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Vascular adhesion protein-1 (VAP-1)

  • Chapter
Adhesion Molecules: Function and Inhibition

Part of the book series: Progress in Inflammation Research ((PIR))

Abstract

In 1980s the leukocyte adhesion molecules and their ligands on the vascular endothelium were thought to explain tissue-selective, or even tissue-specific, leukocyte traffic. At the same time it became apparent that vessels in inflamed joints displayed binding characteristics clearly distinct from those in peripheral lymph nodes, gut and skin. In search of joint-selective endothelial adhesion molecules we therefore isolated vascular fragments from inflamed human synovial samples to raise monoclonal antibodies (mAbs) against endothelial antigens [1]. From this screen, we identified an mAb, 1B2, that readily stained synovial blood vessels and inhibited lymphocyte adhesion in classical frozen section binding assays. Differential screening against other known endothelial adhesion molecules allowed us to conclude that we had identified a new adhesion molecule. This antigen was named vascular adhesion protein-1 (VAP-1; nowadays also known by the gene name amine oxidase copper containing -3, AOC3).

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Author information

Authors and Affiliations

  1. MediCity Research Laboratory and Department of Microbiology and Immunology, University of Turku, 20520, Turku, Finland

    Marko Salmi

  2. Department of Bacterial and Inflammatory Diseases, National Public Health Institute, 20520, Turku, Finland

    Sirpa Jalkanen

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  1. Marko Salmi
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  2. Sirpa Jalkanen
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Editors and Affiliations

  1. La Jolla Institute for Allergy & Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA

    Klaus Ley

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Salmi, M., Jalkanen, S. (2007). Vascular adhesion protein-1 (VAP-1). In: Ley, K. (eds) Adhesion Molecules: Function and Inhibition. Progress in Inflammation Research. Birkhäuser Basel. https://doi.org/10.1007/978-3-7643-7975-9_10

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