Source:http://linkedlifedata.com/resource/pubmed/id/17613526
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
2007-9-10
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pubmed:databankReference | |
pubmed:abstractText |
Phytanic acid and pristanic acid are derived from phytol, which enter the body via the diet. Phytanic acid contains a methyl group in position three and, therefore, cannot undergo beta-oxidation directly but instead must first undergo alpha-oxidation to pristanic acid, which then enters beta-oxidation. Both these pathways occur in peroxisomes, and in this study we have identified a novel peroxisomal acyl-CoA thioesterase named ACOT6, which we show is specifically involved in phytanic acid and pristanic acid metabolism. Sequence analysis of ACOT6 revealed a putative peroxisomal targeting signal at the C-terminal end, and cellular localization experiments verified it as a peroxisomal enzyme. Subcellular fractionation experiments showed that peroxisomes contain by far the highest phytanoyl-CoA/pristanoyl-CoA thioesterase activity in the cell, which could be almost completely immunoprecipitated using an ACOT6 antibody. Acot6 mRNA was mainly expressed in white adipose tissue and was co-expressed in tissues with Acox3 (the pristanoyl-CoA oxidase). Furthermore, Acot6 was identified as a target gene of the peroxisome proliferator-activated receptor alpha (PPARalpha) and is up-regulated in mouse liver in a PPARalpha-dependent manner.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/PPAR alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Phytanic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Thiolester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/phytanoyl-coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/pristanic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26707-16
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pubmed:meshHeading |
pubmed-meshheading:17613526-Animals,
pubmed-meshheading:17613526-Base Sequence,
pubmed-meshheading:17613526-Coenzyme A,
pubmed-meshheading:17613526-Fatty Acids,
pubmed-meshheading:17613526-Male,
pubmed-meshheading:17613526-Mice,
pubmed-meshheading:17613526-Mice, Inbred C57BL,
pubmed-meshheading:17613526-Molecular Sequence Data,
pubmed-meshheading:17613526-Oxidation-Reduction,
pubmed-meshheading:17613526-PPAR alpha,
pubmed-meshheading:17613526-Peroxisomes,
pubmed-meshheading:17613526-Phytanic Acid,
pubmed-meshheading:17613526-Thiolester Hydrolases
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pubmed:year |
2007
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pubmed:articleTitle |
Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse.
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pubmed:affiliation |
Department of Laboratory Medicine, Division of Clinical Chemistry, C1-74, Karolinska University Hospital at Huddinge, Karolinska Institutet, SE-141 86 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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