The mouse tectorins - Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system
The mouse tectorins - Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system
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DOI：
10.1074/jbc.272.13.8791
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发表时间：
1997-03-28
影响因子：
4.8
通讯作者：
Richardson, GP
中科院分区：
文献类型：
--
作者：
Legan, PK;Rau, A;Richardson, GP
的cDNA和衍生的氨基酸序列的两个主要的非胶原蛋白的小鼠盖膜，α-和β-tectorin，提出。α-tectorin的cDNA预测具有33个潜在的N-糖基化位点的239，034 Da的蛋白质，而β-tectorin的cDNA预测具有4个共有N-糖基化位点的36，074 Da的较小蛋白质。Southern和北方印迹分析表明α和β-tectorin是仅在内耳中表达的单拷贝基因，并且原位杂交显示它们由机械感觉上皮中和周围的细胞表达。这两个序列终止于疏水性COOH末端，之前是潜在的内切蛋白酶切割位点，表明tectorins合成为糖基磷脂酰肌醇连接的膜结合前体，通过脂质靶向内耳上皮细胞的顶端表面，并通过蛋白水解释放到细胞外室中。小鼠β-tectorin序列包含一个单一的透明质酸结构域，而α-tectorin由三个不同的模块组成：一个NH 2-末端区域类似于部分的巢蛋白G1结构域，一个大的中央段与三个完整的和两个部分的血管性血友病因子D型重复序列，和羧基末端区域，像β-tectorin，包含一个单一的透明质酸结构域。含有血管性血友病因子D型重复序列的α-tectorin的中心高分子量区域与zonadhesin（一种结合至透明质膜的精子膜蛋白）具有同源性。这些结果表明，这两个主要的非胶原蛋白的覆膜是类似的精卵粘附系统的组件，并因此可能以相同的方式相互作用。
The cDNA and derived amino acid sequences for the two major non-collagenous proteins of the mouse tectorial membrane, alpha- and beta-tectorin, are presented. The cDNA for alpha-tectorin predicts a protein of 239,034 Da with 33 potential N-glycosylation sites, and that of beta-tectorin a smaller protein of 36,074 Da with 4 consensus N-glycosylation sites. Southern and Northern blot analysis indicate alpha and beta-tectorin are single copy genes only expressed in the inner ear, and in situ hybridization shows they are expressed by cells both in and surrounding the mechanosensory epithelia. Both sequences terminate with a hydrophobic COOH terminus preceded by a potential endoproteinase cleavage site suggesting the tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane bound precursors, targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment. The mouse beta-tectorin sequence contains a single zona pellucida domain, whereas alpha-tectorin is composed of three distinct modules: an NH2-terminal region similar to part of the entactin G1 domain, a large central segment with three full and two partial von Willebrand factor type D repeats, and a carboxyl-terminal region which, like beta-tectorin, contains a single zona pellucida domain. The central, high molecular mass region of alpha-tectorin containing the von Willebrand factor type D repeats has homology with zonadhesin, a sperm membrane protein that binds to the zona pellucida. These results indicate the two major non-collagenous proteins of the tectorial membrane are similar to components of the sperm-egg adhesion system, and, as such may interact in the same manner.