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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1998-9-8
|
| pubmed:databankReference | |
| pubmed:abstractText |
The cDNA for a peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol, referred to as rLACH2, was isolated and its genomic structure was determined. The cDNA encoded a 419-amino-acid polypeptide with a calculated molecular weight of 46,011. Sequence analysis identified an active-site serine motif (Gly-x-Ser-x-Gly) common to carboxylesterases and lipases. When expressed in Escherichia coli, the cDNA directed expression of a protein immunoreactive to an anti-rLACH2 antibody with a molecular mass of 47 kDa, identical to that of purified rLACH2. Northern blot analysis showed marked induction of rLACH2 mRNA in the liver after feeding rats with di(2-ethylhexyl)phthalate, a peroxisome proliferator. The rLACH2 gene spanned about 19 kb and comprised 3 exons, the intron/exon boundaries of which were consistent with the donor/acceptor splice rule. A putative peroxisome proliferator response element (AGGTCATGGTTCA) was identified in the 5'-flanking region, suggesting the involvement of peroxisome proliferator-activated receptors in the regulation of rLACH2 gene expression.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Diethylhexyl Phthalate,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitoyl-CoA Hydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
248
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
608-12
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9703974-Amino Acid Sequence,
pubmed-meshheading:9703974-Animals,
pubmed-meshheading:9703974-Base Sequence,
pubmed-meshheading:9703974-Binding Sites,
pubmed-meshheading:9703974-Cloning, Molecular,
pubmed-meshheading:9703974-Cytosol,
pubmed-meshheading:9703974-DNA, Complementary,
pubmed-meshheading:9703974-Diethylhexyl Phthalate,
pubmed-meshheading:9703974-Enzyme Induction,
pubmed-meshheading:9703974-Escherichia coli,
pubmed-meshheading:9703974-Exons,
pubmed-meshheading:9703974-Genomic Library,
pubmed-meshheading:9703974-Introns,
pubmed-meshheading:9703974-Liver,
pubmed-meshheading:9703974-Molecular Sequence Data,
pubmed-meshheading:9703974-Molecular Weight,
pubmed-meshheading:9703974-Palmitoyl-CoA Hydrolase,
pubmed-meshheading:9703974-Rats,
pubmed-meshheading:9703974-Recombinant Proteins,
pubmed-meshheading:9703974-Serine
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
cDNA cloning and genomic organization of peroxisome proliferator-inducible long-chain acyl-CoA hydrolase from rat liver cytosol.
|
| pubmed:affiliation |
Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Science, Japan. junymd@ps.toyaku.ac.jp
|
| pubmed:publicationType |
Journal Article
|