Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Base Sequence
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Binding Sites
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CD4 Antigens / immunology*
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Cell Line
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Cell Nucleus / physiology
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Chloramphenicol O-Acetyltransferase / genetics
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Chloramphenicol O-Acetyltransferase / metabolism
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Clone Cells
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Columbidae
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DNA / genetics
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Gene Expression Regulation*
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Interleukin-2 / genetics*
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Macromolecular Substances
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Mice
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Molecular Sequence Data
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NF-kappa B / metabolism*
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Oligonucleotide Probes
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Promoter Regions, Genetic
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RNA, Messenger / metabolism
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Recombinant Fusion Proteins / metabolism
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T-Lymphocyte Subsets / immunology*
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Transfection
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Tumor Necrosis Factor-alpha / pharmacology
Substances
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CD4 Antigens
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Interleukin-2
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Macromolecular Substances
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NF-kappa B
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Oligonucleotide Probes
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RNA, Messenger
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Recombinant Fusion Proteins
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Tumor Necrosis Factor-alpha
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DNA
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Chloramphenicol O-Acetyltransferase