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J Biol Chem, Vol. 275, Issue 17, 13035-13040, April 28, 2000
From the Departments of Na,K-ATPase activity has been identified in the
apical membrane of rat distal colon, whereas ouabain-sensitive and
ouabain-insensitive H,K-ATPase activities are localized solely to
apical membranes. This study was designed to determine whether apical
membrane Na,K-ATPase represented contamination of basolateral membranes
or an alternate mode of H,K-ATPase expression. An antibody directed
against the H,K-ATPase
Ouabain-sensitive H,K-ATPase Functions as Na,K-ATPase in Apical
Membranes of Rat Distal Colon*
,,¶
Internal Medicine and
§ Surgery, Yale University, New Haven, Connecticut 06520
subunit (HKc) inhibited apical
Na,K-ATPase activity by 92% but did not alter basolateral membrane
Na,K-ATPase activity. Two distinct H,K-ATPase isoforms exist; one of
which, the ouabain-insensitive HKc, has been cloned. Because dietary
sodium depletion markedly increases ouabain-insensitive active
potassium absorption and HKc mRNA and protein expression,
Na,K-ATPase and H,K-ATPase activities and protein expression were
determined in apical membranes from control and sodium-depleted rats.
Sodium depletion substantially increased ouabain-insensitive H,K-ATPase
activity and HKc protein expression by 109-250% but increased
ouabain-sensitive Na,K-ATPase and H,K-ATPase activities by only 30%
and 42%, respectively. These studies suggest that apical membrane
Na,K-ATPase activity is an alternate mode of ouabain-sensitive
H,K-ATPase and does not solely represent basolateral membrane contamination.
*
This study was supported in part by a research grant (DK
18777-19) from the NIDDK, National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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