherent lymphocytes
that transmigrated across cytokine or LPS-activated endothelium. In
addition, inhibition of the amine oxidase activity of VAP-1 reduced
both adhesion and transmigration of lymphocytes to a level similar to
that seen with VAP-1 Ab. Thus, VAP-1 can support transendothelial
migration as well as adhesion, and both functions are dependent on its
enzymatic activity. In the absence of selectins and CD31, VAP-1 may
play a specific role in lymphocyte recruitment via hepatic sinusoidal
endothelium. Moreover, since VAP-1 is induced on nonhepatic endothelium
in response to inflammation, its ability to support lymphocyte
transendothelial migration may be an important systemic function of
VAP-1.
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