Novel Schering and ouabain-insensitive potassium-dependent proton secretion in the mouse cortical collecting duct

Am J Physiol Renal Physiol. 2002 Jan;282(1):F133-43. doi: 10.1152/ajprenal.0124.2001.

Abstract

The intercalated (IC) cells of the cortical collecting duct (CCD) are important to acid-base homeostasis by secreting acid and reabsorbing bicarbonate. Acid secretion is mediated predominantly by apical membrane Schering (SCH-28080)-sensitive H(+)-K(+)- ATPase (HKA) and bafilomycin-sensitive H(+)-ATPase. The SCH-28080-sensitive HKA is believed to be the gastric HKA (HKAg). Here we examined apical membrane potassium-dependent proton secretion in IC cells of wild-type HKAg (+/+) and HKAg knockout (-/-) mice to determine relative contribution of HKAg to luminal proton secretion. The results demonstrated that HKAg (-/-) and wild-type mice had comparable rates of potassium-dependent proton secretion, with HKAg (-/-) mice having 100% of K(+)-dependent H(+) secretion vs. wild-type mice. Potassium-dependent proton secretion was resistant to ouabain and SCH-28080 in HKAg knockout mice but was sensitive to SCH-28080 in wild-type animals. Northern hybridizations did not demonstrate any upregulation of colonic HKA in HKAg knockout mice. These data indicate the presence of a previously unrecognized K(+)-dependent SCH-28080 and ouabain-insensitive proton secretory mechanism in the cortical collecting tubule that may play an important role in acid-base homeostasis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acid-Base Equilibrium / drug effects
  • Acid-Base Equilibrium / physiology*
  • Animals
  • Blotting, Northern
  • Carrier Proteins / metabolism
  • Enzyme Inhibitors / pharmacology*
  • H(+)-K(+)-Exchanging ATPase / genetics*
  • H(+)-K(+)-Exchanging ATPase / metabolism
  • Hydrogen-Ion Concentration
  • Imidazoles / pharmacology*
  • Kidney Cortex / metabolism
  • Kidney Tubules, Collecting / metabolism*
  • Mice
  • Mice, Knockout
  • Ouabain / pharmacology*
  • Potassium / metabolism
  • Protons
  • RNA, Messenger / analysis
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Carrier Proteins
  • Enzyme Inhibitors
  • Imidazoles
  • Protons
  • RNA, Messenger
  • Sch 28080
  • Ouabain
  • H(+)-K(+)-Exchanging ATPase
  • Potassium