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- W8361054 abstract "During animal and human fertilization, the fertilizing spermatozoon creates and passes through a fertilization slit in the vitelline coat (VC) of the oocyte. It has been hypothesized that the penetration of the mammalian VC, the zona pellucida (ZP), is aided by a proteolytic enzyme capable of locally degrading ZP proteins. This putative “zona lysin” is predicted to reside within the sperm head acrosome and be released or exposed by ZP-induced acrosomal exocytosis. Evidence has been accumulating in favor of the 26S proteasome, the ubiquitin-dependent multi-subunit protease acting as the putative vitelline coat/zona lysin in humans and animals. To confirm this hypothesis, three criteria must be met: (1) the sperm receptor on the ZP must be ubiquitinated, (2) proteasomes must be present, exposed, and enzymatically active in the sperm acrosome, and (3) sperm proteasomes must be able to degrade the sperm receptor on the egg coat/ZP during fertilization. This review discusses recent data from a number of mammalian and nonmammalian models addressing these predictions. These data shed light on the mechanisms controlling sperm interactions with VC and on the evolutionary conservation of the proteasome-assisted fertilization mechanisms." @default.
- W8361054 created "2016-06-24" @default.
- W8361054 creator A5019526383 @default.
- W8361054 creator A5034305224 @default.
- W8361054 date "2014-01-01" @default.
- W8361054 modified "2023-09-25" @default.
- W8361054 title "Sperm Proteasome as a Putative Egg Coat Lysin in Mammals" @default.
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- W8361054 doi "https://doi.org/10.1007/978-4-431-54589-7_37" @default.
- W8361054 hasPublicationYear "2014" @default.
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