A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57
A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57
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DOI：
10.1016/j.devcel.2006.03.011
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发表时间：
2006-06-01
影响因子：
11.8
通讯作者：
Primakoff, Paul
中科院分区：
文献类型：
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作者：
Ellerman, Diego A.;Myles, Diana G.;Primakoff, Paul
在哺乳动物中，精卵相互作用是基于配子特有的或也存在于体细胞中的分子事件。在配子融合中，不知道哪些特征是配子特异性的，哪些特征与其他系统共享。巯基-二硫键交换介导的构象变化参与了某些病毒膜融合蛋白的激活。在这里，我们想知道这种机制是否在精卵融合中也起作用。蛋白质二硫键异构酶（PDI）活性的不同抑制剂能够抑制精卵融合在体外。卵母细胞的预处理没有影响，精子的预处理降低了它们的融合能力。在精子头部检测到PDI家族的一些成员，并且使用特异性抗体和底物表明氧化还原酶ERp 57在配子融合中具有作用。结果支持的想法，巯基二硫键交换是一种机制，可能会在配子融合产生融合活性蛋白的构象变化。
In mammals, sperm-egg interaction is based on molecular events either unique to gametes or also present in somatic cells. In gamete fusion, it is unknown which features are gamete specific and which are shared with other systems. Conformational changes mediated by thiol-disulfide exchange are involved in the activation of some virus membrane fusion proteins. Here we asked whether that mechanism is also operative in sperm-egg fusion. Different inhibitors of protein disulfide isomerase (PDI) activity were able to inhibit sperm-egg fusion in vitro. While pretreatmentof oocytes had no effect, pretreatment of sperm reduced their fusion ability. Some members of the PDI family were detected on the sperm head, and use of specific antibodies and substrates suggested that the oxidoreductase ERp57 has a role in gamete fusion. The results support the idea that thiol-disulfide exchange is a mechanism that may act in gametefusion to produce conformational changes in fusion-active proteins.