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- W2177209358 abstract "Although low doses of tumor-derived stress protein gp96 elicit protective immunity to the tumor from which it is isolated, protection is lost at high doses because of the induction of immunoregulatory CD4+ T cells. This study evaluated the influence of gp96 on resting rat bone marrow-derived dendritic cells (BMDCs) and purified CD3+ T cells. In contrast to previous reports, gp96 had no effect on adhesion and costimulatory molecule expression by BMDCs, nor did it influence interleukin (IL)-10 and IL-12 secretion or their allostimulatory capacity. Gp96 did not bind to BMDCs but dose-dependently bound to CD4+ and CD8+ T cells. At low concentrations (1 and 25 microg/mL), gp96 acted as a costimulator of CD3+ T cells, inducing proliferation and the secretion of interferon (IFN)-gamma- and IL-10. Gp96 also increased the proliferation of CD28-costimulated CD3+ T cells and their secretion of IFN-gamma, IL-4, and IL-10. Gp96 had no effect at higher concentrations (50 and 100 microg/mL), despite the occurrence of cell surface binding at these concentrations. These findings indicate that gp96 can act as a costimulatory molecule for CD3+ T cells, and an observed increase in the IL-10: IFN-gamma secretion ratio induced by gp96 suggests that it might, at appropriate concentrations, promote a regulatory T-helper 2 (Th2)-like phenotype." @default.
- W2177209358 created "2016-06-24" @default.
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- W2177209358 date "2006-01-01" @default.
- W2177209358 modified "2023-09-25" @default.
- W2177209358 title "The stress protein gp96 is not an activator of resting rat bone marrow–derived dendritic cells, but is a costimulator and activator of CD3+ T cells" @default.
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- W2177209358 doi "https://doi.org/10.1379/csc-208.1" @default.
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