Pharmacological and genetic evidence that cathepsin B is not the physiological activator of rodent prorenin

Biol Chem. 2010 Dec;391(12):1469-73. doi: 10.1515/BC.2010.140.

Abstract

Renin is the first enzyme in the renin-angiotensin-aldosterone system which is the principal regulator of blood pressure and hydroelectrolyte balance. Previous studies suggest that cathepsin B is the activator of the prorenin zymogen. Here, we show no difference in plasma renin activity, or mean arterial blood pressure between wild-type and cathepsin B knockout mice. To account for potential gene compensation, a potent, selective, reversible cathepsin B inhibitor was developed to determine the role of cathepsin B on prorenin processing in rats. Pharmacological inhibition of cathepsin B in spontaneously hypertensive and double transgenic rats did not result in a reduction in renal mature renin protein levels or plasma renin activity. We conclude that cathepsin B does not play a significant role in this process in rodents.

MeSH terms

  • Animals
  • Cathepsin B / antagonists & inhibitors
  • Cathepsin B / genetics
  • Cathepsin B / physiology*
  • Enzyme Inhibitors / pharmacology
  • Hypertension / genetics
  • Hypertension / metabolism
  • Mice
  • Mice, Knockout
  • Rats
  • Rats, Transgenic
  • Renin / metabolism*

Substances

  • Enzyme Inhibitors
  • Cathepsin B
  • Renin