Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-12-13
pubmed:databankReference
pubmed:abstractText
The gene encoding aromatase P-450 (CYP XIX) has been isolated from two types of human genomic DNA libraries. It spans at least 70 kb and consists of 10 exons. The translational initiation site and the termination site are located in exon 2 and exon 10, respectively. The promoter region of the gene contains a TATA box, a CAAT box and two putative AP-1 binding sites beginning at -28, -83, -55 and -68 bp, respectively, from the transcriptional initiation site. In addition, a palindromic nucleotide sequence is observed between -209 and -196 and two types of repetitious hexanucleotide (consensus: AATGAA and CCATAAGG) are also present within the regions between -485 and -433 and between -358 and -331. Transient expression studies of chloramphenicol acetyltransferase constructs bearing various lengths of 5'-flanking region of the gene show that the region between -500 and -243 contains negative cis-acting element(s), whereas the region between -242 and -183 is required for efficient transcriptional activity. Northern blot analysis demonstrates that the expression of aromatose P-450 gene is remarkably stimulated by treatment of cells with 12-O-tetradecanoyl-phorbol 13-acetate. By chloramphenicol acetyltransferase assay the region up to nucleotide position -242 relative to the transcriptional initiation site is shown to participate in the transcriptional responsiveness to this phorbol ester.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
193
pubmed:geneSymbol
CYP XIX
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
559-65
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structural and functional characterization of human aromatase P-450 gene.
pubmed:affiliation
Department of Medical Chemistry, Kochi Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't