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1 University of Minnesota Medical School, Minneapolis, Minnesota 55455; 3 State University of New York, Brooklyn, New York 11203-2012; and 2 Jichi Medical School, Minamikawachi 329-0498, Japan
Na-K-ATPase plays a central role in a variety of physiological
processes, including ion transport and regulation of cell volume. Our
previous data showed that hyperoxia increased the expression of
Na-K-ATPase 
1 and
1 mRNA in lung type II cells.
We similarly show that hyperoxia (
95%
O2 for 24-48 h) increased
steady-state mRNA levels in both Na-K-ATPase subunits in Madin-Darby
canine kidney (MDCK) cells. The mechanism of gene regulation by
hyperoxia was assessed. Stability of the Na-K-ATPase mRNA levels of
both subunits was unchanged in hyperoxia-exposed MDCK cells. To
determine whether gene transcription was augmented by hyperoxia, MDCK
cells were transfected with a
1-subunit promoter-reporter
construct. Transfection with the wild-type promoter
(1-817) revealed a
1.9 ± 0.2-fold increase in promoter activity. Transfection with
5' deletion constructs identified a 61-base pair (bp) region
between 
102 and 41 that was necessary for this increase
in promoter activity by hyperoxia. Incorporation of this 61-bp region
into a minimal promoter (mouse mammary tumor virus) similarly increased promoter activity 2.3-fold in the presence of hyperoxia. This increase
in promoter activity was not seen when MDCK cells were incubated with
various concentrations of hydrogen peroxide. In summary, hyperoxia
increased Na-K-ATPase 1-subunit
mRNA steady-state level due to increased transcription in MDCK cells. A
region necessary for this hyperoxic effect on
1 transcription is located
between base pairs 102 and 41 on the promoter.
ribonucleic acid stability; transcription; transfection; sodium pump; oxidants; Madin-Darby canine kidney cells
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