The acyl-CoA thioesterase I is regulated by PPARα and HNF4α via a distal response element in the promoter
The cytosolic acyl-coenzyme A thioesterase I (Acot1) is an enzyme that hydrolyzes long-chain acyl-CoAs of C12-C20-CoA in chain length to the free fatty acid and CoA. Acot1 was shown previously to be strongly upregulated at the mRNA and protein level in rodents by fibrates. In this study, we show tha...
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| Published in | Journal of lipid research Vol. 48; no. 8; pp. 1781 - 1791 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Elsevier Inc
01.08.2007
American Society for Biochemistry and Molecular Biology Elsevier |
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| Abstract | The cytosolic acyl-coenzyme A thioesterase I (Acot1) is an enzyme that hydrolyzes long-chain acyl-CoAs of C12-C20-CoA in chain length to the free fatty acid and CoA. Acot1 was shown previously to be strongly upregulated at the mRNA and protein level in rodents by fibrates. In this study, we show that Acot1 mRNA levels were increased by 90-fold in liver by treatment with Wy-14,643 and that Acot1 mRNA was also increased by 15-fold in the liver of hepatocyte nuclear factor 4α (HNF4α) knockout animals. Our study identified a direct repeat 1 (DR1) located in the Acot1 gene promoter in mouse, which binds the peroxisome proliferator-activated receptor α (PPARα) and HNF4α. Chromatin immunoprecipitation (ChIP) assay showed that the identified DR1 bound PPARα/retinoid X receptor α (RXRα) and HNF4α, whereas the binding in ChIP was abrogated in the PPARα and HNF4α knockout mouse models. Reporter gene assays showed activation of the Acot1 promoter in cells by the PPARα agonist Wy-14,643 after cotransfection with PPARα/RXRα. However, transfection with a plasmid containing HNF4α also resulted in an increase in promoter activity. Together, these data show that Acot1 is under regulation by an interplay between HNF4α and PPARα. |
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| AbstractList | The cytosolic acyl-coenzyme A thioesterase I (Acot1) is an enzyme that hydrolyzes long-chain acyl-CoAs of C₁₂-C₂₀-CoA in chain length to the free fatty acid and CoA. Acot1 was shown previously to be strongly upregulated at the mRNA and protein level in rodents by fibrates. In this study, we show that Acot1 mRNA levels were increased by 90-fold in liver by treatment with Wy-14,643 and that Acot1 mRNA was also increased by 15-fold in the liver of hepatocyte nuclear factor 4α (HNF4α) knockout animals. Our study identified a direct repeat 1 (DR1) located in the Acot1 gene promoter in mouse, which binds the peroxisome proliferator-activated receptor α (PPARα) and HNF4α. Chromatin immunoprecipitation (ChIP) assay showed that the identified DR1 bound PPARα/retinoid X receptor α (RXRα) and HNF4α, whereas the binding in ChIP was abrogated in the PPARα and HNF4α knockout mouse models. Reporter gene assays showed activation of the Acot1 promoter in cells by the PPARα agonist Wy-14,643 after cotransfection with PPARα/RXRα. However, transfection with a plasmid containing HNF4α also resulted in an increase in promoter activity. Together, these data show that Acot1 is under regulation by an interplay between HNF4α and PPARα. The cytosolic acyl-coenzyme A thioesterase I (Acot1) is an enzyme that hydrolyzes long-chain acyl-CoAs of C12-C20-CoA in chain length to the free fatty acid and CoA. Acot1 was shown previously to be strongly upregulated at the mRNA and protein level in rodents by fibrates. In this study, we show that Acot1 mRNA levels were increased by 90-fold in liver by treatment with Wy-14,643 and that Acot1 mRNA was also increased by 15-fold in the liver of hepatocyte nuclear factor 4α (HNF4α) knockout animals. Our study identified a direct repeat 1 (DR1) located in the Acot1 gene promoter in mouse, which binds the peroxisome proliferator-activated receptor α (PPARα) and HNF4α. Chromatin immunoprecipitation (ChIP) assay showed that the identified DR1 bound PPARα/retinoid X receptor α (RXRα) and HNF4α, whereas the binding in ChIP was abrogated in the PPARα and HNF4α knockout mouse models. Reporter gene assays showed activation of the Acot1 promoter in cells by the PPARα agonist Wy-14,643 after cotransfection with PPARα/RXRα. However, transfection with a plasmid containing HNF4α also resulted in an increase in promoter activity. Together, these data show that Acot1 is under regulation by an interplay between HNF4α and PPARα. |
| Author | Shah, Yatrik Hunt, Mary C. Kim, Insook Gonzalez, Frank J. Dongol, Bikesh |
| Author_xml | – sequence: 1 givenname: Bikesh surname: Dongol fullname: Dongol, Bikesh organization: Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry C1-74, Karolinska University Hospital at Huddinge, S-141 86 Stockholm, Sweden – sequence: 2 givenname: Yatrik surname: Shah fullname: Shah, Yatrik organization: Laboratory of Metabolism, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 – sequence: 3 givenname: Insook surname: Kim fullname: Kim, Insook organization: Laboratory of Metabolism, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 – sequence: 4 givenname: Frank J. surname: Gonzalez fullname: Gonzalez, Frank J. organization: Laboratory of Metabolism, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 – sequence: 5 givenname: Mary C. surname: Hunt fullname: Hunt, Mary C. email: mary.hunt@ki.se organization: Karolinska Institutet, Department of Laboratory Medicine, Division of Clinical Chemistry C1-74, Karolinska University Hospital at Huddinge, S-141 86 Stockholm, Sweden |
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| Keywords | acyl-coenzyme A direct repeat 1 hepatic nuclear factor 4α peroxisome proliferator response element lipid metabolism peroxisome proliferator-activated receptor α |
| Language | English |
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| SubjectTerms | acyl-coenzyme A direct repeat 1 hepatic nuclear factor 4α lipid metabolism peroxisome proliferator response element peroxisome proliferator-activated receptor α |
| Title | The acyl-CoA thioesterase I is regulated by PPARα and HNF4α via a distal response element in the promoter |
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