Abstract

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.

Keywords

Glucocorticoid receptorMineralocorticoid receptorMineralocorticoidBiologyReceptorGlucocorticoidGeneTranscription factorHormone response elementDNACell biologyMolecular biologyGeneticsEndocrinologyEstrogen receptor

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Publication Info

Year
1987
Type
article
Volume
237
Issue
4812
Pages
268-275
Citations
1935
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Jeffrey L. Arriza, Cary Weinberger, Gail Cerelli et al. (1987). Cloning of Human Mineralocorticoid Receptor Complementary DNA: Structural and Functional Kinship with the Glucocorticoid Receptor. Science , 237 (4812) , 268-275. https://doi.org/10.1126/science.3037703

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DOI
10.1126/science.3037703