Kang S M, Tran A C, Grilli M, Lenardo M J
Laboratory of Immunology, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
Science. 1992 Jun 5;256(5062):1452-6. doi: 10.1126/science.1604322.
Regulation of interleukin-2 (IL-2) gene expression by the p50 and p65 subunits of the DNA binding protein NF-kappa B was studied in nontransformed CD4+ T lymphocyte clones. A homodimeric complex of the NF-kappa B p50 subunit was found in resting T cells. The amount of p50-p50 complex decreased after full antigenic stimulation, whereas the amount of the NF-kappa B p50-p65 heterodimer was increased. Increased expression of the IL-2 gene and activity of the IL-2 kappa B DNA binding site correlated with a decrease in the p50-p50 complex. Overexpression of p50 repressed IL-2 promoter expression. The switch from p50-p50 to p50-p65 complexes depended on a protein that caused sequestration of the p50-p50 complex in the nucleus.
在未转化的CD4 + T淋巴细胞克隆中研究了DNA结合蛋白NF-κB的p50和p65亚基对白细胞介素-2（IL-2）基因表达的调控。在静息T细胞中发现了NF-κB p50亚基的同二聚体复合物。完全抗原刺激后，p50-p50复合物的量减少，而NF-κB p50-p65异二聚体的量增加。IL-2基因表达的增加和IL-2 κB DNA结合位点的活性与p50-p50复合物的减少相关。p50的过表达抑制了IL-2启动子的表达。从p50-p50复合物到p50-p65复合物的转变取决于一种导致p50-p50复合物在细胞核中隔离的蛋白质。
