Modulation of H+,K+‐ATPase activity by the molecular chaperone ERp57 highly expressed in gastric parietal cells

ERp57 is a ubiquitous ER chaperone that has disulfide isomerase activity. Here, we found that both ERp57 and gastric H+,K+‐ATPase are expressed in a sample derived from the apical canalicular membranes of parietal cells. Overexpression of ERp57 in HEK293 cells stably expressing H+,K+‐ATPase significantly increased the ATPase activity without changing the expression level of H+,K+‐ATPase. Interestingly, overexpression of a catalytically inactive mutant of ERp57 (C57S/C60S/C406S/C409S) in the cells also increased H+,K+‐ATPase activity. In contrast, knockdown of endogenous ERp57 in H+,K+‐ATPase‐expressing cells significantly decreased ATPase activity without changing the expression level of H+,K+‐ATPase. Overexpression and knockdown of ERp57 had no significant effect on the expression and function of Na+,K+‐ATPase. These results suggest that ERp57 positively regulates H+,K+‐ATPase activity apart from its chaperoning function.

• Publication year

  2013

• Venue

  FEBS Letters

• Publication date

  2013-12-11

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.febslet.2013.10.030PMID 24188822
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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