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

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: Kivi E, Elima K, Aalto K, Nymalm Y, Auvinen K, Koivunen E, Otto DM, Crocker PR, Salminen TA, Salmi M, Jalkanen S
Publiceringsår: 2009
Tidskrift: Blood
Tidskriftsakronym: BLOOD
Volym: 114
Nummer: 26
Artikelns första sida, sidnummer: 5385
Artikelns sista sida, sidnummer: 5392
Antal sidor: 8
ISSN: 0006-4971


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)

Senast uppdaterad 2019-14-11 vid 04:08