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Regulation of glucocorticoid receptor function and angiotensin-converting enzyme activity
Author(s) -
P P Golikov
Publication year - 1997
Publication title -
problems of endocrinology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.124
H-Index - 5
eISSN - 2308-1430
pISSN - 0375-9660
DOI - 10.14341/probl199743451-54
Subject(s) - cytoplasm , endoplasmic reticulum , glucocorticoid receptor , receptor , microbiology and biotechnology , glucocorticoid , biology , chaperone (clinical) , heat shock protein , endocrinology , chemistry , medicine , gene , biochemistry , pathology
The central link in the mechanism of action of glucocorticoids is specific cytoplasmic glucocorticoid receptors (GH). Their synthesis is programmed by 1 gene of chromosome 5 [44]. The direct biosynthesis of GR occurs in the endoplasmic reticulum of the cytoplasm [12]. In the cytoplasm, GRs bind to heat shock proteins (HSP, chaperone proteins) mol. mass of 50, 70, 90 kD [20, 59]. Like the mass of the GR – HSP complex is 300 kD [14]. In the absence of glucocorticoids, GRs are localized mainly in the cytoplasm [30, 63]. In 1 cell contains from 5000 to 100 000 specific GH. GRs have been found in many mammalian tissues [13], however, certain tissues do not contain GRs: the intermediate pituitary, Kupffer and endothelial cells of the liver, renal glomeruli, and proximal convoluted tubules [12, 31].

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