Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-5-3
pubmed:abstractText
The lanosterol 14alpha-demethylase protein complex is composed of a cytochrome P450 enzyme CYP51 and its redox partner NADPH cytochrome P450 reductase. The complex participates in cholesterol biosynthesis and produces folicular fluid meiosis activating sterol (FF-MAS) from lanosterol. FF-MAS is metabolized further by sterol Delta14-reductase to testis-meiosis activating sterol (T-MAS). Additional enzymatic steps are needed before cholesterol is produced. Using the anti-human CYP51 antibody we have studied CYP51 protein expression by confocal microscopy in male and female mouse gonads. Leydig cells and acrosomes of spermatids express the highest levels of the CYP51 protein. CYP51 protein is also detected in primary mouse oocytes of non-treated mice and in some granulosa cells. While regulatory mechanisms responsible for FF-MAS accumulation in the ovary are not yet established, two mechanisms contributing to production the of T-MAS in the testis have been found. Potential in vivo roles of FF-MAS and T-MAS in fertilization are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
187
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
179-87
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Lanosterol 14alpha-demethylase and MAS sterols in mammalian gametogenesis.
pubmed:affiliation
Medical Center for Molecular Biology, Faculty of Medicine, Institute of Biochemistry, University of Ljubljana, Vrazov trg 2, 1000, Ljubljana, Slovenia. damjana.rozman@mf.uni-lj.si
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't