Evidence map›Paper›PMID 18536934›Full record

ReviewPflugers Archiv : European journal of physiology2009

The gastric HK-ATPase: structure, function, and inhibition.

Jai Moo Shin, Keith Munson, Olga Vagin, George Sachs

Erratum issuedAbstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 258 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Review
  6. Proton pump inhibitor exposure modulates functional and transcriptional responses inFrontiers in cellular and infection microbiology · 2026
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Can Pantoprazole be Used for Premedication in Meckel Scintigraphy?Molecular imaging and radionuclide therapy · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. [History and Pharmacological Mechanism of Gastric Acid-suppressive Drugs].The Korean journal of helicobacter and upper gastrointestinal research · 2023
    Review
  20. Article

37 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Jai Moo ShinDepartment of Physiology, David Geffen School of Medicine, University of California at Los Angeles and VA Greater Los Angeles Healthcare System, Los Angeles, CA 90073, USA.
Keith Munson
Olga Vagin
George Sachs
VA Greater Los Angeles Healthcare System · USMembrane Technology & Research (United States) · USUniversity of California, Los Angeles · US

Funding

The Gastric Biology of Helicobacter PyloriR01DK053642 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SACHS, GEORGE · 1997 to 2012
$3.2M
THE GASTRIC ACID PUMP AS A TARGET FOR ULCER TREATMENTR01DK058333 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SACHS, GEORGE · 2000 to 2009
$2.6M
Role of Na, K-ATPase beta isoforms in pump sorting and epithelial integrityR01DK077149 · NIDDK · BRENTWOOD BIOMEDICAL RESEARCH INSTITUTE · PI VAGIN, OLGA · 2007 to 2010
$811k
The Gastric Acid Pump as a Target for Ulcer TreatmentR56DK058333 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SACHS, GEORGE · 2010 to 2010
$229k
NIDDK NIH HHS DK053642NIDDK NIH HHS DK58333NIDDK NIH HHS R01 DK053642NIDDK NIH HHS R01 DK058333NIDDK NIH HHS R01 DK077149NIDDK NIH HHS R56 DK058333
6 · The paper itself

Abstract

The gastric H,K-ATPase, a member of the P(2)-type ATPase family, is the integral membrane protein responsible for gastric acid secretion. It is an alpha,beta-heterodimeric enzyme that exchanges cytoplasmic hydronium with extracellular potassium. The catalytic alpha subunit has ten transmembrane segments with a cluster of intramembranal carboxylic amino acids located in the middle of the transmembrane segments TM4, TM5,TM6, and TM8. Comparison to the known structure of the SERCA pump, mutagenesis, and molecular modeling has identified these as constituents of the ion binding domain. The beta subunit has one transmembrane segment with N terminus in cytoplasmic region. The extracellular domain of the beta subunit contains six or seven N-linked glycosylation sites. N-glycosylation is important for the enzyme assembly, maturation, and sorting. The enzyme pumps acid by a series of conformational changes from an E(1) (ion site in) to an E(2) (ion site out) configuration following binding of MgATP and phosphorylation. Several experimental observations support the hypothesis that expulsion of the proton at 160 mM (pH 0.8) results from movement of lysine 791 into the ion binding site in the E(2)P configuration. Potassium access from the lumen depends on activation of a K and Cl conductance via a KCNQ1/KCNE2 complex and Clic6. K movement through the luminal channel in E(2)P is proposed to displace the lysine along with dephosphorylation to return the enzyme to the E(1) configuration. This enzyme is inhibited by the unique proton pump inhibitor class of drug, allowing therapy of acid-related diseases.

Indexed as

Gastrointestinal HormonesBinding SitesEnzyme InhibitorsHumansModels, MolecularMolecular StructurePotassiumProtein ConformationStomachEnzyme InhibitorsGastrointestinal Hormoneshydrogen potassium ATPase, gastric endogenous activator protein, mammalPotassium

Identifiers

PMID18536934
PMCPMC3079481
OpenAlexW2062078340

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.