| The contribution of uncoupling protein and ATP synthase to state 3 respiration in Acanthamoeba castellanii mitochondria. | |
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MedLine Citation:
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PMID: 15218546 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Wiesława Jarmuszkiewicz; Małgorzata Czarna; Claudine Sluse-Goffart; Francis E Sluse |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Acta biochimica Polonica Volume: 51 ISSN: 0001-527X ISO Abbreviation: Acta Biochim. Pol. Publication Date: 2004 |
Date Detail:
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Created Date: 2004-06-25 Completed Date: 2005-02-25 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 14520300R Medline TA: Acta Biochim Pol Country: Poland |
Other Details:
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Languages: eng Pagination: 533-8 Citation Subset: IM |
Affiliation:
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Laboratory of Bioenergetics, Adam Mickiewicz University, Poznań, Poland. wiesiaj@main.amu.edu.pl |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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ATP Synthetase Complexes
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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:
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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 |
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