Carnitine cycle in brown adipose tissue mitochondria as a tool for studying the regulatory role of fatty acids in the uncoupling protein function
Language English Country Great Britain, England Media print
Document type Journal Article
PubMed
2920823
DOI
10.1016/0014-5793(89)81213-x
PII: 0014-5793(89)81213-X
Knihovny.cz E-resources
- MeSH
- Adenosine Diphosphate pharmacology MeSH
- Adenosine Triphosphate pharmacology MeSH
- Guanosine Diphosphate pharmacology MeSH
- Adipose Tissue, Brown metabolism MeSH
- Homeostasis MeSH
- Ion Channels MeSH
- Carnitine metabolism MeSH
- Kinetics MeSH
- Cricetinae MeSH
- Oleic Acid MeSH
- Fatty Acids, Nonesterified physiology MeSH
- Oleic Acids pharmacology MeSH
- Membrane Proteins metabolism MeSH
- Mitochondrial Proteins MeSH
- Mitochondria drug effects metabolism MeSH
- Uncoupling Agents pharmacology MeSH
- Oxygen Consumption drug effects MeSH
- Carrier Proteins * MeSH
- Uncoupling Protein 1 MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Adenosine Diphosphate MeSH
- Adenosine Triphosphate MeSH
- Guanosine Diphosphate MeSH
- Ion Channels MeSH
- Carnitine MeSH
- Oleic Acid MeSH
- Fatty Acids, Nonesterified MeSH
- Oleic Acids MeSH
- Membrane Proteins MeSH
- Mitochondrial Proteins MeSH
- Uncoupling Agents MeSH
- Carrier Proteins * MeSH
- Uncoupling Protein 1 MeSH
A concerted function of purine nucleotide (PN) binding and fatty acid (FA) release from the uncoupling protein (UP) resulting in the maximum coupling (potential) of brown adipose tissue (BAT) mitochondria was demonstrated. The uncoupling effect of FA was studied (at 4 mM MgCl2): 17 nmol oleate per mg protein caused a slight uncoupling with 8.9 mM ATP but with ATP below 3.6 mM almost total uncoupling was achieved. This shows that the PN-controlled gate can be stabilized in the closed conformation (with 8.9 mM ATP), also when FA is bound to UP. The sensitivity of the FA effect to ATP proves that oleate directly interacts with UP. The closed conformation of the H+ channel of UP is then abolished by oleate when a lower free ATP concentration is maintained outside.
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