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

Mol Endocrinol. 1993 Apr;7(4):597-603. doi: 10.1210/mend.7.4.8388999.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

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


  • Glucocorticoids
  • Receptors, Glucocorticoid
  • Receptors, Mineralocorticoid
  • Receptors, Steroid
  • DNA