Quinacrine mustard and lipophilic cations inhibitory to both vacuolar H+-ATPase and F0F1-ATP synthase

Yoshinori Moriyama, Vikram Patel, Masamitsu Futai

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

Various lipophilic cations, such as quinacrine mustard and dequalinium, which are known to inhibit mitochondrial F1-ATPase, strongly inhibited vacuolar H+-ATPase purified from bovine adrenal chromaffin granules. Quinacrine mustard bound irreversibly to vacuolar H+-ATPase subunit A, and the 115 kDa accessory polypeptide and dithiothreitol had no effect. The binding was competitively inhibited by chlorpromazine and quinacrine, and these compounds specifically reduced the amount of labeling of subunit A. Quinacrine mustard also prevented the binding of [α-32P]ATP to subunit A but had no effect on the binding of [3H]N-ethylmaleimide to either subunit A or the 115 kDa accessory polypeptide. These results suggest that the binding site of quinacrine mustard in subunit A is not related to the N-ethylmaleimide-binding site(s), which is important for activity.

Original languageEnglish
Pages (from-to)69-72
Number of pages4
JournalFEBS Letters
Volume359
Issue number1
DOIs
Publication statusPublished - Feb 6 1995

Keywords

  • Chromaffin granule
  • Dequalinium
  • Inhibitor
  • Lipophilic cation
  • Quinacrine mustard
  • Vacuolar H-ATPase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Quinacrine mustard and lipophilic cations inhibitory to both vacuolar H<sup>+</sup>-ATPase and F<sub>0</sub>F<sub>1</sub>-ATP synthase'. Together they form a unique fingerprint.

Cite this