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J Biol Chem, Vol. 274, Issue 37, 26003-26007, September 10, 1999
From the Uncoupling protein 1 (UCP1) dissipates energy and
generates heat by catalyzing back-flux of protons into the
mitochondrial matrix, probably by a fatty acid cycling mechanism. If
the newly discovered UCP2 and UCP3 function similarly, they will
enhance peripheral energy expenditure and are potential molecular
targets for the treatment of obesity. We expressed UCP2 and UCP3 in
Escherichia coli and reconstituted the detergent-extracted
proteins into liposomes. Ion flux studies show that purified UCP2 and
UCP3 behave identically to UCP1. They catalyze electrophoretic flux of
protons and alkylsulfonates, and proton flux exhibits an obligatory
requirement for fatty acids. Proton flux is inhibited by purine
nucleotides but with much lower affinity than observed with UCP1. These
findings are consistent with the hypothesis that UCP2 and UCP3 behave
as uncoupling proteins in the cell.
Transport Function and Regulation of Mitochondrial Uncoupling
Proteins 2 and 3
rek
,
echa,
ek
,
Department of Biochemistry and Molecular
Biology, Oregon Graduate Institute of Science and Technology,
Beaverton, Oregon 97006-8921, Institute of Physiology, Academy
of Science of the Czech Republic, Víde
ská
1083, CZ 14220, Prague, Czech Republic, ¶ Millenium
Pharmaceuticals, Cambridge, Massachusetts 02139, and ** Department of
Metabolic Diseases, Hoffman-La Roche Inc., Nutley, New Jersey 07110
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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