Title | The receptor for glucocorticoid hormones: an insight into its structure and cellular dynamics | |
Authors | M.N. Alexis, I. Mavridou, L. Baki and C. KioussiBiological Research Center, The National Hellenic Research Foundation | |
Citation | Alexis, M.N., Mavridou, I., Baki L. and Kioussi, C.: The Receptor for Glucocorticoid Hormones: an insight into its structure and cellular dynamics, Epitheorese Klin. Farmakol. Farmakokinet. 1(1): 39-54 (1987) | |
Publication Date | 1987-07 | |
Full Text Language | English | |
Order – Buy | Ηλεκτρονική Μορφή: pdf (10 €) – Digital Type: pdf (10 €)pharmakonpress[at]pharmakonpress[.]gr | |
Keywords | Receptor, glucocorticoid, hormone, structure, function in vivo. | |
Other Terms | review article | |
Summary | Glucocorticoid hormone receptor (GR) is a regulatory factor of eukaryotic gene transcription acting by hormone receptor complex, binding to transcriptional enhancer (DNA) elements in vivo. The response is elicited by hormone-induced conformational ‘transformation’ and ‘translocation’ of the hormone-GR complex from the cytoplasm to the nucleus. The role of the receptor in eliciting the glucocorticoid response is investigated with Dexamethasone 21-mesylate (DM), which covalently links the synthetic glucocorticoid Dexamethasone (Dex) to the receptor. The purification of the non-transformed and the transformed form of the GR by affinity chromatography and ion-exchange chromatography respectively led to the production of specific antibodies in rabbits. The use of immunochemical methods and receptor labeling techniques for analysing the fine structure and subunit constitution of the receptor in the non-transformed and transformed conformation is described. Examination of GR fine structure revealed several proteolytic ‘hinge’ regions likely involved in receptor transformation and turnover in vivo. Differential sensitivity of some of the ‘hinges’ to the presence of calcium ions is established, suggesting a signaling mechanism sensitive to several other hormones and growth factors. Evidence is presented on a putative subunit constitution of the non-transformed form suggesting that it is a heteropolymer comprising at least one non-steroid binding subunit in addition to the GR. These data on the GR structure are discussed with respect to receptor cellular dynamics and function in vivo. | |
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