Transactivation and synergistic properties of the mineralocorticoid receptor: relationship to the glucocorticoid receptor

R Rupprecht, J L Arriza, D Spengler, J M Reul, R M Evans, F Holsboer, K Damm

Research output: Contribution to journalArticle (Academic Journal)peer-review

176 Citations (Scopus)

Abstract

The human mineralocorticoid (hMR) and glucocorticoid (hGR) receptors mediate biological responses to adrenal corticosteroids and synthetic ligands. In transient transfection studies, corticosteroid-responsive promoters were used to monitor the hormone-dependent transcriptional regulatory properties of both receptors. The hMR mediates a lower stimulation of the transcription rate than the hGR and does not show cooperative activity on promoters containing multiple palindromic glucocorticoid-responsive elements. The functional importance of the amino-terminus in this differential response was demonstrated by hMR/hGR hybrid receptors in which this region was exchanged or deleted. These experiments revealed that the hMR amino-terminus does not provide the strong transactivation function present in the equivalent hGR domain and, in contrast to the hGR amino-terminus, interferes with the synergistic activity mediated by the DNA- and ligand-binding domains of both receptors.

Original languageEnglish
Pages (from-to)597-603
Number of pages7
JournalMolecular Endocrinology
Volume7
Issue number4
DOIs
Publication statusPublished - Apr 1993

Keywords

  • Base Sequence
  • Binding Sites
  • DNA
  • Gene Expression Regulation
  • Glucocorticoids
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Neuroblastoma
  • Promoter Regions, Genetic
  • Receptors, Glucocorticoid
  • Receptors, Mineralocorticoid
  • Receptors, Steroid
  • Transcription, Genetic
  • Transcriptional Activation
  • Transfection
  • Tumor Cells, Cultured

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