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Effect of angiotensin II on rat renal cortical 11β-hydroxysteroid dehydrogenase

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Abstract

Renal 11β-hydroxysteroid dehydrogenases (11β-HSDs) are subject to modulation by various endogenous factors. 11β-HSDs convert glucocorticoids into inactive 11-ketones and thereby determine tissue levels of active glucocorticoids and thus the extent of glucocorticoid receptor (GR) and mineralocorticoid receptor (MR) activation. As such, modulation of the activity of renal 11β-HSDs may contribute to the cascade of regulatory events involved in renal electrolyte water handling. We investigated whether renal 11β-HSDs are modulated by elevated circulating angiotensin II. In rats infused for 2 wk with angiotensin II (250 ng/[kg.min] subcutaneously), plasma angiotensin II, aldosterone, and corticosterone were raised 5.1-, 10.7-, and 2.3-fold, respectively, compared with control rats. Angiotensin II infusion raised corticosterone 11β-oxidation 1.46- and 1.35-fold in renal cortical proximal and distal tubules (enriched by Percoll centrifugation), respectively, but had no effect on 11β-HSD1 and 11β-HSD2 mRNA levels (semiquantitative reverse transcriptase solymerase chain reaction), except for distal tubular 11β-HSD1 mRNA, which was decreased to 50%. In vitro treatment of freshly isolated tubules with angiotensin II for 45 min prior to assessment of 11β-HSD activity showed no direct acute effects of angiotensin II on tubular corticosterone 11β-oxidation. The enhanced renal tubular corticosterone 11β-oxidation in vivo may partly protect renal GR and MR from elevated plasma corticosterone on angiotensin II infusion.

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Authors and Affiliations

  1. Department of Pharmacology and Toxicology, Cardiovascular Research Institute Maastricht, Universiteit Maastricht, PO Box 616, 6200 MD, Maastricht, Netherlands

    J. J. Rob Hermans, Marc A. J. Fischer, Paul M. Schiffers & Harry A. J. Struijker-Boudier

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  1. J. J. Rob Hermans
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Hermans, J.J.R., Fischer, M.A.J., Schiffers, P.M. et al. Effect of angiotensin II on rat renal cortical 11β-hydroxysteroid dehydrogenase. Endocr 13, 393–399 (2000). https://doi.org/10.1385/ENDO:13:3:393

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