| First Author | Tahara-Hanaoka S | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 329 |
| Issue | 3 | Pages | 996-1000 |
| PubMed ID | 15752754 | Mgi Jnum | J:97476 |
| Mgi Id | MGI:3575493 | Doi | 10.1016/j.bbrc.2005.02.067 |
| Citation | Tahara-Hanaoka S, et al. (2005) Identification and characterization of murine DNAM-1 (CD226) and its poliovirus receptor family ligands. Biochem Biophys Res Commun 329(3):996-1000 |
| abstractText | The leukocyte adhesion molecule DNAM-1 (CD226) is a member of the immunoglobulin superfamily and constitutively expressed on the majority of CD4+ and CD8+ T lymphocytes, natural killer (NK) cells, monocytes/macrophages, and a subset of B lymphocytes. The poliovirus receptor (PVR; CD155) and its family member nectin 2 (CD112) have recently been identified as the ligands for DNAM-1. Interaction of DNAM-1 with the ligands induces NK cell- and CD8+ T cell-mediated cytotoxicity and cytokine secretion. However, in vivo function of the receptor-ligand interaction has remained unclear. Here, we identified murine DNAM-1 and PVR homologues that physically and functionally bind each other. We demonstrated that ligand binding of murine DNAM-1 induced a costimulatory signal in antigen-specific CD8+ T cells. These results should provide a useful animal model to explore a role of DNAM-1 in immune responses in vivo. |
