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[H+, K+ -ATPase, H+ -ATPase]

N Takeguchi1, S Asano, M Morii

  • 1Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan.

Nihon Rinsho. Japanese Journal of Clinical Medicine
|March 1, 1996
PubMed
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This study reveals a key residue in the gastric H+, K+-ATPase alpha-subunit crucial for potassium ion (K+) affinity. It also clarifies the binding site number for proton pump inhibitors like omeprazole.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzyme Kinetics

Context:

  • The gastric H+, K+-ATPase (proton pump) is essential for acid secretion.
  • Understanding its structure-function relationship is vital for developing effective treatments for acid-related disorders.

Purpose:

  • To elucidate the role of specific residues in the alpha-subunit of gastric H+, K+-ATPase in determining potassium ion (K+) affinity.
  • To clarify the number of binding sites for proton pump inhibitors (PPIs) like omeprazole and rabeprazole.
  • To investigate the oligomeric state required for enzyme function.

Summary:

  • Functional expression of gastric H+, K+-ATPase in an animal cell line.
  • Mutation of glutamic acid (345) in the alpha-subunit's 4th transmembrane domain significantly reduced K+ affinity, identifying it as critical for K+ binding.

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  • The study identified a single binding site for PPIs, contradicting previous proposals of multiple sites, and demonstrated that interaction between 2 or 4 alpha-subunits is necessary for pump function.

    • Impact:

    • Provides critical insights into the molecular mechanisms of gastric acid secretion.
    • Offers a refined understanding of proton pump inhibitor binding, potentially guiding the development of new therapeutic agents.
    • Contributes to the fundamental knowledge of ion pump structure and function.