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中华外科杂志 1987年第4期25卷 245-247+256页

作者：黄宗海高瀚徐仁宝谭金兴第二军医大学长征医院普通外科第二军医大学病理生理教研室

本实验采用放射配体结合法,研究了肠缺血性休克狗以及感染性休克患者外周血液中白细胞糖皮质激素受体(GCR)的变化。结果发现:实验组动物休克后GCR水平呈进行性降低,其降低的程度与休克病情的严重程度之间有明显的正相关。10名感染性休... 详细信息

本实验采用放射配体结合法,研究了肠缺血性休克狗以及感染性休克患者外周血液中白细胞糖皮质激素受体(GCR)的变化。结果发现:实验组动物休克后GCR水平呈进行性降低,其降低的程度与休克病情的严重程度之间有明显的正相关。10名感染性休克患者的GCR水平显著低于对照组水平。本研究结果为临床上应用大剂量糖皮质激素(GC)抗休克提供了实验依据。

关键词：受体糖皮质激素/代谢休克脓毒性/代谢

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支气管哮喘外周白细胞糖皮质激素受体变化的初步研究

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中华结核和呼吸杂志 1993年第3期16卷 171-171页

作者：刘辉国牛汝楫胡道桢李苏华同济医科大学附属同济医院内科湖北省卫生职工医学院

我们采用放射配基结合分析法测定了33例外源性哮喘、13例内源性哮喘和22例正常人外周血白细胞内糖皮质激素受体(GCR)水平,同时用放免法测定其血浆皮质醇水平。结果:①外源性哮喘患者白细胞GCR为2177±1226位点/细胞,明显低于正常对照

关键词：白细胞受体糖皮质激素/代谢哮喘/免疫学

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流行性出血热肾损害的免疫状态与血浆糖皮质激素及其受体的变化

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中华肾脏病杂志 1991年第1期7卷 39-39,68页

作者：王吉娜王新慧江国良蔡天沛安徽医科大学附院肾内科

The relation between immunity, plasm glucocorticoid (GC) and Lymphocyte glucocorticoid receptor (GCR) number were studied in 4 patients with hemorrhagic fever with nephrntic syndrome (HFNS) by using radioimmune assay and radioligand binding technique. We found that there was increasing of plasm GC and lymphocyte GCR number with the developing of specific immune response in HFRS. This result caused immune inhibitory effect. It may be a reason that HFNS patients occur rarely immune disease after convalescence. It is necessary to further study the relation of immunity and endocrine during immunity diseases.

关键词：肾疾病/免疫学肾综合征出血热/病因学受体糖皮质激素/代谢糖皮质激素类/血液

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Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第25期274卷 18121-18127页

作者： Subramaniam, N Treuter, E Okret, S Huddinge Univ Hosp Karolinska Inst Dept Med Nutr SE-14186 Huddinge Sweden Huddinge Univ Hosp Karolinska Inst Ctr Biotechnol SE-14186 Huddinge Sweden

Recent development in the field of gene regulation by nuclear receptors (NRs) have identified a role for cofactors in transcriptional control. While some of the NR-associated proteins serve as coactivators, the effect of the receptor interacting protein 140 (RIP140) on NR transcriptional responses is complex. In this report we have studied the effect of RIP140 on gene regulation by the glucocorticoid receptor (GR). We demonstrate that RIP140 antagonized all GR-mediated responses tested, which included activation through classical GRE, the synergistic effects of glucocorticoids on AP-1 and Pbx1/HOXB1 responsive elements, as well as gene repression through a negative GRE and cross-talk with NF-kappa B (RelA). This involved the ligand-binding domain of the GR and did not occur when the GR was bound to the antagonist RU486, The strong repressive effect of RIP140 was restricted to glucocorticoid-mediated responses in as much as it slightly increased signaling through the RelA and the Pit-1/Pbx proteins and only slightly repressed signaling through the Pbx1/HOXB1 and AP-1 proteins, excluding general squelching as a mechanism. Instead, this suggests that RIP140 acts as a direct inhibitor of GR function. In line with a direct effect of RIP140 on the GR, we demonstrate a GR-RIP140 interaction in vitro by a glutathione S-transferase-pull down assay. Furthermore, the repressive effect of RIP140 could partially be overcome by overexpression of the coactivator TIF2, which involved a competition between TIF2 and RIP140 for binding to the GR.

