Linked Life Data

2789010

Source:http://linkedlifedata.com/resource/pubmed/id/2789010

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-10-5
pubmed:abstractText
A complete amino acid sequence for rat testis P-450 17 alpha was deduced from nucleotide analysis of a cDNA clone isolated from a rat Leydig cell library. This cDNA expressed in COS-1 cells both 17 alpha-hydroxylase and 17,20 lyase activities. Rat P-450 17 alpha exhibited significant similarity to the nucleotide and deduced amino acid sequences of the bovine and human P-450 17 alpha, particularly with the highly conserved regions and secondary structure. The rat P-450 17 alpha is anchored to the ER by two transmembrane regions: the N-terminal insertion peptide and the stop-transfer sequence. The C-terminal is associated with the ER by four hydrophobic clefts including the steroid-binding site. We have demonstrated a dual effect of hCG, causing early increases of Leydig cell P-450 17 alpha mRNA levels at low doses, while higher desensitizing doses caused marked subsequent reduction of mRNA levels. Our studies demonstrate that gonadotropin stimulation and desensitization of P-450 17 alpha dependent enzymes (17 alpha-hydroxylase/17,20 desmolase) in the adult rat testis and E2 induced desensitization in fetal Leydig cells are related to levels of P-450 17 alpha mRNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
564
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-76
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Lactogen and LH receptors. Rat P-450 17 alpha, structural analysis and hormonal regulation of mRNA levels in the Leydig cell.
pubmed:affiliation
Molecular Endocrinology Section, National Institute of Child Health and Human Development, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article