A functional cytochrome P450 lanosterol 14α -demethylase CYP51 enzyme in the acrosome: transport through the Golgi and synthesis of meiosis-activating sterols. (CROSBI ID 109957)
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Podaci o odgovornosti
Cotman, Marko ; Ježek, Davor ; Fon Tacer Klementina ; Frangež, R ; Rozman, Damjana
engleski
A functional cytochrome P450 lanosterol 14α -demethylase CYP51 enzyme in the acrosome: transport through the Golgi and synthesis of meiosis-activating sterols.
Mammalian lanosterol 14a-demethylase (CYP51) is a microsomal cytochrome P450 that demethylates lanosterol to FFMAS, an oocyte meiosis-activating sterol and late intermediate of cholesterol biosynthesis. 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. In the mouse, CYPS1 (53 kDa) resides in endoplasmic reticulum (ER) and Golgi during all phases of acrosome development, indicating an intracellular transport irom ERs through the Golgi to the acrosome. CYPS1 (50 kDa) also resides on acrosomal membranes of bull- and ram-ejaculated sperm.
CYP51; meiosis-activating sterol; Golgi apparatus
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