Regulation of nuclear factor-kappa B and activator protein-1 activities after stimulation of T cells via glycosylphosphatidylinositol-anchored Ly-6A/E.

摘要: Cross-linking of glycosylphosphatidylinositol-anchored proteins, including mouse Ly-6A/E, leads to IL-2 secretion and T cell activation, whereas engagement Ly-6A/E uniquely inhibits production induced via TCR. However, little is known concerning the molecular mechanism by which proteins regulate expression. In this study, we have examined ability an anti-Ly-6A/E mAb transcription factors controlling Stimulation EL4J(Ly-6E).A4 cells with anti-CD3 epsilon or anti-Ly6A/E mAbs nuclear factor (NF)-kappa B p65-p50 (RelA/p50) AP-1 (Fos/Jun) binding activities increased activated (NF-AT) activity, octamer-binding NF-Y levels were stable. Cyclic AMP response element protein cell-specific factor-1 (alpha) selectively enhanced epsilon, but not anti-Ly6A/E, suggests that signaling TCR Ly-6 identical. Costimulation these both produced substantially reduced AP-1, NF-AT, and, especially, NF-kappa cyclic factor-1(alpha) a level seen after stimulation epsilon. The inducibility enhancer in vivo contribution individual for induction assessed use reporter chloramphenicol acetyltransferase constructs containing oligomerized sites factors. These experiments also demonstrated key role transcriptional regulation gene TCR- Ly6A/E-mediated signaling. By using 2B4.11 hybridoma mutated variant, revealed crucial zeta-chain activation B.