| First Author | Matsumoto M | Year | 2009 |
| Journal | J Immunol | Volume | 183 |
| Issue | 11 | Pages | 7204-11 |
| PubMed ID | 19890058 | Mgi Jnum | J:157397 |
| Mgi Id | MGI:4430772 | Doi | 10.4049/jimmunol.0902173 |
| Citation | Matsumoto M, et al. (2009) P-selectin glycoprotein ligand-1 negatively regulates T-cell immune responses. J Immunol 183(11):7204-11 |
| abstractText | Cell surface sialomucins often act as antiadhesive molecules by virtue of their extended structure and negative charge. CD43 is one such sialomucin, expressed on most leukocytes. P-selectin glycoprotein ligand-1 (PSGL-1) is another sialomucin expressed by leukocytes. It serves as a major selectin ligand, but no antiadhesive role for it has been described. In this study, we showed that PSGL-1-deficient T cells, like CD43-deficient T cells, exhibited increased adhesion and proliferation compared with wild-type cells. The loss of both PSGL-1 and CD43 led to a further increase in T cell adhesion and proliferation. The reexpression of full-length PSGL-1 or CD43 in double-deficient CD4(+) T cells reversed their increased adhesion and proliferation phenotype. Using chimeric constructs of human CD8 and either PSGL-1 or CD43, we demonstrated that the intracellular domain of PSGL-1 or CD43 is required for suppressing proliferation but not adhesion. Furthermore, in a mouse model of inflammatory bowel disease induced by the adoptive transfer of naive T cells into RAG-deficient hosts, a PSGL-1 deficiency exacerbated the development of inflammation. These results reveal a novel regulatory role for PSGL-1 in T cell adhesion and proliferation and suggest that PSGL-1 negatively regulates T cell immune responses in vivo. |
