The parietal cell gastric H, K-ATPase also functions as the Na, K-ATPase and Ca-ATPase in altered states

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The parietal cell gastric H, K-ATPase also functions as the Na, K-ATPase and Ca-ATPase in altered states

This article offers an explanation for the apparent lack of Na, K-ATPase activity in parietal cells although ouabain has been known to inhibit gastric acid secretion since 1962. The gastric H, K-ATPase (proton-pump) seems to be acting in altered states, thus behaving like a Na, K-ATPase (Na-pump) and/or Ca-ATPase (Ca-pump) depending on cellular needs.  This conclusion is based on the following ...

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Does the colonic H,K-ATPase also act as an Na,K-ATPase?

We previously have demonstrated that the colonic P-ATPase alpha subunit cDNA encodes an H,K-ATPase when expressed in Xenopus laevis oocytes. Besides its high level of amino acid homology (75%) with the Na,K-ATPase, the colonic H,K-ATPase also shares a common pharmacological profile with Na,K-ATPase, because both are ouabain-sensitive and Sch 28080-insensitive. These features raise the possibili...

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Cation selectivity of gastric H,K-ATPase and Na,K-ATPase chimeras.

Chimeras of the catalytic subunits of the gastric H,K-ATPase and Na, K-ATPase were constructed and expressed in LLC-PK1 cells. The chimeras included the following: (i) a control, H85N (the first 85 residues comprising the cytoplasmic N terminus of Na,K-ATPase replaced by the analogous region of H,K-ATPase); (ii) H85N/H356-519N (the N-terminal half of the cytoplasmic M4-M5 loop also replaced); a...

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Regulation of CA II and H+,K(+)-ATPase gene expression in canine gastric parietal cells.

Acid secretagogue-specific receptor activation in parietal cells triggers rapid and coordinate gene expression of gastric H+,K(+)-ATPase and of CA II. The rapid rise in steady-state levels of CA II mRNA is due to new transcription of the CA II gene in stimulated cells. Although the presumed function of CA II in activated parietal cells is to catalyze the generation of HCO3- from OH-, regulation...

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Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.

The crystal structure of SERCA1a (skeletal-muscle sarcoplasmic-reticulum/endoplasmic-reticulum Ca(2+)-ATPase) has recently been determined at 2.6 A (note 1 A = 0.1 nm) resolution [Toyoshima, Nakasako, Nomura and Ogawa (2000) Nature (London) 405, 647-655]. Other P-type ATPases are thought to share key features of the ATP hydrolysis site and a central core of transmembrane helices. Outside of the...

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ژورنال

عنوان ژورنال: F1000Research

سال: 2013

ISSN: 2046-1402

DOI: 10.12688/f1000research.2-165.v2