| First Author | Kivi E | Year | 2009 |
| Journal | Blood | Volume | 114 |
| Issue | 26 | Pages | 5385-92 |
| PubMed ID | 19861682 | Mgi Jnum | J:155834 |
| Mgi Id | MGI:4415776 | Doi | 10.1182/blood-2009-04-219253 |
| Citation | Kivi E, et al. (2009) Human Siglec-10 can bind to vascular adhesion protein-1 and serves as its substrate. Blood 114(26):5385-92 |
| abstractText | 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. |
