Differential localization of colonic H(+)-K(+)-ATPase isoforms in surface and crypt cells

Am J Physiol. 1998 Feb;274(2):G424-9. doi: 10.1152/ajpgi.1998.274.2.G424.

Abstract

Two distinct colonic H(+)-K(+)-adenosinetriphosphatase (H(+)-K(+)-ATPase) isoforms can be identified in part on the basis of their sensitivity to ouabain. The colonic H(+)-K(+)-ATPase alpha-subunit (HKc alpha) was recently cloned, and its message and protein are present in surface (and the upper 20% of crypt) cells in the rat distal colon. These studies were performed to establish the spatial distribution of the ouabain-sensitive and ouabain-insensitive components of both H(+)-K(+)-ATPase activity in apical membranes prepared from surface and crypt cells and K(+)-dependent intracellular pH (pHi) recovery from an acid load both in isolated perfused colonic crypts and in surface epithelial cells. Whereas H(+)-K(+)-ATPase activity in apical membranes from surface cells was 46% ouabain sensitive, its activity in crypt apical membranes was 96% ouabain sensitive. Similarly, K(+)-dependent pHi recovery in isolated crypts was completely ouabain sensitive, whereas in surface cells K(+)-dependent pHi recovery was insensitive to ouabain. These studies provide compelling evidence that HKc alpha encodes the colonic ouabain-insensitive H(+)-K(+)-ATPase and that a colonic ouabain-sensitive H(+)-K(+)-ATPase isoform is present in colonic crypts and remains to be cloned and identified.

Publication types

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

MeSH terms

  • Animals
  • Barium / pharmacology
  • Colon / cytology
  • Colon / enzymology*
  • H(+)-K(+)-Exchanging ATPase / metabolism*
  • Hydrogen-Ion Concentration
  • Isoenzymes / metabolism*
  • Male
  • Ouabain / pharmacology
  • Potassium / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Surface Properties

Substances

  • Isoenzymes
  • Barium
  • Ouabain
  • H(+)-K(+)-Exchanging ATPase
  • Potassium