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汞刺激大鼠肝脏糖皮质激素受体与热休克蛋白90(Hsp90)和热休克蛋白70(Hsp70)的结合。

Mercury stimulates rat liver glucocorticoid receptor association with Hsp90 and Hsp70.

作者信息

Brkljacić Jelena, Milutinović Danijela Vojnović, Dundjerski Jadranka, Matić Gordana

机构信息

Department of Biochemistry, Institute for Biological Research, 29th November 142, 11060 Belgrade, Serbia and Montenegro.

出版信息

J Biochem Mol Toxicol. 2004;18(5):257-60. doi: 10.1002/jbt.20032.

Abstract

The subject of the present study is the influence of mercury on association of rat liver glucocorticoid receptor (GR) with heat shock proteins Hsp90 and Hsp70. The glucocorticoid receptor heterocomplexes with Hsp90 and Hsp70 were immunopurified from the liver cytosol of rats administered with different doses of mercury. The amounts of co-immunopurified apo-receptor, Hsp90 and Hsp70 were then determined by quantitative Western blotting. The ratio between the amount of heat shock protein Hsp90 or Hsp70 and the amount of apo-receptor within immunopurified heterocomplexes was found to increase in response to mercury administration. On the other hand, the levels of Hsp90 and Hsp70 in hepatic cytosol remained unaltered. The finding that mercury stimulates association of the two heat shock proteins with the glucocorticoid receptor, rendering the cytosolic heat shock protein levels unchanged, suggests that mercury affects the mechanisms controlling the assembly of the receptor heterocomplexes.

摘要

本研究的主题是汞对大鼠肝脏糖皮质激素受体(GR)与热休克蛋白Hsp90和Hsp70结合的影响。从给予不同剂量汞的大鼠肝脏胞质溶胶中免疫纯化出与Hsp90和Hsp70形成的糖皮质激素受体异源复合物。然后通过定量蛋白质免疫印迹法测定共免疫纯化的无激素受体、Hsp90和Hsp70的量。结果发现,给予汞后,免疫纯化的异源复合物中热休克蛋白Hsp90或Hsp70的量与无激素受体的量之比增加。另一方面,肝脏胞质溶胶中Hsp90和Hsp70的水平保持不变。汞刺激这两种热休克蛋白与糖皮质激素受体结合,而胞质热休克蛋白水平不变,这一发现表明汞影响受体异源复合物组装的调控机制。

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