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

E Kivi, K Elima, K Aalto, Y Nymalm, K Auvinen, E Koivunen, DM Otto, PR Crocker, Tiina Salminen, M Salmi, S Jalkanen

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    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 languageUndefined/Unknown
    Pages (from-to)5385–5392
    Number of pages8
    Issue number26
    Publication statusPublished - 2009
    MoE publication typeA1 Journal article-refereed

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