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This version published online on November 20, 2003
Endocrinology, doi:10.1210/en.2003-1332
A more recent version of this article appeared on March 1, 2004
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Submitted on October 6, 2003
Accepted on November 13, 2003

A functional cytochrome P450 lanosterol 14{alpha}-demethylase CYP51 enzyme in the acrosome: transport through the Golgi and synthesis of meiosis activating sterols

M. Cotman1, D. Jezek1, K. Fon Tacer1, R. Frangez1, and D. Rozman1

1 Laboratory for Genetics, Veterinary Faculty, University of Ljubljana, Slovenia, Institute of Histology and Embriology, School of Medicine, University of Zagreb, Croatia. Medical Center for Molecular Biology, Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Slovenia, Institute of Physiology, Pharmacology and Toxicology Veterinary Faculty, University of Ljubljana, Slovenia

Mammalian lanosterol 14{alpha}-demethylase (CYP51) is a microsomal cytochrome P450 (CYP) that demethylates lanosterol to FF-MAS, 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, where it synthesizes FF-MAS in the presence of the acrosomal form of NADPH-P450 reductase. In the mouse, CYP51 (53 kDa) resides in ER and Golgi during all phases of acrosome development, indicating an intracellular transport from ER through the Golgi to the acrosome. CYP51 (50 kDa) resides also on acrosomal membranes of bull and ram ejaculated sperm. 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. Glycosylated high molecular mass (HMM) CYP51-immunoreactive proteins in acrosomal membranes of bull and ram and in Golgi-enriched fractions of mouse liver indicate that mammalian CYP51s are subjected to post-translational modifications in the Golgi. In conclusion, CYP51 is the first CYP enzyme to be detected on acrosomal membranes. It exhibits a unique, cell-type specific intracellular transport that is in agreement with its cell-type specific physiological role - production of cholesterol in the liver and sterols with signaling properties in sperm. 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.




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