Document Detail


The contribution of uncoupling protein and ATP synthase to state 3 respiration in Acanthamoeba castellanii mitochondria.
MedLine Citation:
PMID:  15218546     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mitochondria of the amoeba Acanthamoeba castellanii possess a free fatty acid-activated uncoupling protein (AcUCP) that mediates proton re-uptake driven by the mitochondrial proton electrochemical gradient. We show that AcUCP activity diverts energy from ATP synthesis during state 3 mitochondrial respiration in a fatty acid-dependent way. The efficiency of AcUCP in mitochondrial uncoupling increases when the state 3 respiratory rate decreases as the AcUCP contribution is constant at a given linoleic acid concentration while the ATP synthase contribution decreases with respiratory rate. Respiration sustained by this energy-dissipating process remains constant at a given linoleic acid concentration until more than 60% inhibition of state 3 respiration by n-butyl malonate is achieved. The present study supports the validity of the ADP/O method to determine the actual contributions of AcUCP (activated with various linoleic acid concentrations) and ATP synthase in state 3 respiration of A.castellanii mitochondria fully depleted of free fatty acid-activated and describes how the two contributions vary when the rate of succinate dehydrogenase is decreased by succinate uptake limitation.
Authors:
Wiesława Jarmuszkiewicz; Małgorzata Czarna; Claudine Sluse-Goffart; Francis E Sluse
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Acta biochimica Polonica     Volume:  51     ISSN:  0001-527X     ISO Abbreviation:  Acta Biochim. Pol.     Publication Date:  2004  
Date Detail:
Created Date:  2004-06-25     Completed Date:  2005-02-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  14520300R     Medline TA:  Acta Biochim Pol     Country:  Poland    
Other Details:
Languages:  eng     Pagination:  533-8     Citation Subset:  IM    
Affiliation:
Laboratory of Bioenergetics, Adam Mickiewicz University, Poznań, Poland. wiesiaj@main.amu.edu.pl
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MeSH Terms
Descriptor/Qualifier:
ATP Synthetase Complexes / metabolism*
Acanthamoeba castellanii / physiology*
Adenosine Triphosphate / metabolism
Animals
Carrier Proteins / metabolism,  physiology*
Electrochemistry
Ion Channels
Linoleic Acid / chemistry,  metabolism
Membrane Potentials
Membrane Proteins / metabolism,  physiology*
Mitochondrial Proteins
Models, Chemical
Oxygen Consumption*
Phosphorylation
Protein Binding
Protons
Time Factors
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Ion Channels; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/Protons; 0/mitochondrial uncoupling protein; 2197-37-7/Linoleic Acid; 56-65-5/Adenosine Triphosphate; EC 2.7.4.-/ATP Synthetase Complexes

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


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