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J Biol Chem, Vol. 274, Issue 3, 1301-1305, January 15, 1999
From the Department of Cellular and Molecular Physiology, Tufts
University School of Medicine, Boston, Massachusetts 02111
It has been previously demonstrated that the
vacuolar H+-ATPase (V-ATPase) of clathrin-coated
vesicles is reversibly inhibited by disulfide bond formation between
conserved cysteine residues at the catalytic site on the A subunit
(Feng, Y., and Forgac, M. (1994) J. Biol. Chem. 269, 13224-13230). Proton transport and ATPase activity of the purified,
reconstituted V-ATPase are now shown to be inhibited by the nitric
oxide-generating reagent S-nitrosoglutathione (SNG). The
K0.5 for inhibition by SNG following incubation
for 30 min at 37 °C is 200-400 µM. As with disulfide
bond formation at the catalytic site, inhibition by SNG is reversed
upon treatment with 100 mM dithiothreitol and is partially
protected in the presence of ATP. Also as with disulfide bond
formation, treatment of the V-ATPase with SNG protects activity from
subsequent inactivation by N-ethylmaleimide, as
demonstrated by restoration of activity by dithiothreitol following
sequential treatment of the V-ATPase with SNG and
N-ethylmaleimide. Moreover, inhibition by SNG is readily
reversed by dithiothreitol but not by the reduced form of glutathione,
suggesting that the disulfide bond formed at the catalytic site of the
V-ATPase may not be immediately reduced under intracellular conditions.
These results suggest that SNG inhibits the V-ATPase through disulfide
bond formation between cysteine residues at the catalytic site and that
nitric oxide (or nitrosothiols) might act as a negative regulator of
V-ATPase activity in vivo.
The Vacuolar H+-ATPase of Clathrin-coated Vesicles Is
Reversibly Inhibited by S-Nitrosoglutathione
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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