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Fatty acid interaction with mitochondrial uncoupling proteins.
- Source :
-
Journal of bioenergetics and biomembranes [J Bioenerg Biomembr] 1999 Oct; Vol. 31 (5), pp. 457-66. - Publication Year :
- 1999
-
Abstract
- The phenomena of fatty acid interaction with mitochondrial integral membrane proteins, namely uncoupling proteins (UCPs), are reviewed to emphasize the fatty acid cycling mechanism that has been suggested to explain the UCP function. Fatty acid-induced uncoupling is suggested to serve in bioenergetic systems, to set the optimum efficiency, and to tune the degree of coupling of oxidative phosphorylation. Fatty acid interaction with the "classic" uncoupling protein (UCP1) from mitochondria of thermogenic brown adipose tissue (BAT) is well known. UCP1 is considered to mediate purine nucleotide-sensitive uniport of monovalent unipolar anions, including anionic fatty acids. The return of protonated fatty acid leads to H+ uniport and uncoupling. Experiments supporting this mechanism are also reviewed for plant uncoupling mitochondrial protein (PUMP) and ADP/ATP carrier. The fatty acid cycling mechanism is predicted, as well for the recently discovered uncoupling proteins, UCP2 and UCP3.
- Subjects :
- Animals
Binding Sites
Forecasting
Humans
Ion Channels
Mitochondrial Proteins
Plants
Proteolipids metabolism
Structure-Activity Relationship
Uncoupling Protein 1
Adipose Tissue, Brown metabolism
Carrier Proteins metabolism
Fatty Acids metabolism
Membrane Proteins metabolism
Mitochondria metabolism
Uncoupling Agents metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0145-479X
- Volume :
- 31
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of bioenergetics and biomembranes
- Publication Type :
- Academic Journal
- Accession number :
- 10653474
- Full Text :
- https://doi.org/10.1023/a:1005496306893