Linked Life Data

16508140

Source:http://linkedlifedata.com/resource/pubmed/id/16508140

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-3-1
pubmed:abstractText
Meiosis activating sterol (MAS), the intermediate of cholesterol biosynthesis, is an important substance to stimulate oocytes maturation in FSH-induced signal transduction pathway. Lanosterol 14alpha-demethylase (CYP51) converts lanosterol to MAS. Although MAS is firstly isolated from bovine testis, the information about bovine CYP51 gene and its expression is little. In present studies, the cDNA cloning, genomic structure, chromosomal mapping, and expression patterns of bovine CYP51 were demonstrated. The cDNA coding bovine CYP51 contains a 1509 bp open reading frame and a 1119 bp 3' untranslated region. And the bovine CYP51 gene includes 10 exons and spans about 17 kb. Screening the cattle RH5000 panel bovine CYP51 is mapped to chromosome 4 (0cR). The sequenced promoter region is TATA-less and contains several highly conserved regulatory elements, such as GC-box, cAMP-responsive elements (CRE), sterol regulatory element (SRE) which is important fragment for its transcription. No evidence of processed pseudogenes is found using long PCR and Southern blot. Northern blot analysis reveals that an approximately 2.7 kb mRNA is expressed in all the examined bovine tissues, while a 1.8 kb mRNA is found only in the mature bovine testis where the MAS is accumulated. Immunochemistry analysis shows that leydig cells express the highest level of the CYP51 protein in testis. Among different stages follicles it is localized primarily to the oocytes with the level varying slightly. Granulosa cells of primordial, primary and secondary follicles show background staining. While granulosa cells facing the antrum and cumulus granulosa cells of antral follicles show considerably heavier staining. The highest level is expressed in corpus lutea. These data indicate a stage- and cell type-specific expression of CYP51 protein in bovine oogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
430-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:16508140-Animals, pubmed-meshheading:16508140-Base Sequence, pubmed-meshheading:16508140-Blotting, Northern, pubmed-meshheading:16508140-Cattle, pubmed-meshheading:16508140-Cholestenes, pubmed-meshheading:16508140-Chromosome Mapping, pubmed-meshheading:16508140-Cloning, Molecular, pubmed-meshheading:16508140-Cytochrome P-450 Enzyme System, pubmed-meshheading:16508140-DNA, Complementary, pubmed-meshheading:16508140-Exons, pubmed-meshheading:16508140-Female, pubmed-meshheading:16508140-Immunohistochemistry, pubmed-meshheading:16508140-Introns, pubmed-meshheading:16508140-Male, pubmed-meshheading:16508140-Molecular Sequence Data, pubmed-meshheading:16508140-Ovary, pubmed-meshheading:16508140-Oxidoreductases, pubmed-meshheading:16508140-RNA, pubmed-meshheading:16508140-Sterol 14-Demethylase, pubmed-meshheading:16508140-Testis
pubmed:year
2006
pubmed:articleTitle
cDNA cloning, genomic structure and expression analysis of the bovine lanosterol 14alpha-demethylase (CYP51) in gonads.
pubmed:affiliation
College of Biological Science, China Agricultural University, Beijing, PR China.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't