Features that affect secretion and assembly of zona pellucida glycoproteins during mammalian oogenesis.

摘要: For sperm to fertilize eggs, they must bind and penetrate the zona pellucida (ZP) that surrounds plasma membrane of all mammalian eggs. The ZP first appears during oocyte growth increases in thickness as oocytes increase diameter. is an extracellular matrix composed long, crosslinked filaments. In mice, three glycoproteins, called mZP1-3, are synthesised secreted by growing assembled into a thick (-6.5 microm) coat over 2-3 week period. Recently, we identified several regions nascent glycoproteins affect their secretion incorporation (assembly) oocytes. Among these domain, consensus furin cleavage site (CFCS) C-terminal propeptide (CTP) with its transmembrane domain (TMD), external hydrophobic patch (EHP), charged (CP), conserved cysteine (Cys) residue, short cytoplasmic tail (CT). Particularly important approximately 260 amino acid region 8 Cys residues common variety proteins diverse functions found wide range multicellular eukaryotes. Our results show polymerisation module N-terminal half, including 4 residues, largely responsible for this role. Additionally, two sequences, one within (internal patch; IHP) another CTP apparently regulate glycoproteins. Collectively, our findings suggest general mechanism assembly based on coupling between proteolytic processing polymerisation.