Characterization of human zona pellucida glycoproteins

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dc.contributor.authorBauskin A.R.
dc.contributor.authorFranken D.R.
dc.contributor.authorEberspaecher U.
dc.contributor.authorDonner P.
dc.date.accessioned2011-05-15T16:17:24Z
dc.date.available2011-05-15T16:17:24Z
dc.date.issued1999
dc.description.abstractThe 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 ZP2(p), 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.
dc.description.versionArticle
dc.identifier.citationMolecular Human Reproduction
dc.identifier.citation5
dc.identifier.citation6
dc.identifier.issn13609947
dc.identifier.other10.1093/molehr/5.6.534
dc.identifier.urihttp://hdl.handle.net/10019.1/14204
dc.subjectbinding protein
dc.subjectglycoprotein
dc.subjectacrosome
dc.subjectarticle
dc.subjectcontrolled study
dc.subjectfemale
dc.subjectfertilization
dc.subjecthuman
dc.subjecthuman cell
dc.subjectpolyploidy
dc.subjectpolyspermy
dc.subjectpriority journal
dc.subjectprotein degradation
dc.subjectprotein determination
dc.subjectprotein glycosylation
dc.subjectspermatozoon
dc.subjectzona pellucida
dc.subjectAcrosome Reaction
dc.subjectAmino Acid Sequence
dc.subjectEgg Proteins
dc.subjectExocytosis
dc.subjectFemale
dc.subjectFertilization in Vitro
dc.subjectGlycosylation
dc.subjectHumans
dc.subjectMale
dc.subjectMembrane Glycoproteins
dc.subjectMetaphase
dc.subjectMolecular Sequence Data
dc.subjectOocytes
dc.subjectProphase
dc.subjectReceptors, Cell Surface
dc.subjectSperm-Ovum Interactions
dc.subjectZona Pellucida
dc.titleCharacterization of human zona pellucida glycoproteins
dc.typeArticle
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