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Departments of 1 Internal Medicine, 3 Surgery, and 2 Cellular and Molecular Physiology, Yale University, New Haven, Connecticut 06520
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
-subunit (HKc) 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
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.
K+-dependent intracellular pH regulation; rat colon; H+-K+-adenosinetriphosphatase
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