Identification and characterization of murine DNAM-1 (CD226) and its poliovirus receptor family ligands

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 fami...

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Published inBiochemical and biophysical research communications Vol. 329; no. 3; pp. 996 - 1000
Main Authors Tahara-Hanaoka, Satoko, Miyamoto, Akitomo, Hara, Ayumi, Honda, Shin-ichiro, Shibuya, Kazuko, Shibuya, Akira
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.04.2005
ACADEMIC PRESS INC ELSEVIER SCIENCE
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ISSN0006-291X
1090-2104
DOI10.1016/j.bbrc.2005.02.067

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Summary: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.
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ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.02.067