Source:http://linkedlifedata.com/resource/pubmed/id/11469812
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2001-7-25
|
pubmed:abstractText |
Androgen action in mammals can be regulated at the pre-receptor level by the intracellular formation and degradation of potent androgens, such as 5alpha-dihydrotestosterone (5alpha-DHT). In androgen target tissues (e.g. prostate), 5alpha-DHT is formed from circulating testosterone by the action of the type 2 steroid 5alpha-reductase (5alpha-R) and its action is terminated by the action of a reductive 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) which forms the weak androgen 3alpha-androstanediol. Oxidative 3alpha-HSD isoforms, however, can provide an alternative source of potent androgens by converting 3alpha-androstanediol to 5alpha-DHT. Working in concert, 5alpha-Rs and 3alpha-HSDs determine the amount and the type of androgen available for the androgen receptor and hence affect transcription of genes under androgen control. In peripheral tissues (e.g. liver), type 1 5alpha-R and reductive 3alpha-HSD isoforms work consecutively to eliminate androgens and protect against hormone excess. Thus, different 5alpha-R and 3alpha-HSD isoforms participate in distinct anabolic and catabolic processes and their important roles in androgen action render them drug targets for the treatment of androgen-dependent diseases.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
1521-690X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
15
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
79-94
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:11469812-3-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:11469812-3-Oxo-5-alpha-Steroid 4-Dehydrogenase,
pubmed-meshheading:11469812-3-alpha-Hydroxysteroid Dehydrogenase (B-Specific),
pubmed-meshheading:11469812-Androgens,
pubmed-meshheading:11469812-Animals,
pubmed-meshheading:11469812-Humans
|
pubmed:year |
2001
|
pubmed:articleTitle |
Steroid 5alpha-reductases and 3alpha-hydroxysteroid dehydrogenases: key enzymes in androgen metabolism.
|
pubmed:affiliation |
Department of Pharmacology, University of Pennsylvania School of Medicine, 3620 Hamilton Walk, Philadelphia, PA, 19104-6084, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
|