INTERFERENCE BETWEEN PATHWAY-SPECIFIC TRANSCRIPTION FACTORS - GLUCOCORTICOIDS ANTAGONIZE PHORBOL ESTER-INDUCED AP-1 ACTIVITY WITHOUT ALTERING AP-1 SITE OCCUPATION INVIVO
INTERFERENCE BETWEEN PATHWAY-SPECIFIC TRANSCRIPTION FACTORS - GLUCOCORTICOIDS ANTAGONIZE PHORBOL ESTER-INDUCED AP-1 ACTIVITY WITHOUT ALTERING AP-1 SITE OCCUPATION INVIVO
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DOI：
10.1002/j.1460-2075.1992.tb05283.x
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发表时间：
1992-06-01
期刊：
影响因子：
11.4
通讯作者：
HERRLICH, P
中科院分区：
文献类型：
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作者：
KONIG, H;PONTA, H;HERRLICH, P
佛波酯刺激和糖皮质激素下调多种启动子，如通过转录因子AP-1（Fos/Jun）的胶原酶基因。我们现在通过胶原酶启动子的基因组足迹显示，佛波醇酯处理细胞导致AP-1与其同源DNA结合位点在体内结合。在活细胞中获得的DNA-蛋白质接触也在体外使用克隆的DNA和纯化的AP-1发现。尽管体外合成的糖皮质激素受体可以干扰Jun同源二聚体的DNA结合，但它不干扰Fos-Jun异源二聚体或纯化的AP-1的体外结合。一致地，完全抑制剂量的糖皮质激素在体内引起AP-1结合位点的表观占据没有变化。激素受体本身不与DNA结合而起作用。
Phorbol esters stimulate and glucocorticoid hormones down-regulate a variety of promoters such as that of the collagenase gene through the transcription factor AP-1 (Fos/Jun). We now show by genomic footprinting of the collagenase promoter that phorbol ester treatment of cells results in the binding of AP-1 to its cognate DNA binding site in vivo. The DNA-protein contacts obtained in living cells are also found in vitro using cloned DNA and purified AP-1. Although in vitro synthesized glucocorticoid receptor can disturb the DNA binding of Jun homodimers, it does not interfere with the binding of Fos-Jun heterodimers or of purified AP-1 in vitro. Consistently, fully inhibitory doses of glucocorticoid hormone cause no change in apparent occupation of the AP-1 binding site in vivo. The hormone receptor acts without itself binding to DNA.