Linked Life Data

14672739

Source:http://linkedlifedata.com/resource/pubmed/id/14672739

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2003-12-15
pubmed:abstractText
In vitro enzyme assays have demonstrated that human type 10 17beta-hydroxysteroid dehydrogenase (17beta-HSD10) catalyzes the oxidation of 5alpha-androstane-3alpha,17beta-diol (adiol), an almost inactive androgen, to dihydrotestosterone (DHT) rather than androsterone or androstanedione. To further investigate the role of this steroid-metabolizing enzyme in intact cells, we produced stable transfectants expressing 17beta-HSD10 or its catalytically inactive Y168F mutant in human embryonic kidney (HEK) 293 cells. It was found that DHT levels in HEK 293 cells expressing 17beta-HSD10, but not its catalytically inactive mutant, will dramatically increase if adiol is added to culture media. Moreover, certain malignant prostatic epithelial cells have more 17beta-HSD10 than normal controls, and can generate DHT, the most potent androgen, from adiol. This event might promote prostate cancer growth. Analysis of the 17beta-HSD10 sequence shows that this enzyme does not have any ER retention signal or transmembrane segments and has not originated by divergence from a retinol dehydrogenase. The data suggest that the unique mitochondrial location of this HSD [Eur. J. Biochem. 268 (2001) 4899] does not prevent it from oxidizing the 3alpha-hydroxyl group of a C19 sterol in living cells. The experimental results lead to the conclusion that mitochondrial 17beta-HSD10 plays a significant part in a non-classical androgen synthesis pathway along with microsomal retinol dehydrogenases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0960-0760
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14672739-17-Hydroxysteroid Dehydrogenases, pubmed-meshheading:14672739-3-Hydroxyacyl CoA Dehydrogenases, pubmed-meshheading:14672739-3-alpha-Hydroxysteroid Dehydrogenase (B-Specific), pubmed-meshheading:14672739-Alcohol Oxidoreductases, pubmed-meshheading:14672739-Amino Acid Sequence, pubmed-meshheading:14672739-Amino Acid Substitution, pubmed-meshheading:14672739-Cell Line, pubmed-meshheading:14672739-Dihydrotestosterone, pubmed-meshheading:14672739-Epithelial Cells, pubmed-meshheading:14672739-Humans, pubmed-meshheading:14672739-Male, pubmed-meshheading:14672739-Molecular Sequence Data, pubmed-meshheading:14672739-Oxidation-Reduction, pubmed-meshheading:14672739-Prostate, pubmed-meshheading:14672739-Prostatic Neoplasms, pubmed-meshheading:14672739-Recombinant Proteins, pubmed-meshheading:14672739-Sequence Homology, Amino Acid, pubmed-meshheading:14672739-Transfection
pubmed:year
2003
pubmed:articleTitle
Oxidative 3alpha-hydroxysteroid dehydrogenase activity of human type 10 17beta-hydroxysteroid dehydrogenase.
pubmed:affiliation
Department of Pharmacology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't