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

Jeffrey L. Arriza, Cary Weinberger, Gail Cerelli, Thomas M Glaser, Barbara L. Handelin, David E. Housman, Ronald M. Evans

Research output: Contribution to journalArticle

1525 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)268-275
Number of pages8
JournalScience
Volume237
Issue number4812
StatePublished - 1987
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)
  • General

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    Arriza, J. L., Weinberger, C., Cerelli, G., Glaser, T. M., Handelin, B. L., Housman, D. E., & Evans, R. M. (1987). Cloning of human mineralocorticoid receptor complementary DNA: Structural and functional kinship with the glucocorticoid receptor. Science, 237(4812), 268-275.