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.
Cvoro
A
A
Department of Biochemistry, Institute for Biological Research, 29. Novembra 142, 11060 Belgrade, Yugoslavia.
Matić
G
G
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