Fatty Acid Interaction with Mitochondrial Uncoupling Proteins |
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Authors: | Petr Ježek |
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Institution: | (1) Institute of Physiology, Department of Membrane Transport Biophysics, Academy of Sciences of the Czech Republic, Vídenská 1083, CZ 14220 Prague, Czech Republic |
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Abstract: | The phenomena of fatty acid interaction with mitochondrial integral membrane proteins, namelyuncoupling proteins (UCPs), are reviewed to emphasize the fatty acid cycling mechanism thathas been suggested to explain the UCP function. Fatty acid-induced uncoupling is suggestedto serve in bioenergetic systems, to set the optimum efficiency, and to tune the degree ofcoupling of oxidative phosphorylation. Fatty acid interaction with the classic uncouplingprotein (UCP1) from mitochondria of thermogenic brown adipose tissue (BAT) is well known.UCP1 is considered to mediate purine nucleotide-sensitive uniport of monovalent unipolaranions, including anionic fatty acids. The return of protonated fatty acid leads to H+ uniportand uncoupling. Experiments supporting this mechanism are also reviewed for plant uncouplingmitochondrial protein (PUMP) and ADP/ATP carrier. The fatty acid cycling mechanism ispredicted, as well for the recently discovered uncoupling proteins, UCP2 and UCP3. |
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Keywords: | Uncoupling of mitochondria uncoupling proteins UCP1 UCP2 UCP3 plant uncoupling mitochondrial protein ADP/ATP carrier fatty acids proteoliposomes brown adipose tissue mitochondria |
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