关键词：衔接蛋白质类信号转导细胞系基因表达调控/药物作用基因报告糖皮质激素类/药理学核蛋白质类/代谢核蛋白质类/药理学核受体共激活因子2 蛋白质结合受体胞质和核/代谢受体糖皮质激素/遗传学受体糖皮质激素/代谢调控序列核酸阻遏蛋白质类/遗传学十四酰佛波乙酯/药理学转录因子AP-1/代谢转录因子/遗传学转染动物人类

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JAB1 interacts with both the progesterone receptor and SRC-1

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第12期275卷 8540-8548页

作者： Chauchereau, A Georgiakaki, M Perrin-Wolff, M Milgrom, E Loosfelt, H Hop Bicetre INSERM U135 F-94275 Le Kremlin Bicetre France

JAB1 (Jun activation domain-binding protein-1) has previously been described as a coactivator of AP1 transcription factor. We show here, by yeast and mammalian two-hybrid analyses and by pull-down experiments, that JAB1 also interacts with both the progesterone receptor (PR) and the steroid receptor coactivator 1 (SRC-1) and that it stabilizes PR-SRC-1 complexes. We also show that JAB1 potentiates the activity of a variety of transcription factors known to associate with SRC-1 (nuclear receptors, activator protein-1, and nuclear factor KB). This occurs without any modification of PR or SRC-1 concentration. JAB1 is a subunit of a large multiprotein complex that has been called the COP9 signalosome. The latter is present in plant and animal cells and has been shown to be involved in a variety of cellular mechanisms including transcription regulation, cell cycle control, and phosphorylation cascades. We now show that it is also involved in the mechanisms of action of nuclear receptors and of their coactivators.

关键词：结合部位 DNA结合蛋白质类/遗传学 DNA结合蛋白质类/代谢组蛋白酰基转移酶核受体共激活因子1 肽水解酶类蛋白质结合受体胞质和核/代谢受体糖皮质激素/代谢受体孕酮/代谢重组蛋白质类/代谢信号传导转录因子AP-1/代谢转录因子/遗传学转录因子/代谢双杂交系统技术

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Comparison of nucleosome remodeling by the yeast transcription factor Pho4 and the glucocorticoid receptor

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第12期275卷 9035-9042页

作者： Bergh, FT Flinn, EM Svaren, J Wright, AP Hörz, W Univ Munich Inst Physiol Chem D-80336 Munich Germany Karolinska Inst Dept Biosci Novum S-14157 Huddinge Sweden Sodertorns Hogskola S-14104 Huddinge Sweden

Chromatin reorganization of the PHO5 and murine mammary tumor virus (MMTV) promoters is triggered by binding of either Pho4 or the glucocorticoid receptor (GR), respectively. In order to compare the ability of Pho4 and GR to remodel chromatin and activate transcription, hybrid promoter constructs were created by insertion of the MMTV B nucleosome sequence into the PHO5 promoter and then transformed into a yeast strain expressing GR, Activation of either Pho4 (by phosphate depletion) or GR (by hormone addition) resulted in only slight induction of hybrid promoter activity. However, simultaneous activation of both Pho4 and GR resulted in synergistic activation to levels exceeding that of the wild type PHO5 promoter. Under these conditions, Pho4 completely disrupted the nucleosome containing its binding site. In contrast, GR had little effect on the stability of the MMTV B nucleosome. A minimal transactivation domain of the GR fused to the Pho4 DNA-binding domain is capable of efficiently disrupting the nucleosome with a Pho4-binding site, whereas the complementary hybrid protein (Pho4 activation domain, GR DNA-binding domain) does not labilize the B nucleosome. Therefore, we conclude that significant activation by Pho4 requires nucleosome disruption, whereas equivalent transcriptional activation by GR is not accompanied by overt perturbation of nucleosome structure. Our results show that the DNA-binding domains of the two factors play critical roles in determining how chromatin structure is modified during promoter activation.

