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Science 17 July 1987:
Vol. 237. no. 4812, pp. 268 - 275
DOI: 10.1126/science.3037703

Articles

Science, Vol 237, Issue 4812, 268-275
Copyright © 1987 by American Association for the Advancement of Science


articles

Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor

JL Arriza, C Weinberger, G Cerelli, TM Glaser, BL Handelin, DE Housman, and RM Evans

Low-stringency hybridization with human glucocorticoid receptor (hGR) complementary DNA was used to isolate a new gene encoding a predicted 107-kilodalton polypeptide. Expression studies demonstrate its ability to bind aldosterone with high affinity and to activate gene transcription in response to aldosterone, thus establishing its identity as the human mineralocorticoid receptor (hMR). This molecule also shows high affinity for glucocorticoids and stimulates a glucocorticoid-responsive promoter. Together the hMR and hGR provide unexpected functional diversity in which hormone-binding properties, target gene interactions, and patterns of tissue-specific expression may be used in a combinatorial fashion to achieve complex physiologic control.





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Science. ISSN 0036-8075 (print), 1095-9203 (online)