Document Detail


Effect of fatty acid-binding proteins on intermembrane fatty acid transport studies on different types and mutant proteins.
MedLine Citation:
PMID:  10998056     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Liposomes of different charge fixed to nitrocellulose filters were used to study the transfer of fatty acids to rat heart or liver mitochondria in the presence of fatty acid-binding protein (FABP) or albumin. [14C]Palmitate oxidation was used as a parameter. Different FABP types and heart FABP mutants were tested. The charge of the liposomes did not influence the solubilization and mitochondrial oxidation of palmitate without FABP and the amount of solubilized palmitate in the presence of FABP. Mitochondria did not show a preference for oxidation of FABP-bound palmitate over their tissue-specific FABP type. All FABP types increased palmitate oxidation by heart and liver mitochondria with neutral, positive and negative liposomes by 2.5-fold, 3.2-fold and twofold, respectively. Ileal lipid-binding protein and H-FABP mutants that do not bind fatty acid had no effect. Other H-FABP mutants had different effects, dependent on the site of mutation. The effect of albumin was similar to, but not dependent on, liposome charge. The ionic strength had only a slight effect. In conclusion, the transfer of palmitate from liposomal membranes to mitochondria was increased by all FABP types to a similar extent. The membrane charge had a large effect in contrast to the origin of the mitochondria.
Authors:
J H Veerkamp; H T Van Moerkerk And; A W Zimmerman
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  267     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2000-11-13     Completed Date:  2000-11-13     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  5959-66     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Nijmegen, The Netherlands. J.Veerkamp@bioch.kun.nl
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Animals
Biological Transport
Carrier Proteins / classification,  genetics,  metabolism*
Coenzyme A Ligases / metabolism
Diffusion
Fatty Acid-Binding Proteins
Fatty Acids / metabolism*
Humans
Liposomes / metabolism
Male
Membrane Potentials
Mitochondria, Heart / metabolism
Mitochondria, Liver / metabolism
Neoplasm Proteins*
Nerve Tissue Proteins*
Organ Specificity
Oxidation-Reduction
Palmitates / metabolism
Rats
Rats, Wistar
Recombinant Proteins / metabolism
Tumor Suppressor Proteins*
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/FABP7 protein, human; 0/Fabp7 protein, rat; 0/Fatty Acid-Binding Proteins; 0/Fatty Acids; 0/Liposomes; 0/Neoplasm Proteins; 0/Nerve Tissue Proteins; 0/Palmitates; 0/Recombinant Proteins; 0/Tumor Suppressor Proteins; EC 6.2.1.-/Coenzyme A Ligases

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


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