Transport function and regulation of mitochondrial uncoupling
proteins 2 and 3

J 1999

Transport function and regulation of mitochondrial uncoupling proteins 2 and 3

JABŮREK, M., M. VAŘECHA, R.E. GIMENO, M. DEMBSKI, P. JEŽEK et. al.

Základní údaje

Originální název

Transport function and regulation of mitochondrial uncoupling proteins 2 and 3

Název česky

Transportní funkce a regulace mitochondriálních odpřahujících proteinů 2 a 3

Autoři

JABŮREK, M. (203 Česká republika), M. VAŘECHA (203 Česká republika, garant), R.E. GIMENO (840 Spojené státy), M. DEMBSKI (840 Spojené státy), P. JEŽEK (203 Česká republika), M. ZHANG (840 Spojené státy), P. BURN (840 Spojené státy), L.A. TARTAGLIA (840 Spojené státy) a K.D. GARLID (840 Spojené státy)

Vydání

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 1999, 0021-9258

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 7.666

Kód RIV

RIV/00216224:14330/99:00030506

Organizační jednotka

Fakulta informatiky

UT WoS

000082469700011

Klíčová slova anglicky

uncoupling protein; fatty acid; mitochondria

Štítky

fatty acid, mitochondria, uncoupling protein

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 3. 2010 12:20, Mgr. Miroslav Vařecha, Ph.D.

Anotace

ORIG CZ

V originále

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.

Česky

Transportní funkce a regulace mitochondriálních odpřahujících proteinů 2 a 3.

Citovat

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.

@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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