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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1995-6-5
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pubmed:databankReference | |
pubmed:abstractText |
Several mammalian livers contain monomeric 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD) with A-stereospecificity in hydrogen transfer, which differs from the B-specific dimeric enzyme of human placenta in its ability to catalyze the oxidoreduction of xenobiotic trans-dihydrodiols of aromatic hydrocarbons and carbonyl compounds. Here, we report the isolation and characterization of a mouse cDNA clone encoding monomeric 17 beta-HSD of the liver. This clone had an entire coding region for a protein of 323 amino acid residues with a molecular weight of 37,055. The deduced sequence of the protein aligned with a high degree of identity with rat and rabbit 20 alpha-HSDs, rat and human 3 alpha-HSD/dihydrodiol dehydrogenases, and bovine prostaglandin F synthase, which are members of the aldoketoreductase family, but was distinct from human 17 beta-HSD and carbonyl reductase, members of the short chain dehydrogenases. The expression of the cDNA in Escherichia coli resulted in synthesis of a protein that was active toward androgens, estrogens, and xenobiotic substrates. The recombinant and mouse liver 17 beta-HSDs also exhibited low 20 alpha-HSD activity toward progestins, which is similar to bifunctional activity of human placental 17 beta-HSD. Therefore, the mouse enzyme was given the designation of estradiol 17 beta-dehydrogenase (A-specific). Northern analysis of mouse tissues revealed the existence of a single 1.7-kilobase 17 beta-HSD mRNA species in the liver, kidney, testis, and stomach. The liver mRNA content was considerably more abundant than those found in the other tissues, as 17 beta-HSD protein was mainly detected in the liver by Western analysis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10461-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7737980-Amino Acid Sequence,
pubmed-meshheading:7737980-Animals,
pubmed-meshheading:7737980-Base Sequence,
pubmed-meshheading:7737980-Cloning, Molecular,
pubmed-meshheading:7737980-DNA, Complementary,
pubmed-meshheading:7737980-Estradiol Dehydrogenases,
pubmed-meshheading:7737980-Gene Expression,
pubmed-meshheading:7737980-Mice,
pubmed-meshheading:7737980-Molecular Sequence Data,
pubmed-meshheading:7737980-Peptide Fragments,
pubmed-meshheading:7737980-RNA, Messenger,
pubmed-meshheading:7737980-Restriction Mapping,
pubmed-meshheading:7737980-Sequence Alignment,
pubmed-meshheading:7737980-Sequence Homology, Amino Acid,
pubmed-meshheading:7737980-Tissue Distribution
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pubmed:year |
1995
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pubmed:articleTitle |
Molecular cloning and characterization of mouse estradiol 17 beta-dehydrogenase (A-specific), a member of the aldoketoreductase family.
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pubmed:affiliation |
Biochemistry Laboratory, Gifu Pharmaceutical University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study
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