Abstract
In an effort to understand the relationship between a 72-kDa heat shock protein (Hsp72) and peroxisome proliferator-activated receptors (PPARs), we have characterized their interaction using clofibric acid-Sepharose chromatography and co-immunoprecipitation with antisera raised against either rat PPAR (rPPAR) or Hsp72. First, we observed that both rPPAR and Hsp72 elute in a clofibrate-dependent manner from the clofibric acid-Sepharose matrix. Second, we found that immunoprecipitation of either protein from solution resulted in the precipitation of the other. This result was obtained from rat liver cytosol, from Spodoptera frugiperda (Sf9) insect cells expressing rPPAR, and from reticulocyte lysate rPPAR expression systems. These results suggest that Hsp72 and rPPAR form a complex in vivo and that Hsp72 may play a role in the folding, subcellular localization, and/or signaling pathway of PPARs.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antibodies, Monoclonal
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Base Sequence
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Blotting, Western
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Chromatography, Affinity
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Clofibrate
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Cloning, Molecular
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DNA Primers
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Electrophoresis, Polyacrylamide Gel
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Heat-Shock Proteins / biosynthesis
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Heat-Shock Proteins / isolation & purification
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Heat-Shock Proteins / metabolism*
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Liver / metabolism*
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Male
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Molecular Sequence Data
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Moths
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Polymerase Chain Reaction / methods
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Rats
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Rats, Inbred F344
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Receptors, Cytoplasmic and Nuclear / biosynthesis
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Receptors, Cytoplasmic and Nuclear / isolation & purification
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Transcription Factors / biosynthesis
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Transcription Factors / isolation & purification
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Transcription Factors / metabolism*
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Transfection
Substances
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Antibodies, Monoclonal
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DNA Primers
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Heat-Shock Proteins
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Receptors, Cytoplasmic and Nuclear
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Recombinant Proteins
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Transcription Factors
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Clofibrate