Glucocorticoid receptor interaction with Hsp90 remains unaltered after whole body hyperthermia.
The influence of 41 degrees C whole body hyperthermic stress on glucocorticoid receptor (GR) association with 90-kDa heat shock protein (Hsp90) in the rat liver cytosol was examined. Total cytosolic GR and Hsp90 concentrations, as well as the amount of Hsp90 co-immunoprecipitated with the GR were determined by quantitative Western blotting using BuGR2 as anti-GR and AC88 as anti-Hsp90 monoclonal antibody. After exposure of the animals to the heat stress, the level of cytosolic Hsp90 increased, while its ratio to apo-receptor within non-activated GR heterooligomeric complexes remained unaltered. Therefore, the Hsp90 recruitment by the GR was not dependent on Hsp90 total cytosolic concentration.
Department of Biochemistry, Institute for Biological Research, 29. Novembra 142, 11060 Belgrade, Yugoslavia.
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Cvoro
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Matić
D000315:Adrenalectomy; D000818:Animals; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D001831:Body Temperature / Q000502:physiology; D003600:Cytosol / Q000378:metabolism; D019281:Dimerization; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D018869:Heat-Shock Response / Q000502:physiology; D006979:Hyperthermia, Induced; D008099:Liver / Q000378:metabolism; D008297:Male; D011233:Precipitin Tests; D011485:Protein Binding / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D013312:Stress, Physiological / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D018841:HSP90 Heat-Shock Proteins; D011965:Receptors, Glucocorticoid