Vitellogenin C-terminal fragments participate in fertilization as egg-coat binding partners of sperm trypsin-like proteases in the ascidian Halocynthia roretzi
Vitellogenin C-terminal fragments participate in fertilization as egg-coat binding partners of sperm trypsin-like proteases in the ascidian Halocynthia roretzi
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DOI：
10.1016/j.bbrc.2010.01.006
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发表时间：
2010-02-19
影响因子：
3.1
通讯作者：
Sawada, Hitoshi
中科院分区：
文献类型：
--
作者：
Akasaka, Mari;Harada, Yoshito;Sawada, Hitoshi
精子胰蛋白酶样蛋白酶在受精过程中起重要作用，但其具体功能尚不清楚。我们以前探讨了结合伴侣的精子胰蛋白酶样蛋白酶，HrProacrosin和HrSpermosin，在海鞘Halocynthia roretzi，我们分离出几个候选蛋白质的卵黄外套。我们发现其中一些蛋白质与卵黄蛋白原的C末端编码区（CT）和血管性血友病因子D型（vWF-D）结构域相同。我们还发现受精后卵黄膜上的CT消失。卵黄蛋白原是一种在卵黄发生过程中被酶促加工的大的脂质转运蛋白。尽管已知包括卵黄蛋白和卵黄脂磷蛋白的加工结构域作为卵黄营养蛋白起作用，但CT和vWF-D结构域的作用仍然难以捉摸。我们的研究结果表明，卵黄蛋白原的CT和vWF-D结构域被加工并附着在卵黄膜上，它们反过来又作为精子蛋白酶的结合伴侣参与受精。(C)2010年爱思唯尔公司All rights reserved.
Sperm trypsin-like proteases are known to play important roles in fertilization, but their detailed functions are still unknown. We previously explored the binding partners of sperm trypsin-like proteases, HrProacrosin and HrSpermosin, in the ascidian Halocynthia roretzi, and we isolated several candidate proteins on the vitelline coat. We found that some of these proteins are identical to the C-terminal coding region (CT) and von Willebrand factor type D (vWF-D) domain of vitellogenin. We also found that CT on the vitelline coat disappears after fertilization. Vitellogenin is a large lipid transfer protein that is enzymatically processed during vitellogenesis. Although the processed domains including phosvitin and lipovitellin are known to function as yolk nutrient proteins, the roles of the CT and vWF-D domain remain elusive. Our results showed that the CT and vWF-D domain of vitellogenin are processed and attached to the vitelline coat, which in turn participate in fertilization as the binding partners of sperm proteases. (C) 2010 Elsevier Inc. All rights reserved.