Evidence for a Common Binding-Site for Omeprazole and N-Ethylmaleimide in Subunit A of Chromaffin Granule Vacuolar-Type H+-ATPase

Y. Moriyama, V. Patel, I. Ueda, M. Futai

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Vacuolar-type H+-ATPase from adrenal chromaffin granules wasfound to be sensitive to omeprazole, a known gastric H+/K+-ATPase inhibitor, the concentration required for 50 % inhibition being 80 μM freshly-prepared and 12 μM acid-treated reagent. ATP and ADP protected the enzyme from inhibition by omeprazole. The activity of the inhibited enzyme was restored by the addition of reduced glutathione. Omeprazole protected the enzyme from inhibition by N-ethylmaleimide and its binding to the subunit A. As subunit A has a nucleotide binding site(s) and as a cysteine residue is involved in the inhibition by N-ethylmaleimide, these results suggested that the two sulfhydryl reagents bind to the same cysteine residue near the nucleotide binding domain in the subunit A, resulting in inactivation of vacuolar-type H+-ATPase.

Original languageEnglish
Pages (from-to)699-706
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume196
Issue number2
DOIs
Publication statusPublished - Oct 29 1993
Externally publishedYes

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Chromaffin Granules
Vacuolar Proton-Translocating ATPases
Ethylmaleimide
Proton-Translocating ATPases
Omeprazole
Binding Sites
Cysteine
Enzymes
Nucleotides
H(+)-K(+)-Exchanging ATPase
Sulfhydryl Reagents
Adenosine Diphosphate
Glutathione
Adenosine Triphosphate
Acids

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Evidence for a Common Binding-Site for Omeprazole and N-Ethylmaleimide in Subunit A of Chromaffin Granule Vacuolar-Type H+-ATPase. / Moriyama, Y.; Patel, V.; Ueda, I.; Futai, M.

In: Biochemical and Biophysical Research Communications, Vol. 196, No. 2, 29.10.1993, p. 699-706.

Research output: Contribution to journalArticle

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