| pubmed-article:8547174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8547174 | lifeskim:mentions | umls-concept:C0439849 | lld:lifeskim |
| pubmed-article:8547174 | lifeskim:mentions | umls-concept:C0086345 | lld:lifeskim |
| pubmed-article:8547174 | lifeskim:mentions | umls-concept:C2246646 | lld:lifeskim |
| pubmed-article:8547174 | lifeskim:mentions | umls-concept:C1517488 | lld:lifeskim |
| pubmed-article:8547174 | pubmed:issue | 5-6 | lld:pubmed |
| pubmed-article:8547174 | pubmed:dateCreated | 1996-2-20 | lld:pubmed |
| pubmed-article:8547174 | pubmed:abstractText | The isoenzymes of the 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene-isomerase (3 beta-HSD) gene family catalyse the transformation of all 5-ene-3 beta-hydroxysteroids into the corresponding 4-ene-3-keto-steroids and are responsible for the interconversion of 3 beta-hydroxy- and 3-keto-5 alpha-androstane steroids. The two human 3 beta-HSD genes and the three related pseudogenes are located on the chromosome 1p13.1 region, close to the centromeric marker D1Z5. The 3 beta-HSD isoenzymes prefer NAD+ to NADP+ as cofactor with the exception of the rat liver type III and mouse kidney type IV, which both prefer NADPH as cofactor for their specific 3-ketosteroid reductase activity due to the presence of Tyr36 in the rat type III and of Phe36 in mouse type IV enzymes instead of Asp36 found in other 3 beta-HSD isoenzymes. The rat types I and IV, bovine and guinea pig 3 beta-HSD proteins possess an intrinsic 17 beta-HSD activity specific to 5 alpha-androstane 17 beta-ol steroids, thus suggesting that such "secondary" activity is specifically responsible for controlling the bioavailability of the active androgen DHT. To elucidate the molecular basis of classical form of 3 beta-HSD deficiency, the structures of the types I and II 3 beta-HSD genes in 12 male pseudohermaphrodite 3 beta-HSD deficient patients as well as in four female patients were analyzed. The 14 different point mutations characterized were all detected in the type II 3 beta-HSD gene, which is the gene predominantly expressed in the adrenals and gonads, while no mutation was detected in the type I 3 beta-HSD gene predominantly expressed in the placenta and peripheral tissues. The mutant type II 3 beta-HSD enzymes carrying mutations detected in patients affected by the salt-losing form exhibit no detectable activity in intact transfected cells, at the exception of L108W and P186L proteins, which have some residual activity (approximately 1%). Mutations found in nonsalt-loser patients have some residual activity ranging from approximately 1 to approximately 10% compared to the wild-type enzyme. Characterization of mutant proteins provides unique information on the structure-function relationships of the 3 beta-HSD superfamily. | lld:pubmed |
| pubmed-article:8547174 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8547174 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8547174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8547174 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8547174 | pubmed:issn | 0960-0760 | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:SanchezRR | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:Luu-TheVV | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:SimardJJ | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:MonárSS | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:de LaunoitYY | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:DurocherFF | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:RhéaumeEE | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:MebarkiFF | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:LabrieYY | lld:pubmed |
| pubmed-article:8547174 | pubmed:author | pubmed-author:TurgeonCC | lld:pubmed |
| pubmed-article:8547174 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8547174 | pubmed:volume | 55 | lld:pubmed |
| pubmed-article:8547174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8547174 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:8547174 | pubmed:pagination | 489-505 | lld:pubmed |
| pubmed-article:8547174 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8547174 | pubmed:meshHeading | pubmed-meshheading:8547174-... | lld:pubmed |
| pubmed-article:8547174 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8547174 | pubmed:articleTitle | Structure-function relationships and molecular genetics of the 3 beta-hydroxysteroid dehydrogenase gene family. | lld:pubmed |
| pubmed-article:8547174 | pubmed:affiliation | Medical Research Council Group in Molecular Endocrinology, CHUL Research Center, Québec, Canada. | lld:pubmed |
| pubmed-article:8547174 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8547174 | pubmed:publicationType | Comparative Study | lld:pubmed |
