Inhibition of renin secretion from rat renal cortical slices by (R)-12-HETE

William L Henrich, J. R. Falck, William B. Campbell

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The arachidonic acid metabolite 12-hydroxyeicosatetraenoic acid (12-HETE) inhibits renin secretion both in vivo and in vitro, but the enzymatic origin of the 12-HETE responsible for renin inhibition is unknown. These studies examined the effect of the 12-HETE stereoisomers (R)-12-HETE (a product of the cytochrome P-450 monooxygenase enzyme system) and (S)-12-HETE (a product of the lipoxygenase enzyme system) on basal and stimulated renin secretion from superficial cortical slices in the rat. First, rat cortex was shown to produce 12-HETE; chiral-phase high-performance liquid chromatography revealed that cortex produced 81% (S)-12-HETE and 19% (R)-12-HETE. (R)-12-HETE reduced basal renin release by 28 ± 4% to 49 ± 5% at concentrations of 10-9 to 10-7 M (P < 0.05 to 0.01). (S)-12-HETE did not significantly affect renin release. (R)-12-HETE also blunted isoproterenol-stimulated renin secretion (P < 0.05) at a concentration of 10-6 M. 20-HETE, another cytochrome P-450 product, did not exert a significant effect on renin release. In summary, both (R)-12-HETE and (S)-12-HETE are synthesized by renal cortical tissue. Only (R)-12-HETE directly inhibits in vitro renin release. These findings suggest that the renal cytochrome P-450 enzyme system is capable of directly influencing local renin secretion.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Renal Fluid and Electrolyte Physiology
Volume263
Issue number4 32-4
StatePublished - Oct 1992
Externally publishedYes

Fingerprint

Hydroxyeicosatetraenoic Acids
Renin
Kidney
12-Hydroxy-5,8,10,14-eicosatetraenoic Acid
Cytochrome P-450 Enzyme System
Stereoisomerism
Lipoxygenase
Isoproterenol
Arachidonic Acid
High Pressure Liquid Chromatography

Keywords

  • Cytochrome P-450 system
  • Hydroxyeicosatetraenoic acid
  • Renal cortex

ASJC Scopus subject areas

  • Physiology

Cite this

Inhibition of renin secretion from rat renal cortical slices by (R)-12-HETE. / Henrich, William L; Falck, J. R.; Campbell, William B.

In: American Journal of Physiology - Renal Fluid and Electrolyte Physiology, Vol. 263, No. 4 32-4, 10.1992.

Research output: Contribution to journalArticle

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abstract = "The arachidonic acid metabolite 12-hydroxyeicosatetraenoic acid (12-HETE) inhibits renin secretion both in vivo and in vitro, but the enzymatic origin of the 12-HETE responsible for renin inhibition is unknown. These studies examined the effect of the 12-HETE stereoisomers (R)-12-HETE (a product of the cytochrome P-450 monooxygenase enzyme system) and (S)-12-HETE (a product of the lipoxygenase enzyme system) on basal and stimulated renin secretion from superficial cortical slices in the rat. First, rat cortex was shown to produce 12-HETE; chiral-phase high-performance liquid chromatography revealed that cortex produced 81{\%} (S)-12-HETE and 19{\%} (R)-12-HETE. (R)-12-HETE reduced basal renin release by 28 ± 4{\%} to 49 ± 5{\%} at concentrations of 10-9 to 10-7 M (P < 0.05 to 0.01). (S)-12-HETE did not significantly affect renin release. (R)-12-HETE also blunted isoproterenol-stimulated renin secretion (P < 0.05) at a concentration of 10-6 M. 20-HETE, another cytochrome P-450 product, did not exert a significant effect on renin release. In summary, both (R)-12-HETE and (S)-12-HETE are synthesized by renal cortical tissue. Only (R)-12-HETE directly inhibits in vitro renin release. These findings suggest that the renal cytochrome P-450 enzyme system is capable of directly influencing local renin secretion.",
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