MORIKUNI Tadahiro Osaka Dental Univ. Dept. of Dentistry, Associate Professor, 歯学部, 講師 (60098027)
UMEHARA Hisanori Osaka Dental Univ. Dept. of Dentistry, Associate Professor, 歯学部, 講師 (70247881)
IMAI Hisao Osaka Dental Univ. Dept. of Dentistry, Professor, 歯学部, 教授 (80067024)
NAGANO Yutaka Osaka Dental Univ. Dept. of Dentistry, Associate Professor, 歯学部, 講師 (80228048)
|Budget Amount *help
¥2,700,000 (Direct Cost : ¥2,700,000)
Fiscal Year 1999 : ¥1,300,000 (Direct Cost : ¥1,300,000)
Fiscal Year 1998 : ¥1,400,000 (Direct Cost : ¥1,400,000)
Periodontitis is chronic inflammation caused by immunocompetent cells activated by pathologic bacteria. We investigated the interaction between T cells and fibroblasts, and costimulatory effects of CD2 stimulation on IL-2-mediated NK cell proliferation and signal pathways through CD2 and IL-2 using NK cell line, NK3.3.
PHA-activated T cells adhered to ICAM-1 and ECMs in a dose-dependent manner and PMA markedly enhanced the adhesion of PHA-activated T cells to ICAM and ECMs. The CC-chemokines, such as MCP-1 and RANTES, enhanced adhesion of PHA-activated T cells to ICAM-1, but not to ECMs, whereas, the CX3C-chemokine, fractalkine had no effect on PHA-activated T cell adhesion. To examine the natural setting of the interaction between T cells and fibroblasts, the binding of PHA-activated T cells to immobilized fibroblast like cell line, E11 cells was examined. We found that adhesion of PHA-activated T cells to E11 cells was ICAM-1 dependent and that MCP-1 and RANTES, but not fractalkine, enhanced binding of PHA-activated T cells to E11 cells. These results suggest that some chemokines have important roles in adhesion of T cells to fibroblasts, which may be involved in pathogenesis of periodontitis through enhancing immunologic reaction at the inflammatory sites.
Costimulation of CD2 crosslinking significantly enhanced IL-2-mediated NK3.3 proliferation. Crosslinking of CD2 induced tyrosine phosphorylation of protein tyrosine kinase, Syk and adapter proteins, Shc and Cbl. However, IL-2 stimulation enhanced tyrosine phosphorylation of Shc, but not Syk nor Cbl. Cbl constitutively associates with Grb2 through N-SH3 domain, whereas Shc associates with Grb2 through SH2 domain in an activation-dependent manner.