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Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy.

Authors: Burkart, AD  Xiong, B  Baibakov, B  Jimenez-Movilla, M  Dean, J 
Citation: Burkart AD, etal., J Cell Biol. 2012 Apr 2;197(1):37-44. doi: 10.1083/jcb.201112094.
Pubmed: (View Article at PubMed) PMID:22472438
DOI: Full-text: DOI:10.1083/jcb.201112094

The mouse zona pellucida is composed of three glycoproteins (ZP1, ZP2, and ZP3), of which ZP2 is proteolytically cleaved after gamete fusion to prevent polyspermy. This cleavage is associated with exocytosis of cortical granules that are peripherally located subcellular organelles unique to ovulated eggs. Based on the cleavage site of ZP2, ovastacin was selected as a candidate protease. Encoded by the single-copy Astl gene, ovastacin is an oocyte-specific member of the astacin family of metalloendoproteases. Using specific antiserum, ovastacin was detected in cortical granules before, but not after, fertilization. Recombinant ovastacin cleaved ZP2 in native zonae pellucidae, documenting that ZP2 was a direct substrate of this metalloendoprotease. Female mice lacking ovastacin did not cleave ZP2 after fertilization, and mouse sperm bound as well to Astl-null two-cell embryos as they did to normal eggs. Ovastacin is a pioneer component of mouse cortical granules and plays a definitive role in the postfertilization block to sperm binding that ensures monospermic fertilization and successful development.

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CRRD Object Information
CRRD ID: 8554097
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.