Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate

Elina Kivi, Kati Elima, Kristiina Aalto, Yvonne Nymalm, Kaisa Auvinen, Erkki Koivunen, Diana M. Otto, Paul R. Crocker, Tiina A. Salminen, Marko Salmi, Sirpa Jalkanen

    Research output: Contribution to journalArticlepeer-review

    68 Citations (Scopus)


    Leukocytes migrate from the blood into areas of inflammation by interacting with various adhesion molecules on endothelial cells. Vascular adhesion protein-1 (VAP-1) is a glycoprotein expressed on inflamed endothelium where it plays a dual role: it is both an enzyme that oxidizes primary amines and an adhesin that is involved in leukocyte trafficking to sites of inflammation. Although VAP-1 was identified more than 15 years ago, the counterreceptor(s) for VAP-1 on leukocytes has remained unknown. Here we have identified Siglec-10 as a leukocyte ligand for VAP-1 using phage display screenings. The binding between Siglec-10 and VAP-1 was verified by different adhesion assays, and this interaction was also consistent with molecular modeling. Moreover, the interaction between Siglec-10 and VAP-1 led to increased hydrogen peroxide production, indicating that Siglec-10 serves as a substrate for VAP-1. Thus, the Siglec-10-VAP-1 interaction seems to mediate lymphocyte adhesion to endothelium and has the potential to modify the inflammatory microenvironment via the enzymatic end products. (Blood. 2009; 114: 5385-5392)

    Original languageEnglish
    Pages (from-to)5385-5392
    Number of pages8
    Issue number26
    Early online date27 Oct 2009
    Publication statusPublished - 17 Dec 2009


    • Genetic algorithm
    • Oxidase activity
    • Amine oxidase
    • Lymph nodes
    • VAP-1
    • Endothelium
    • Recognition
    • Cloning
    • Transmigration
    • Molecule


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