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J. Biol. Chem., Vol. 276, Issue 41, 37986-37992, October 12, 2001
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From the Division of Signal Transduction, Harvard Institutes of
Medicine, Boston, Massachusetts 02215
Protein kinase C This article is dedicated to the late Dr. Lazaro J. Mandel. Laz's
friendship and scientific expertise in epithelia are greatly missed.
Rottlerin Is a Mitochondrial Uncoupler That Decreases Cellular
ATP Levels and Indirectly Blocks Protein Kinase C
Tyrosine
Phosphorylation*
(PKC) is activated
by stimuli that increase its tyrosine phosphorylation, including
neurotransmitters that initiate fluid secretion in salivary gland
(parotid) epithelial cells. Rottlerin, a compound reported to be a
PKC-selective inhibitor, rapidly increased the rate of oxygen
consumption (QO2) of parotid acinar cells and PC12
cells. In parotid cells, this was distinct from the effects of the
muscarinic receptor ligand carbachol, which promoted a sodium
pump-dependent increase in respiration. Rottlerin increased
the QO2 of isolated rat liver mitochondria to a level
similar to that produced when oxidative phosphorylation was initiated
by ADP or when mitochondria were uncoupled by carbonyl cyanide
p-trifluoromethoxyphenylhydrazone (FCCP). The effects of
rottlerin on mitochondrial QO2 were neither mimicked nor
blocked by the PKC inhibitor GF109203X. Rottlerin was not effective in blocking PKC activity in vitro. Exposure of freshly
isolated parotid acinar cells to rottlerin and FCCP reduced cellular
ATP levels and reduced stimuli-dependent increases in
tyrosine phosphorylation of PKC. Neither rottlerin nor FCCP reduced
stimuli-dependent PKC tyrosine phosphorylation in RPG1
cells (a salivary ductal line) or PC12 cells, consistent with their
dependence on glycolysis rather than oxidative phosphorylation for
energy-dependent processes. These results demonstrate that
rottlerin directly uncouples mitochondrial respiration from oxidative
phosphorylation. Previous studies using rottlerin should be evaluated cautiously.
*
This work was supported by Grant DE-10877 from the NIDCR,
National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Division of Signal
Transduction, Harvard Institutes of Medicine, Room 1025, Beth Israel
Deaconess Medical Center, Dept. of Medicine, 330 Brookline Ave.,
Boston, MA 02215. Tel.: 617-667-0949; Fax: 617-667-0957; E-mail:
ssoltoff@caregroup.harvard.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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