Function-blocking antibodies to human vascular adhesion protein-1: A potential anti-inflammatory therapy

C. M. Kirton, Marja-Leena Laukkanen, A. Nieminen, M. Merinen, C. M. Stolen, K. Armour, D. J. Smith, M. Salmi, S. Jalkanen, M. R. Clark (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    26 Citations (Scopus)

    Abstract

    Human vascular adhesion protein‐1 (VAP‐1) is a homodimeric 170‐kDa sialoglycoprotein that is expressed on the surface of endothelial cells and functions as a semicarbazide‐sensitive amine oxidase and as an adhesion molecule. Blockade of VAP‐1 has been shown to reduce leukocyte adhesion and transmigration in in vivo and in vitro models, suggesting that VAP‐1 is a potential target for anti‐inflammatory therapy. In this study we have constructed mouse‐human chimeric antibodies by genetic engineering in order to circumvent the potential problems involved in using murine antibodies in man. Our chimeric anti‐VAP‐1 antibodies, which were designed to lack Fc‐dependent effector functions, bound specifically to cell surface‐expressed recombinant human VAP‐1 and recognized VAP‐1 in different cell types in tonsil. Furthermore, the chimeric antibodies prevented leukocyte adhesion and transmigration in vitro and in vivo. Hence, these chimeric antibodies have the potential to be used as a new anti‐inflammatory therapy.
    Original languageEnglish
    Pages (from-to)3119 - 3130
    Number of pages12
    JournalEuropean Journal of Immunology
    Volume35
    Issue number11
    DOIs
    Publication statusPublished - 2005
    MoE publication typeA1 Journal article-refereed

    Keywords

    • Chimeric antibody
    • Cell adhesion
    • Vascular adhesion protein-1
    • Fc receptor

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