JABŮREK, M., M. VAŘECHA, R.E. GIMENO, M. DEMBSKI, P. JEŽEK, M. ZHANG, P. BURN, L.A. TARTAGLIA a K.D. GARLID. Transport function and regulation of mitochondrial uncoupling proteins 2 and 3. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 1999, roč. 274, č. 37, s. 26003-26007. ISSN 0021-9258. |
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@article{485150, author = {Jabůrek, M. and Vařecha, M. and Gimeno, R.E. and Dembski, M. and Ježek, P. and Zhang, M. and Burn, P. and Tartaglia, L.A. and Garlid, K.D.}, article_location = {Bethesda, USA}, article_number = {37}, keywords = {uncoupling protein; fatty acid; mitochondria}, language = {eng}, issn = {0021-9258}, journal = {Journal of Biological Chemistry}, title = {Transport function and regulation of mitochondrial uncoupling proteins 2 and 3}, volume = {274}, year = {1999} }
TY - JOUR ID - 485150 AU - Jabůrek, M. - Vařecha, M. - Gimeno, R.E. - Dembski, M. - Ježek, P. - Zhang, M. - Burn, P. - Tartaglia, L.A. - Garlid, K.D. PY - 1999 TI - Transport function and regulation of mitochondrial uncoupling proteins 2 and 3 JF - Journal of Biological Chemistry VL - 274 IS - 37 SP - 26003-26007 EP - 26003-26007 PB - Amer. Soc. Biochem. Mol. Biol. SN - 00219258 KW - uncoupling protein KW - fatty acid KW - mitochondria N2 - 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. ER -
JABŮREK, M., M. VAŘECHA, R.E. GIMENO, M. DEMBSKI, P. JEŽEK, M. ZHANG, P. BURN, L.A. TARTAGLIA a K.D. GARLID. Transport function and regulation of mitochondrial uncoupling proteins 2 and 3. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 1999, roč.~274, č.~37, s.~26003-26007. ISSN~0021-9258.
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