Inhibition of renal PGE2-9-ketoreductase by diuretics

Prostaglandins. 1976 Aug;12(2):197-207. doi: 10.1016/0090-6980(76)90115-5.

Abstract

The metabolism of PGE2 by extracts of renal cortex is species dependent. In the rat PGE2-15-hydroxydehydrogenase initiates metabolism whereas in the rabbit PGE2-9-ketoreductase predominates. In man both mechanisms may operate. Each of the metabolic enzymes, which limits the vasodilator-diuretic actions of PGE2, was inhibited by ethacrynic acid, furosemide and indomethacin. Some inhibition of PGE2-9-ketoreductase was also observed with chlorthalidone, hydralazine and phentolamine but the thiazide diuretics and a number of other cardiovascular-active agents were without significant effect. We conclude that the inhibition of PGE2-9-ketoreductase and PGE2-15-hydroxydehydrogeanse could contribute to the mechanism of action of the non-thiaxide diuretics in man.

MeSH terms

  • Alcohol Oxidoreductases / metabolism*
  • Animals
  • Chlorthalidone / pharmacology
  • Diuretics / pharmacology*
  • Ethacrynic Acid / pharmacology
  • Furosemide / pharmacology
  • Humans
  • Hydralazine / pharmacology
  • Hydroxyprostaglandin Dehydrogenases / metabolism*
  • Indomethacin / pharmacology
  • Kidney Cortex / enzymology*
  • Phentolamine / pharmacology
  • Prostaglandins E / metabolism*
  • Rabbits
  • Rats
  • Thiazines / pharmacology

Substances

  • Diuretics
  • Prostaglandins E
  • Thiazines
  • Hydralazine
  • Furosemide
  • Alcohol Oxidoreductases
  • Hydroxyprostaglandin Dehydrogenases
  • Ethacrynic Acid
  • Chlorthalidone
  • Indomethacin
  • Phentolamine