Putative sperm fusion protein IZUMO and the role of N-glycosylation
Putative sperm fusion protein IZUMO and the role of N-glycosylation
复制标题
DOI：
10.1016/j.bbrc.2008.10.073
复制
发表时间：
2008-12-19
影响因子：
3.1
通讯作者：
Okabe, Masaru
中科院分区：
文献类型：
--
作者：
Inoue, Naokazu;Ikawa, Masahito;Okabe, Masaru
IZUMO是一种被证明对与卵子融合至关重要的小鼠精子蛋白。它包含一个免疫球蛋白样结构域，其中有一个保守的糖基化位点。在本文中，我们在Izumol -/-背景下构建了表达未糖基化IZUMO （N204Q-IZUMO）的转基因小鼠系。N204Q-IZUMO的表达挽救了IZUMO受损小鼠的不育表型，表明糖基化对IZUMO的融合促进活性不是必需的。N204Q-IZUMO对睾丸产生的不良影响与野生型IZUMO相当，但当精子到达附睾尾部时，N204Q-IZUMO对精子的影响显著减少。这些数据表明，糖基化对IZUMO的功能不是必需的，但在保护其免受附睾尾断裂方面起作用。(C) 2008爱思唯尔公司版权所有。
IZUMO is the Mouse sperm protein proven to be essential for fusion with eggs. It contains one immunnoglobulin-like domain with a conserved glycosylation site within. In the present paper, we produced transgenic mouse lines expressing unglycosylated IZUMO (N204Q-IZUMO) in Izumol -/- background. The expression of N204Q-IZUMO rescued the infertile phenotype of IZUMO disrupted mice, indicating glycosylation is not essential for fusion-facilitating activity of IZUMO. The N204Q-IZUMO was produced ill testis in comparable amounts to wild-type IZUMO, but the amount of N204Q-IZUMO on sperm was significantly decreased by the time sperm reached the cauda epididymis. These data Suggest that glycosylation is not essential for the function of IZUMO, but has a role in protecting it from fragmentation in Cauda epididymis. (C) 2008 Elsevier Inc. All rights reserved.