共查询到20条相似文献,搜索用时 890 毫秒
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Subtle metabolic and liver gene transcriptional changes underlie diet-induced fatty liver susceptibility in insulin-resistant mice 总被引:2,自引:1,他引:1
Toye AA Dumas ME Blancher C Rothwell AR Fearnside JF Wilder SP Bihoreau MT Cloarec O Azzouzi I Young S Barton RH Holmes E McCarthy MI Tatoud R Nicholson JK Scott J Gauguier D 《Diabetologia》2007,50(9):1867-1879
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Role of Transcriptional Factors in Stellate Cell Activation 总被引:3,自引:0,他引:3
Richard A. Rippe 《Alcoholism, clinical and experimental research》1999,23(5):926-929
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Estrogen-like activity of metals in MCF-7 breast cancer cells 总被引:14,自引:0,他引:14
Martin MB Reiter R Pham T Avellanet YR Camara J Lahm M Pentecost E Pratap K Gilmore BA Divekar S Dagata RS Bull JL Stoica A 《Endocrinology》2003,144(6):2425-2436
The ability of metals to activate estrogen receptor-alpha (ERalpha) was measured in the human breast cancer cell line, MCF-7. Similar to estradiol, treatment of cells with the divalent metals copper, cobalt, nickel, lead, mercury, tin, and chromium or with the metal anion vanadate stimulated cell proliferation; by d 6, there was a 2- to 5-fold increase in cell number. The metals also decreased the concentration of ERalpha protein and mRNA by 40-60% and induced expression of the estrogen-regulated genes progesterone receptor and pS2 by1.6- to 4-fold. Furthermore, there was a 2- to 4-fold increase in chloramphenicol acetyltransferase activity after treatment with the metals in COS-1 cells transiently cotransfected with the wild-type receptor and an estrogen-responsive chloramphenicol acetyltransferase reporter gene. The ability of the metals to alter gene expression was blocked by an antiestrogen, suggesting that the activity of these compounds is mediated by ERalpha. In binding assays the metals blocked the binding of estradiol to the receptor without altering the apparent binding affinity of the hormone (K(d) = 10(-10) M). Scatchard analysis employing either recombinant ERalpha or extracts from MCF-7 cells demonstrated that (57)Co and (63)Ni bind to ERalpha with equilibrium dissociation constants of 3 and 9.5 x 10(-9) and 2 and 7 x 10(-9) M, respectively. The ability of the metals to activate a chimeric receptor containing the hormone-binding domain of ERalpha suggests that their effects are mediated through the hormone-binding domain. Mutational analysis identified amino acids C381, C447, E523, H524, N532, and D538 as potential interaction sites, suggesting that divalent metals and metal anions activate ERalpha through the formation of a complex within the hormone-binding domain of the receptor. 相似文献
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CPF: An orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7α-hydroxylase gene 总被引:6,自引:0,他引:6 下载免费PDF全文
Masahiro Nitta Sherry Ku Chaline Brown Arthur Y. Okamoto Bei Shan 《Proceedings of the National Academy of Sciences of the United States of America》1999,96(12):6660-6665
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