Document Detail


Coordinate induction of acyl-CoA binding protein, fatty acid binding protein and peroxisomal beta-oxidation by peroxisome proliferators.
MedLine Citation:
PMID:  8499488     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Acyl-CoA binding protein (ACBP) and fatty acid binding protein (FABP) are important intracellular lipid binding proteins. The purpose of the present experiments was to test the hypothesis that peroxisome proliferators induce ACBP in rat hepatocytes as has been shown previously for FABP. The effects of two structurally dissimilar peroxisome proliferators perfluorodecanoic acid (PFDA) and clofibric acid (CPIB) were examined in primary rat hepatocyte cultures in a chemically defined media. Both compounds alter lipid metabolism in primary rat hepatocytes in a similar fashion, although PFDA is more potent than CPIB at inducing peroxisomal beta-oxidation. In addition, PFDA and CPIB compete with long-chain fatty acids for binding to FABP but do not compete with long-chain acyl-CoA esters for binding to ACBP. The concentration of ACBP and FABP was increased in peroxisome proliferator-treated hepatocytes relative to vehicle controls within 48 h of treatment. Evidence is given to support increases in ACBP and FABP mRNA being the cause of the increased protein levels by peroxisome proliferators. In addition, the peroxisome proliferators PFDA, perfluorooctanoic acid and ciprofibrate induced hepatic ACBP following in vivo administration to rats indicating that this phenomena is not exclusive to in vitro systems. Therefore, ACBP appears to be a member of the peroxisome proliferator loci, a group of lipid metabolizing proteins, including FABP, which are regulated by peroxisome proliferators such as fibric acids and perfluorinated fatty acids.
Authors:
J P Vanden Heuvel; P F Sterchele; D J Nesbit; R E Peterson
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1177     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1993 Jun 
Date Detail:
Created Date:  1993-07-01     Completed Date:  1993-07-01     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  183-90     Citation Subset:  IM    
Affiliation:
Environmental Toxicology Center, University of Wisconsin, Madison 53706.
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MeSH Terms
Descriptor/Qualifier:
Animals
Carrier Proteins / biosynthesis*,  metabolism
Cells, Cultured
Clofibric Acid / administration & dosage,  pharmacology*
Coenzyme A Ligases / biosynthesis
Decanoic Acids / administration & dosage,  pharmacology*
Diazepam Binding Inhibitor
Enzyme Induction / drug effects
Fatty Acid-Binding Proteins
Fluorocarbons / administration & dosage,  pharmacology*
Liver / drug effects*,  metabolism
Male
Microbodies / drug effects*,  metabolism
Neoplasm Proteins*
Nerve Tissue Proteins*
Oleic Acid
Oleic Acids / metabolism
Oxidation-Reduction / drug effects
Protein Biosynthesis / drug effects
RNA, Messenger / isolation & purification,  metabolism
Rats
Rats, Sprague-Dawley
Repressor Proteins*
Saccharomyces cerevisiae Proteins*
Grant Support
ID/Acronym/Agency:
CA07175/CA/NCI NIH HHS; GM41131/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Decanoic Acids; 0/Diazepam Binding Inhibitor; 0/Fabp7 protein, rat; 0/Fatty Acid-Binding Proteins; 0/Fluorocarbons; 0/Neoplasm Proteins; 0/Nerve Tissue Proteins; 0/Oleic Acids; 0/RNA, Messenger; 0/Repressor Proteins; 0/Saccharomyces cerevisiae Proteins; 112-80-1/Oleic Acid; 335-76-2/perfluorodecanoic acid; 882-09-7/Clofibric Acid; EC 6.2.1.-/Coenzyme A Ligases; EC 6.2.1.3/FAA2 protein, S cerevisiae; EC 6.2.1.3/long-chain-fatty-acid-CoA ligase

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


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