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つくばリポジトリ (Tulips-R) >
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Biochemical and biophysical research communications >
Please use this identifier to cite or link to this item:
http://hdl.handle.net/2241/101999
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| Title: | Identification and characterization of murine DNAM-1 (CD226) and its poliovirus receptor family ligands |
| Authors: | Tahara-Hanaoka, Satoko
Miyamoto, Akitomo
Hara, Ayumi
Honda, Shin-ichiro
Shibuya, Kazuko
Shibuya, Akira
渋谷, 彰
渋谷, 和子
本多, 伸一郎
田原, 聡子 |
| Issue Date: | Apr-2005 |
| Publisher: | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| Journal Title: | Biochemical and biophysical research communications |
| Volume: | 329 |
| Issue: | 3 |
| Start Page: | 996 |
| End Page: | 1000 |
| DOI: | 10.1016/j.bbrc.2005.02.067 |
| PMID: | 15752754 |
| Abstract: | 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. |
| URI: | http://hdl.handle.net/2241/101999 |
| Rights: | Copyright © 2005 Elsevier Inc. |
| Text Version: | author |
| Appears in Collections: | Biochemical and biophysical research communications
渋谷 和子 (Shibuya Kazuko)
本多 伸一郎 (Honda Shin-ichiro)
田原 聡子 (Tahara Satoko)
渋谷 彰 (Shibuya Akira)
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