关键词：染色质/代谢染色质/超微结构 DNA结合蛋白质类真菌蛋白质类/代谢乳房瘤病毒鼠/遗传学核小体/代谢核小体/超微结构启动区遗传蛋白质结合受体糖皮质激素/代谢酿酒酵母菌/遗传学酿酒酵母蛋白质类转录因子/代谢转录激活

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Redox-dependent regulation of nuclear import of the glucocorticoid receptor

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第15期274卷 10363-10371页

作者： Okamoto, K Tanaka, H Ogawa, H Makino, Y Eguchi, H Hayashi, S Yoshikawa, N Poellinger, L Umesono, K Makino, I Asahikawa Med Coll Dept Internal Med 2 Asahikawa Hokkaido 0788510 Japan Kyoto Univ Inst Virus Res Dept Genet & Mol Biol Kyoto 6068507 Japan Saitama Canc Ctr Res Inst Dept Biochem Ina Saitama 3620800 Japan Karolinska Inst Nobel Med Inst Dept Cell & Mol Biol S-17177 Stockholm Sweden

A number of transcription factors including the glucocorticoid receptor (GR) are regulated in a redox-dependent fashion. We have previously reported that the functional activity of the GR is suppressed under oxidative conditions and restored in the presence of reducing reagents. In the present study, we have used a chimeric human GR fused to the Aequorea green fluorescent protein and demonstrated that both ligand-dependent and -independent nuclear translocation of the GR is impaired under oxidative conditions in living cells. Substitution of Cys-481 for Ser within NL1 of the human GR resulted in reduction of sensitivity to oxidative treatment, strongly indicating that Cys-481 is one of the target amino acids for redox regulation of the receptor. Taken together, we may conclude that redox-dependent regulation of nuclear translocation of the GR constitutes an important mechanism for modulation of glucocorticoid-dependent signal transduction.

关键词：氨基酸序列氨基酸取代生物转运/药物作用 CHO细胞 COS细胞细胞核/代谢仓鼠亚科半胱氨酸/代谢绿色荧光蛋白质类过氧化氢/药理学配体发光蛋白质类/遗传学发光蛋白质类/代谢分子序列数据氧化还原氧化性应激受体糖皮质激素/遗传学受体糖皮质激素/代谢重组融合蛋白质类/代谢丝氨酸/代谢信号传导锌指动物人类

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Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1β-induced histone H4 acetylation on lysines 8 and 12

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MOLECULAR AND CELLULAR BIOLOGY 2000年第18期20卷 6891-6903页

作者： Ito, K Barnes, PJ Adcock, IM Natl Heart & Lung Inst Imperial Coll Sch Med London SW3 6LY England

We have investigated the ability of dexamethasone to regulate interleukin-1 beta (IL-1 beta)-induced gene expression, histone acetyltransferase (HAT) and histone deacetylase (HDAC) activity. Low concentrations of dexamethasone (10(-10) M) repress IL-1 beta-stimulated granulocyte-macrophage colony-stimulating factor (GM-CSF) expression and fail to stimulate secretory leukocyte proteinase inhibitor expression. Dexamethasone (10(-7) M) and IL-1 beta (1 ng/ml) both stimulated HAT activity but showed a different pattern of histone H4 acetylation. Dexamethasone targeted lysines K5 and K16, whereas IL-1 beta targeted K8 and K12. Low concentrations of dexamethasone (10(-10) M), which do not transactivate, repressed IL-1 beta-stimulated K8 and K12 acetylation. Using chromatin immunoprecipitation assays, we show that dexamethasone inhibits IL-1 beta-enhanced acetylated K8-associated GM-CSF promoter enrichment in a concentration-dependent manner. Neither IL-1 beta nor dexamethasone elicited any GM-CSF promoter association at acetylated K5 residues. Furthermore, we show that GR acts both as a direct inhibitor of CREB binding protein (CBP)-associated HAT activity and also by recruiting HDAC2 to the p65 CBP HAT complex. This action does not involve de novo synthesis of HDAC protein or altered expression of CBP or p300/CBP-associated factor. This mechanism for glucocorticoid repression is novel and establishes that inhibition of histone acetylation is an additional level of control of inflammatory gene expression. This further suggests that pharmacological manipulation of of specific histone acetylation status is a potentially useful approach for the treatment of inflammatory diseases.

