High impact information on CYP51

• Herein we report CYP51 unequivocally localized to acrosomal membranes of male germ cells in mouse, bull, and ram, in which it synthesizes FF-MAS in the presence of the acrosomal form of nicotinamide adenine dinucleotide phosphate reduced-P450 reductase [1].
• The decreased synthesis of ergosterol and the concomitant accumulation of 14 alpha-methylsterols provide indirect evidence that R126638 inhibits the activity of CYP51 that catalyzes the oxidative removal of the 14 alpha-methyl group of lanosterol or eburicol [2].
• In mouse liver, a 53-kDa CYP51 is no longer detected in trans Golgi, suggesting retrieval back to the ER and no further transport to other organelles [1].
• Demethylation of lanosterol to FF-MAS by the acrosomal lanosterol 14 alpha-demethylase enzyme complex demonstrates for the first time the ability of ejaculate sperm to synthesize meiosis-activating sterols [1].
• These facts suggest the contribution of ovarian P45014DM to the gonadotropin-dependent formation of the meiosis-activating sterol, and provide a clue to understanding the mechanism how gonadotropins initiate the resumption of meiosis of mammalian oocytes [3].

Biological context of CYP51

• CYP51 proteins are post-translationally modified by glycosylations in the Golgi and on acrosomal membranes of the sperm [4].
• And the bovine CYP51 gene includes 10 exons and spans about 17 kb [5].
• These data indicate a stage- and cell type-specific expression of CYP51 protein in bovine oogenesis [5].
• Screening the cattle RH5000 panel bovine CYP51 is mapped to chromosome 4 (0cR) [5].
• The cDNA coding bovine CYP51 contains a 1509 bp open reading frame and a 1119 bp 3' untranslated region [5].

Anatomical context of CYP51

• Although MAS is firstly isolated from bovine testis, the information about bovine CYP51 gene and its expression is little [5].
• cDNA cloning, genomic structure and expression analysis of the bovine lanosterol 14alpha-demethylase (CYP51) in gonads [5].
• Immunochemistry analysis shows that leydig cells express the highest level of the CYP51 protein in testis [5].

Associations of CYP51 with chemical compounds

• The mRNAs for the MAS-producing enzyme lanosterol 14alpha-demethylase (CYP51) arise by alternative poly (A) signal selection [4].

References