Vidović S, Cvoro A, Dundjerski J, Trajković D, Matić G
School of Medicine, University of Banja Luka, Department of Biology and Human Genetics, Belgrade, Yugoslavia.
Cell Biol Int. 1996 Aug;20(8):553-9. doi: 10.1006/cbir.1996.0072.
Binding capacity of the cytoplasmic and nuclear glucocorticoid receptor (GR) and the activity of tyrosine aminotransferase (TAT) were examined in the liver of intact and adrenalectomized rats exposed to 41 degrees C whole body hyperthermic stress. In glucocorticoid-deprived animals, stress-induced decrease in the cytoplasmic steroid binding was followed by parallel increases in its nuclear binding and TAT activity, suggesting a stimulation of TAT gene transcription by the GR in the absence of the ligand. In intact animals, however, a diminution of the steroid binding in the cytosol, its unchanged nuclear binding and an impairment of TAT activity were observed upon the stress. The results imply that stress could elicit different structural or functional alterations of unliganded vs liganded GR.
在暴露于41摄氏度全身热应激的完整大鼠和肾上腺切除大鼠的肝脏中,检测了细胞质和细胞核糖皮质激素受体(GR)的结合能力以及酪氨酸转氨酶(TAT)的活性。在糖皮质激素缺乏的动物中,应激诱导的细胞质类固醇结合减少之后,其细胞核结合和TAT活性平行增加,这表明在没有配体的情况下,GR刺激了TAT基因转录。然而,在完整动物中,应激时观察到细胞质中类固醇结合减少、细胞核结合不变以及TAT活性受损。结果表明,应激可能引发未结合配体与结合配体的GR不同的结构或功能改变。