Asparagine-linked oligosaccharide-independent secretion of egg envelope glycoprotein ZPC of the Japanese quail (Coturnix japonica).

In avian species, a glycoprotein homologous to mammalian ZPC is synthesized in the granulosa cells of developing follicles. We have previously reported that the newly synthesized ZPC (proZPC) in the granulosa cells is cleaved at the consensus furin cleavage site to generate mature ZPC prior to secretion. In the present study, we examined the role of asparagine (N)-linked oligosaccharides in the proteolytic processing of proZPC and the subsequent secretion of ZPC by using site-directed mutagenesis of the consensus sequence for N-glycosylation, and tunicamycin, an inhibitor for N-glycosylation of glycoprotein. Western blot analysis demonstrated that tunicamycin did not block either proteolytic cleavage of proZPC or the subsequent ZPC secretion. Moreover, a site-directed mutant that possesses a mutated sequence for N-glycosylation was efficiently secreted from the cells. These results indicate that proteolytic cleavage of proZPC, and the subsequent ZPC secretion occur in the absence of N-linked oligosaccharides. Therefore, the addition of N-glycans to ZPC polypeptide is not required for quail ZPC secretion.