TAILIEUCHUNG - Báo cáo Y học: Secretion of egg envelope protein ZPC after C-terminal proteolytic processing in quail granulosa cells

In avian species, an egg envelope homologous to the mammalian zona pellucida is called the perivitelline membrane. We have previously reported that one of its components, a glycoprotein homologous to mammalian ZPC, is synthesized in the granulosa cells of the quail ovary. In the present study, we investigated the proteolytic cleavage of the newly synthesized ZPC and the secretion of ZPC from the granulosa cells. Western blot analysis of the cell lysates demonstrated that the 43-kDa protein is the precursor of mature ZPC (proZPC), and is converted to the 35-kDa protein before secretion. . | Eur. J. Biochem. 269 2223-2231 2002 FEBS 2002 doi Secretion of egg envelope protein ZPC after C-terminal proteolytic processing in quail granulosa cells Tomohiro Sasanami1. Jianzhi Pan1. Yukio Doi2 Miki Hisada3 Tetsuva Kohsaka1. Masaru Torivama1 BBBBBBWBBBB and Makoto Mori1 1 Department of Applied Biological Chemistry Faculty of Agriculture Shizuoka University Japan department of Food Science Kyoto Women s University Higashiyama Kyoto Japan 3Suntory Institute for Bioorganic Research Wakayamadai Shimamoto-cho Mishima-gun Osaka Japan In avian species an egg envelope homologous to the mammalian zona pellucida is called the perivitelline membrane. We have previously reported that one of its components a glycoprotein homologous to mammalian ZPC is synthesized in the granulosa cells of the quail ovary. In the present study we investigated the proteolytic cleavage of the newly synthesized ZPCand the secretion of ZPCfrom the granulosa cells. Western blot analysis of the cell lysates demonstrated that the 43-kDa protein is the precursor of mature ZPC proZPC and is converted to di3 35DDa ptolein before secretion. The accumulation of proZPC in the presence of brefeldin A and conversion of proZPC to ZPC in the presence of monensin indicate the possibility that the proteolytic processing of ZPC occurs in the apparritLIS. An analysis of amino-acid sequence identified that the C terminus of mature ZPC proteéi is Phe360 and the N-lei -minal amino-acid sequence of the proZPC-derived fragment was determined as Asp363. These results suggest that newly synthesized ZPCis cleaved at the consensus furin cleavage site and the resulting two basic residues at the Cterminus are subsequently trimmed off to generate mature ZPC prior to secretion. Keywords zona pellucida ZPC granulosa cell quail post-translational modification. The plasma membrane of oocytes of all vertebrates is overlaid with extracellular matrix generally called the egg envelope .

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