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The Gastric H/K ATPase β Subunit Gene and Transcriptional Pathways in Acid-Secreting Epithelia of the Stomach and Kidney

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Molecular and Cellular Mechanisms of H+ Transport

Part of the book series: NATO ASI Series ((volume 89))

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Abstract

Stomach acid is produced by parietal cells and secreted into the gastric lumen for digestive and protective purposes. The gastric parietal cell has a highly developed acid secretory machinery that can maintain the pH of the gastric lumen at around pH 1 (Forte and Soil, 1993; Sachs et al., 1992; Faller et al., 1993; Rabon and Reuben, 1990). The central role of the gastric H/K ATPase in the secretion of gastric HC1 is undisputed. The protein is located in the membranes of the parietal cell tubulovesicles and secretory canaliculi. The mechanism of action and structure of the gastric H/K ATPase have been extensively reviewed in this volume and elsewhere. The protein is composed of two subunits, a catalytic α and a β subunit. The existence of the a subunit has been known for some time. The protein is 95 kDa and has a large number of membrane spanning domains (probably 8) (Sachs et al., 1992; Green and Stokes, 1992). The pß subunit was only recently discovered in a number of laboratories (Okamoto et al., 1990, Reuben et al. 1990, Shull, 1992, Toh et al, 1990). The 35 kDa protein core is highly glycosylated with N-linked glycans which may terminate in poly-N-acetyllactosamine structures (Callghan et al. 1990, 1992). The β subunit appears to be essential for membrane insertion, may contain intracellular trafficking signals and is required for functional activity (Horisberg et al., 1991; Gottardi and Caplan, 1993; Sachs et al., 1992)

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© 1994 Springer-Verlag Berlin Heidelberg

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van Driel, I.R., Gleeson, P.A., Tan, SS., Toh, BH. (1994). The Gastric H/K ATPase β Subunit Gene and Transcriptional Pathways in Acid-Secreting Epithelia of the Stomach and Kidney. In: Hirst, B.H. (eds) Molecular and Cellular Mechanisms of H+ Transport. NATO ASI Series, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79301-1_2

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  • DOI: https://doi.org/10.1007/978-3-642-79301-1_2

  • Publisher Name: Springer, Berlin, Heidelberg

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