Molecular Human Reproduction, Vol. 5, No. 6, 534-540,
June 1999
© 1999 European Society of Human Reproduction and Embryology
Characterization of human zona pellucida glycoproteins
1 Experimental Biology Unit, Medical Research Council, Tygerberg, Cape Town, 7505, 2 Department of Obstetrics and Gynaecology, Tygerberg Hospital and University of Stellenbosch, Tygerberg, 7505, South Africa and 3 Institute for Cell and Molecular Biology, Schering AG, Berlin, D-13353, Germany
The human egg may only be fertilized by one spermatozoon to prevent polyploidy. In most mammals, the primary block to polyspermy occurs at the zona pellucida (ZP). Little is known of the human ZP and the changes occurring following fertilization to prevent polyploidy. Using antibodies directed against synthetic peptides predicted from the human ZP2 and ZP3 cDNA, we identified ZP3 as a 53–60 kDa glycoprotein and ZP2 as a 90–110 kDa glycoprotein in prophase-I oocytes. Characterization of the ZP from metaphase II arrested eggs (inseminated–unfertilized and fertilized–uncleaved), shows no visible modification of ZP3, but demonstrates that ZP2 undergoes limited proteolysis in the amino terminal domain, to a 60–73 kDa species, denoted ZP2p, which remains linked to the proteolysed fragments by intramolecular disulphide bonds. A lack of ZP2 proteolytic activity in acrosomal supernatants is consistent with an oocyte origin for the protease. The ZP2-specific protease may be released during cortical granule exocytosis which occurs during meiotic maturation and following sperm–egg fusion as part of the block to polyspermy. Since mouse ZP2 acts as a secondary sperm receptor, it is possible that intact ZP2 binds a secondary egg binding protein, whereas cleaved ZP2 does not, suggesting a possible mechanism for the block to polyspermy.
glycosylation/human zona pellucida/proteolysis/ZP2/ZP3
4 Current address: Centre for Immunology, St Vincent's Hospital and University of New South Wales, Sydney, 2010, Australia
5 To whom correspondence should be addressed
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