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 language | English |
|---|---|
| Pages (from-to) | 699-706 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 196 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Oct 29 1993 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Evidence for a Common Binding-Site for Omeprazole and N-Ethylmaleimide in Subunit A of Chromaffin Granule Vacuolar-Type H+-ATPase
AU - Moriyama, Y.
AU - Patel, V.
AU - Ueda, I.
AU - Futai, M.
PY - 1993/10/29
Y1 - 1993/10/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0027430285&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027430285&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1993.2306
DO - 10.1006/bbrc.1993.2306
M3 - Article
C2 - 8240346
AN - SCOPUS:0027430285
VL - 196
SP - 699
EP - 706
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -