Document Detail


On the mechanism of mitochondrial uncoupling protein 1 function.
MedLine Citation:
PMID:  16291746     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Native uncoupling protein 1 (UCP 1) was purified from rat mitochondria by hydroxyapatite chromatography and identified by peptide mass mapping and tandem mass spectrometry. Native and expressed UCP 1 were reconstituted into liposomes, and proton flux through UCP 1 was shown to be fatty acid-dependent and GDP-sensitive. To investigate the mechanism of action of UCP 1, we determined whether hydrophilic modification of the omega-carbon of palmitate effected its transport function. We show that proton flux was greater through native UCP 1-containing proteoliposomes when facilitated by less hydrophilically modified palmitate (palmitate > omega-methoxypalmitate > omega-hydroxypalmitate with little or no proton flux due to glucose-O-omega-palmitate or undecanesulfonate). We show that non-proton-dependent charge transfer was greater when facilitated by less hydrophilically modified palmitate (palmitate/undecanesulfonate > omega-methoxypalmitate > omega-hydroxypalmitate, with no non-proton-dependent charge transfer flux due to glucose-O-omega-palmitate). We show that the GDP-inhibitable oxygen consumption rate in brown adipose tissue mitochondria was reversed by palmitate (as expected) but not by glucose-O-omega-palmitate. Our data are consistent with the model that UCP 1 flips long-chain fatty acid anions and contradict the "cofactor" model of UCP 1 function.
Authors:
Eamon P Breen; Sebastien G Gouin; Andrew F Murphy; Lee R Haines; Angela M Jackson; Terry W Pearson; Paul V Murphy; Richard K Porter
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-11-16
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-23     Completed Date:  2006-03-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2114-9     Citation Subset:  IM    
Affiliation:
School of Biochemistry and Immunology, Trinity College Dublin, College Green, Dublin 2, Ireland.
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MeSH Terms
Descriptor/Qualifier:
Adipose Tissue, Brown / metabolism
Amino Acid Sequence
Animals
Anions
Carrier Proteins / chemistry,  physiology*
Electrophoresis, Polyacrylamide Gel
Escherichia coli / metabolism
Fatty Acids / metabolism
Guanosine Diphosphate / chemistry
Ion Channels
Ions
Liposomes / metabolism
Mass Spectrometry
Membrane Proteins / chemistry,  physiology*
Mitochondria / metabolism
Mitochondrial Proteins
Molecular Sequence Data
Oxygen Consumption
Palmitic Acid / chemistry
Peptide Mapping
Phosphorylation
Proteolipids / metabolism
Protons
Rats
Rats, Wistar
Recombinant Proteins / chemistry
Spectrometry, Fluorescence
Uncoupling Agents / chemistry
Chemical
Reg. No./Substance:
0/Anions; 0/Carrier Proteins; 0/Fatty Acids; 0/Ion Channels; 0/Ions; 0/Liposomes; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/Proteolipids; 0/Protons; 0/Recombinant Proteins; 0/Uncoupling Agents; 0/mitochondrial uncoupling protein; 0/proteoliposomes; 146-91-8/Guanosine Diphosphate; 57-10-3/Palmitic Acid

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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