Secretion of mouse ZP3, the sperm receptor, requires cleavage of its polypeptide at a consensus furin cleavage-site.
Secretion of mouse ZP3, the sperm receptor, requires cleavage of its polypeptide at a consensus furin cleavage-site.
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DOI：
10.1021/bi002275x
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发表时间：
2001-01
期刊：
影响因子：
2.9
通讯作者：
Zev Williams;P. M. Wassarman
中科院分区：
文献类型：
--
作者：
Zev Williams;P. M. Wassarman
小鼠卵细胞外衣，或透明带，由三种糖蛋白组成，称为mZP1-3。每个糖蛋白都有一个被Furin家族的原蛋白转换酶识别的共同序列。此前，据报道，mZP2和mZP3是在它们一致的Furin裂解位点上被切割的，这些裂解位点位于多肽的C-末端附近[Litscher，E.S.，Qi，H.和Wassarman，P.M.(1999年)生化38,12280-12287]。在这里，使用mZP3基因的定点突变和一种特定的呋喃类酶抑制剂显示，从转基因细胞分泌新生的mZP3依赖于mZP3在其共识的Furin裂解位点的裂解。分泌对切割的依赖性代表了Furin家族酶的一种新功能。
The mouse egg extracellular coat, or zona pellucida, consists of three glycoproteins, called mZP1-3. Each glycoprotein possesses a consensus sequence recognized by the furin family of proprotein convertases. Previously, it was reported that mZP2 and mZP3 are cleaved at their consensus furin cleavage-sites located near the C-terminus of the polypeptides [Litscher, E. S., Qi, H., and Wassarman, P. M. (1999) Biochemistry 38, 12280-12287]. Here, use of site-directed mutagenesis of the mZP3 gene and a specific inhibitor of furin-like enzymes revealed that secretion of nascent mZP3 from transfected cells is dependent on cleavage of mZP3 at its consensus furin cleavage-site. The dependence of secretion on cleavage represents a novel function for furin family enzymes.