Carbohydrates located on the top of the "cap" contribute to the adhesive and enzymatic functions of vascular adhesion protein-1

Sanna-Mari Maula, Tiina Salminen, Sam Kaitaniemi, Yvonne Nymalm, David J. Smith, Sirpa Jalkanen

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

    23 Citeringar (Scopus)

    Sammanfattning

    Vascular adhesion protein 1 (VAP-1) is an endothelial adhesion molecule with an enzymatic activity. It deaminates biogenic amines, resulting in the formation of aldehydes and hydrogen peroxide. During the enzymatic reaction a transient Schiff base is formed between endothelial VAP-1 and its leukocytic ligand, and this interaction is important for lymphocyte adhesion. VAP-1 monomer has six potential N-linked, and three putative O-linked glycosylation sites and an SSSS sequence potentially forming an attachment site for an adjacent O-linked site. In this work we modeled the carbohydrate decorations on a structural model of VAP-1, and studied which of those potential glycosylation sites are utilized, and whether those decorations accessible to a lymphocyte ligand are important in lymphocyte adhesion and enzymatic activity of VAP-1. We show that, unlike the O-linked attachment sites, all six N-linked glycosylation sites are in use. Furthermore, mutation of the N-linked attachment sites strategically located on the top of the molecule reduces lymphocyte adhesion in non-static conditions, and enhances the catalytic activity of membrane-bound human VAP-1 in static conditions, suggesting that glycosylation regulates the functional properties of VAP-1.

    OriginalspråkEngelska
    Sidor (från-till)2718-2727
    Antal sidor10
    TidskriftEuropean Journal of Immunology
    Volym35
    Nummer9
    DOI
    StatusPublicerad - sep. 2005
    MoE-publikationstypA1 Tidskriftsartikel-refererad

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