Apical membrane localization of ouabain-sensitive K(+)-activated ATPase activities in rat distal colon

Am J Physiol. 1991 Dec;261(6 Pt 1):G1005-11. doi: 10.1152/ajpgi.1991.261.6.G1005.

Abstract

This study sought to establish the presence of K(+)-activated adenosinetriphosphatase (ATPase) activity in the colonic mucosa of the rat distal colon. K(+)-activated ATPase activity was present in apical membranes but not in basolateral membranes. K(+)-activated ATPase activity in apical membranes represented an approximate 10-fold enrichment compared with that in the homogenate. Na(+)-K(+)-activated ATPase activity was also present in homogenate but was enriched less than fourfold in apical membranes. K(+)-activated ATPase activity in apical membranes had both ouabain-sensitive and ouabain-insensitive components. In contrast, Na(+)-K(+)-activated ATPase activity was completely inhibited by ouabain. Similar half-maximal concentrations for K+ and pH activation curves were found for both ouabain-sensitive and ouabain-insensitive fractions. In addition to K+, the ouabain-sensitive fraction of K(+)-activated ATPase activity was stimulated by Rb+, NH+4, and Cs+, whereas the ouabain-insensitive fraction was activated only by Rb+. K(+)-activated ATPase activity was significantly inhibited by vanadate but not by N-ethylmaleimide or omeprazole. In the proximal colon, in contrast to the distal colon, active K+ absorption is not present, and K(+)-activated ATPase is approximately 20% of that in the distal colon. These studies demonstrate that K(+)-activated ATPase is present in apical membranes of rat distal colon and permit the speculation that this enzyme represents a unique and distinct ATPase (compared with either Na(+)-K(+)-ATPase or gastric parietal cell K(+)-ATPase) and is likely linked closely to the active K+ absorptive process present in this epithelium.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / drug effects
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Ca(2+) Mg(2+)-ATPase / metabolism
  • Cation Transport Proteins
  • Cations / metabolism
  • Cell Membrane / enzymology
  • Colon / enzymology*
  • Colon / ultrastructure
  • Hydrogen-Ion Concentration
  • Intestinal Mucosa / enzymology*
  • Intestinal Mucosa / ultrastructure
  • Magnesium / metabolism
  • Ouabain / pharmacology
  • Potassium / metabolism
  • Rats
  • Rats, Inbred Strains
  • Sodium / metabolism
  • Sodium-Potassium-Exchanging ATPase

Substances

  • Cation Transport Proteins
  • Cations
  • Ouabain
  • Sodium
  • Adenosine Triphosphatases
  • Ca(2+) Mg(2+)-ATPase
  • potassium transporting ATPase
  • Sodium-Potassium-Exchanging ATPase
  • Magnesium
  • Potassium