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Mercury stimulates rat liver glucocorticoid receptor association with Hsp90 and Hsp70
Author(s) -
Brkljačić Jelena,
Milutinović Danijela Vojnović,
Dundjerski Jadranka,
Matić Gordana
Publication year - 2004
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20032
Subject(s) - glucocorticoid receptor , hsp90 , hsp70 , cytosol , heat shock protein , glucocorticoid , receptor , mercury (programming language) , endocrinology , chemistry , medicine , biology , biochemistry , enzyme , gene , computer science , programming language
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. © 2004 Wiley Periodicals, Inc. J Biochem Mol Toxicol 18:257–260, 2004 Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20032