关键词：乙酰化作用乙酰基转移酶类/遗传学结合部位 CREB结合蛋白质细胞周期蛋白质类/遗传学染色质/代谢地塞米松/代谢地塞米松/药理学基因表达/药物作用粒细胞巨噬细胞集落刺激因子/遗传学组蛋白酰基转移酶组蛋白脱乙酰基酶2 组蛋白脱乙酰基酶类/代谢组蛋白类/代谢白细胞介素1/代谢白细胞介素1/药理学赖氨酸/代谢 NF-κB/代谢核蛋白质类/遗传学磷酰化启动区遗传受体糖皮质激素/代谢阻遏蛋白质类反式激活因子类/遗传学转录因子RelA 转录因子转录激活/药物作用肿瘤细胞培养的 p300-CBP转录因子人类

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Resetting of circadian time peripheral tissues by glucocorticoid signaling

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SCIENCE 2000年第5488期289卷 2344-2347页

作者： Balsalobre, A Brown, SA Marcacci, L Tronche, F Kellendonk, C Reichardt, HM Schütz, G Schibler, U Univ Geneva Dept Biol Mol Sci 2 CH-1211 Geneva Switzerland Deutsch Krebsforschungszentrum D-69120 Heidelberg Germany

In mammals, circadian oscillators reside not only in the suprachiasmatic nucleus of the brain, which harbors the central pacemaker, but also in most peripheral tissues. Here, we show that the glucocorticoid hormone analog dexamethasone induces circadian gene expression in cultured rat-1 fibroblasts and transiently changes the phase of circadian gene expression in liver, kidney, and heart. However, dexamethasone does not affect cyclic gene expression in neurons of the suprachiasmatic nucleus. This enabled us to establish an apparent phase-shift response curve specifically for peripheral clocks in intact animals. In contrast to the central clock, circadian oscillators in peripheral tissues appear to remain responsive to phase resetting throughout the day.

关键词：生物钟/生理学细胞周期蛋白质类细胞系昼夜节律/生理学 DNA结合蛋白质类地塞米松/类似物和衍生物地塞米松/药理学基因表达调控/药物作用肾/代谢肝/代谢小鼠近交系突变心肌/代谢神经元/代谢核蛋白质类/遗传学核蛋白质类/代谢周期昼夜节律蛋白质类受体糖皮质激素/遗传学受体糖皮质激素/代谢信号传导上交叉核/代谢转录因子/遗传学转录因子/代谢动物女(雌)性男(雄)性小鼠大鼠

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The glucocorticoid receptor:: Rapid exchange with regulatory sites in living cells

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SCIENCE 2000年第5456期287卷 1262-1265页

作者： McNally, JG Müller, WG Walker, D Wolford, R Hager, GL NCI Lab Receptor Biol & Gene Express Bethesda MD 20892 USA

Steroid receptors bind to site-specific response elements in chromatin and modulate gene expression in a hormone-dependent fashion. With the use of a tandem array of mouse mammary tumor virus reporter elements and a form of glucocorticoid receptor labeled with green fluorescent protein, targeting of the receptor to response elements in live mouse cells was observed. Photobleaching experiments provide direct evidence that the hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment. Thus, the interaction of regulatory proteins with target sites in chromatin is a more dynamic process than previously believed.

关键词：结合部位细胞系转化细胞核/代谢染色质/代谢地塞米松/代谢地塞米松/药理学绿色荧光蛋白质类原位杂交荧光配体发光蛋白质类乳房瘤病毒鼠/遗传学显微镜检查共焦显微镜检查荧光核小体/代谢受体糖皮质激素/代谢反应元件末端重复序列动物小鼠

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