A structure-activity study of fatty acid interaction with mitochondrial uncoupling protein

FEBS Letters
Petr JezekKeith Garlid

Abstract

Fatty acid (FA) uniport via mitochondrial uncoupling protein (UcP) was detected fluorometrically with PBFI, potassium-binding benzofuran phthalate and SPQ, 6-methoxy-N-(3-sulfopropyl)-quinolinium, indicating K+ and H+, respectively. The FA structural patterns required for FA flip-flop, UcP-mediated FA uniport, activation of UcP-mediated H+ transport in proteoliposomes, and inhibition of UcP-mediated Cl- uniport by FA, were identical. Positive responses were found exclusively with FA which were able to flip-flop in a protonated form across the membrane and no responses were found with 'inactive' FA lacking the flip-flop ability. The findings support the existence of FA cycling mechanism.

References

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Citations

Mar 21, 2003·Archives of Biochemistry and Biophysics·Shu-Gui Huang
Mar 10, 2001·Biochimica Et Biophysica Acta·E Rial, M M González-Barroso
Apr 16, 1998·Biochimica Et Biophysica Acta·V P Skulachev
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Jul 20, 2002·The International Journal of Biochemistry & Cell Biology·Petr Jezek
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May 4, 2006·Annual Review of Plant Biology·Aníbal Eugênio VercesiHernan Chaimovich
Jan 11, 2013·Oxidative Medicine and Cellular Longevity·Petr JežekLydie Plecitá-Hlavatá
Mar 9, 2010·FEBS Letters·Petr JezekKeith D Garlid
Jun 30, 2006·The International Journal of Biochemistry & Cell Biology·Petr JezekMartin Jabůrek
Feb 12, 2004·Biochimica Et Biophysica Acta·Eduardo RialAmalia Ledesma
Oct 10, 2013·British Journal of Pharmacology·Sergiy M NadtochiyPaul S Brookes
Jan 29, 2013·The International Journal of Biochemistry & Cell Biology·Martin JabůrekPetr Ježek
Jul 30, 2004·Biochimica Et Biophysica Acta·Paula TomásEduardo Rial
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Jan 21, 2018·Antioxidants & Redox Signaling·Petr JežekMartin Jabůrek
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