Linked Life Data

8547173

Source:http://linkedlifedata.com/resource/pubmed/id/8547173

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1996-2-20
pubmed:databankReference
pubmed:abstractText
The enzyme 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase (3 beta-HSD) is essential for the production of all classes of steroid hormones. Multiple isozymes of this enzyme have been demonstrated in the kidney and liver of both the rat and the mouse, although the function of the enzyme in these tissues is unknown. We have characterized three isozymes of 3 beta-HSD expressed in various tissues of the hamster. Both western and northern blot analyses demonstrated very high levels of 3 beta-HSD in the adrenal, kidney and male liver. Conversely, there were extremely low levels of enzyme expression in the female liver. cDNA libraries prepared from RNA isolated from hamster adrenal, kidney and liver were screened with a full-length cDNA encoding human type 1 3 beta-HSD. Separate cDNAs encoding three isoforms of 3 beta-HSD were isolated from these libraries. To examine the properties of the isoforms, the cDNAs were ligated into expression vectors for over-expression in 293 human fetal kidney cells. The type 1 isoform, isolated from an adrenal cDNA library, was identified as a high-affinity 3 beta-hydroxysteroid dehydrogenase. A separate isoform, designated type 2, was isolated from the kidney, and this was also a high-affinity dehydrogenase/isomerase. Two cDNAs were isolated from the liver, one identical in sequence to type 2 of the kidney, and a distinct cDNA encoding an isoform designated type 3. The type 3 3 beta-HSD possessed no steroid dehydrogenase activity but was found to function as a 3-ketosteroid reductase. Thus male hamster liver expresses a high-affinity 3 beta-HSD (type 2) and a 3-ketosteroid reductase (type 3), whereas the kidney of both sexes express the type 2 3 beta-HSD isoform. These differ from the type 1 3 beta-HSD expressed in the adrenal cortex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0960-0760
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
481-7
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:8547173-Amino Acid Sequence, pubmed-meshheading:8547173-Animals, pubmed-meshheading:8547173-Cloning, Molecular, pubmed-meshheading:8547173-Cricetinae, pubmed-meshheading:8547173-DNA, Complementary, pubmed-meshheading:8547173-Female, pubmed-meshheading:8547173-Gene Expression Regulation, Enzymologic, pubmed-meshheading:8547173-Isoenzymes, pubmed-meshheading:8547173-Male, pubmed-meshheading:8547173-Mesocricetus, pubmed-meshheading:8547173-Molecular Sequence Data, pubmed-meshheading:8547173-Multienzyme Complexes, pubmed-meshheading:8547173-Progesterone Reductase, pubmed-meshheading:8547173-RNA, Messenger, pubmed-meshheading:8547173-Recombinant Proteins, pubmed-meshheading:8547173-Sequence Alignment, pubmed-meshheading:8547173-Sequence Homology, Amino Acid, pubmed-meshheading:8547173-Steroid Isomerases, pubmed-meshheading:8547173-Substrate Specificity
pubmed:year
1995
pubmed:articleTitle
Expression and characterization of isoforms of 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase in the hamster.
pubmed:affiliation
Cecil H. & Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas 75235-9051, USA.
pubmed:publicationType
Journal Article