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J. Biol. Chem., Vol. 260, Issue 27, 14484-14490, Nov, 1985
PL Chong, PA Fortes and DM Jameson
To investigate the mechanisms by which hydrostatic pressure inhibits
(Na,K)-ATPase, we measured enzyme activity, as a function of pressure and
temperature, of purified (Na,K)-ATPase from dog kidney and eel electroplax,
and we monitored protein conformation, possible subunit interactions, and
the fluidity of the membrane with fluorescent probes. The (Na,K)-ATPase and
p-nitrophenylphosphatase activities were inhibited reversibly by pressures
below 1.5 kilobars (eel enzyme) and 2.5 kilobars (dog kidney enzyme). Above
these pressures, the enzymes were inactivated irreversibly. The plots of
1n(activity) versus pressure were curvilinear; this indicates that the
reversible inhibition by pressure involves two or more rate-limiting steps.
The calculated activation volumes varied with temperature and pressure and
were larger for the (Na,K)-ATPase activity compared to the p-
nitrophenylphosphatase activity. The fluorescence polarization of three
hydrophobic probes decreased with increasing temperature (10-36 degrees C)
and increased with increasing pressure (10(-3)-1.5 kilobars), reversibly,
without any evidence of a lipid phase transition. Plots of enzyme activity
versus fluorescence polarization of the lipid probes showed an inverse
relationship; this indicates that enzyme activity was directly related to
the fluidity of the membrane as measured by the lipid probes. Pressure had
no effect on the fluorescence polarization of two cardiac glycoside probes
nor on the efficiency of resonance energy transfer between either donor and
acceptor cardiac glycosides specifically bound to the ouabain sites of
different alpha-subunits, or tryptophan and the bound cardiac glycoside
probe. These results suggest that dissociation of dimeric alpha-subunits is
not related to the inhibition by pressure, and that the cardiac
glycoside-complexed enzyme conformation is stabilized by pressure. It is
concluded that increased pressure decreases the membrane fluidity which
hinders conformational transitions associated with rate-limiting steps of
the (Na,K)-ATPase reaction. It is proposed that ion-bound or -occluded
forms of (Na,K)- ATPase are stabilized by pressure because they occupy a
smaller volume.
Mechanisms of inhibition of (Na,K)-ATPase by hydrostatic pressure studied with fluorescent probes
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