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1 May 2003 Carboxy-Terminal Proteolytic Processing at a Consensus Furin Cleavage Site Is a Prerequisite Event for Quail ZPC Secretion
Tomohiro Sasanami, Masaru Toriyama, Makoto Mori
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Abstract

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 granulosa cells is cleaved at a consensus furin cleavage site to generate mature ZPC prior to secretion. In the present study, we examined the effect of the proteolytic cleavage of proZPC on ZPC secretion by using a specific inhibitor of furin endoprotease and site-directed mutagenesis of the furin cleavage site. Western blot analysis demonstrated that the furin inhibitor efficiently blocked both the proteolytic cleavage of proZPC and the subsequent ZPC secretion. A site-directed mutant that possessed a mutated sequence for furin cleavage was not secreted from the cells. The immunocytochemical observations indicated that proZPC produced in the presence of a furin inhibitor or those produced by the site-directed mutant of the furin cleavage site had accumulated in the endoplasmic reticulum. These results indicate that proZPC is proteolytically cleaved at the consensus furin cleavage site with furin-like protease, and the failure of this cleavage results in its accumulation in the endoplasmic reticulum. Therefore, the C-terminal proteolytic processing of proZPC at the consensus furin cleavage site is a prerequisite event for quail ZPC secretion.

Tomohiro Sasanami, Masaru Toriyama, and Makoto Mori "Carboxy-Terminal Proteolytic Processing at a Consensus Furin Cleavage Site Is a Prerequisite Event for Quail ZPC Secretion," Biology of Reproduction 68(5), 1613-1619, (1 May 2003). https://doi.org/10.1095/biolreprod.102.011841
Received: 2 October 2002; Accepted: 1 November 2002; Published: 1 May 2003
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