Stable Expression of Gastric Proton Pump Activity at the Cell Surface.

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Stable cell lines expressing the gastric proton pump α- and/or β-subunits were constructed. The cell line co-expressing the α-and β-subunits showed inward Rb+ transport, which was activated by Rb+ in a concentration-dependent manner. In the α+β-expressing cell line, rapid recovery of intracellular pH was also observed after acid load, indicating that this cell line transported protons outward. These ion transport activities were inhibited by a proton pump inhibitor, 2-methyl-8-(phenylmethoxy)imidazo[1, 2-a]pyridine-3-acetonitrile (SCH 28080). In a membrane fraction of the α+β-expressing cell line, K+-stimulated ATPase (K+-ATPase) activity and the acylphosphorylation of the α-subunit were observed, both of which were also inhibited by SCH 28080. The specific activity and properties of the K+-ATPase were comparable to those found in the native gastric proton pump. In the stable cell lines, the α-subunit was retained in the intracellular compartment and was unstable in the absence of the β-subunit, but it was stabilized and reached the cell surface in the presence of the β-subunit. On the other hand, the β-subunit was stable and able to travel to the cell surface in the absence of the α-subunit. These cell lines are ideal for the structure-function study of ion transport by the gastric proton pump as well as for characterization of the cellular regulation of surface expression of the functional proton pump.
社団法人日本生化学会の論文

Stable Expression of Gastric Proton Pump Activity at the Cell Surface.

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