K
Karim S. Echtay
Researcher at University of Balamand
Publications - 29
Citations - 4753
Karim S. Echtay is an academic researcher from University of Balamand. The author has contributed to research in topics: Mitochondrion & Superoxide. The author has an hindex of 22, co-authored 29 publications receiving 4553 citations. Previous affiliations of Karim S. Echtay include Ludwig Maximilian University of Munich & Medical Research Council.
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Journal ArticleDOI
Superoxide activates mitochondrial uncoupling proteins
Karim S. Echtay,Damien Roussel,Julie St-Pierre,Mika B. Jekabsons,Susana Cadenas,Jeffrey A. Stuart,James A. Harper,Stephen J. Roebuck,Alastair Morrison,Susan Pickering,John C. Clapham,Martin D. Brand +11 more
TL;DR: It is shown that superoxide increases mitochondrial proton conductance through effects on UCP1, UCP2 and UCP3, indicating that the interaction of superoxide with UCPs may be a mechanism for decreasing the concentrations of reactive oxygen species inside mitochondria.
Journal ArticleDOI
A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling
Karim S. Echtay,Telma C. Esteves,Julian L. Pakay,Mika B. Jekabsons,Adrian J. Lambert,Manuel Portero-Otin,Reinald Pamplona,Antonio Vidal-Puig,Steven Wang,Stephen J. Roebuck,Martin D. Brand +10 more
TL;DR: The findings indicate that hydroxynonenal is not merely toxic, but may be a biological signal to induce uncoupling through UCPs and ANT and thus decrease mitochondrial ROS production.
Journal ArticleDOI
Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants.
TL;DR: It is concluded that superoxide exerts its uncouplings effect by activating the proton transport mechanism of uncoupling proteins at the matrix side of the mitochondrial inner membrane.
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Mitochondrial uncoupling proteins--what is their physiological role?
TL;DR: This review critically examines the evidence of the different proposed mechanisms for UCPs functions, namely (a) to export fatty acid anions from mitochondria, (b) to regulate insulin secretion in pancreatic beta-cells, and (c) to cause mild uncoupling and so diminish mitochondrial superoxide production, hence protecting against oxidative damage.
Journal ArticleDOI
Coenzyme Q is an obligatory cofactor for uncoupling protein function
TL;DR: The identification of coenzyme Q (ubiquinone) as a native UCP cofactor is reported, and on addition of CoQ10 to reconstituted UCP1 from inclusion bodies, fatty-acid-dependent H+ transport reached the same rate as with native U CP1.