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Mineralocorticoid selectivity: molecular and cellular aspects.

N Farman1, B Bocchi

  • 1INSERM U478, Faculté de Médecine Xavier Bichat, Paris, France. farman@bichat.inserm.fr

Kidney International
|April 12, 2000
PubMed
Summary

Mineralocorticoid receptor (MR) selectivity is maintained by the enzyme 11beta hydroxysteroid dehydrogenase (HSD2), which inactivates glucocorticoids. This ensures aldosterone

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Multiple aspects of mineralocorticoid selectivity.

American journal of physiology. Renal physiology·2001

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Biology

Background:

  • Aldosterone binds to the mineralocorticoid receptor (MR) in sensitive cells.
  • MR has similar affinities for aldosterone and more abundant glucocorticoids.
  • Mechanisms are needed to prevent glucocorticoid over-occupation of MR.

Purpose of the Study:

  • To review the cell biology and regulation of 11beta hydroxysteroid dehydrogenase (HSD2).
  • To discuss the role of HSD2 in mineralocorticoid selectivity.
  • To explore the implications of HSD2 in human hypertension.

Main Methods:

  • Review of existing literature on HSD2.
  • Analysis of cellular mechanisms governing MR selectivity.
  • Discussion of dimerization of MR and glucocorticoid receptors.

Main Results:

  • 11beta hydroxysteroid dehydrogenase (HSD2) is the primary enzyme for mineralocorticoid selectivity.
  • HSD2 metabolizes glucocorticoids, reducing their affinity for MR.
  • MR dimerization and other cellular events contribute to fine-tuning gene regulation.

Conclusions:

  • HSD2 is crucial for maintaining aldosterone's specific action.
  • Dysregulation of HSD2 is implicated in human hypertension.
  • Multiple cellular factors contribute to dynamic regulation of MR activity.

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