Ligand-binding properties of annexin from Caenorhabditis elegans (annexin XVI, Nex-1).
Ligand-binding properties of annexin from Caenorhabditis elegans (annexin XVI, Nex-1).
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秀丽隐杆线虫膜联蛋白（膜联蛋白 XVI、Nex-1）的配体结合特性。
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发表时间：
2000
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通讯作者：
I. Matsumoto
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作者：
A. Satoh;H. E. Miwa;K. Kojima;J. Hirabayashi;I. Matsumoto
膜联蛋白是结构上相关的蛋白质，以钙依赖的方式与磷脂结合。最近，我们发现膜联蛋白IV、V和VI也以钙依赖的方式与糖胺聚糖结合。膜联蛋白广泛分布于从低等到高等的真核生物中，线虫秀丽线虫被发现含有膜联蛋白同源物Nex-1。在这里，我们使用重组Nex-1来表征Nex-1的配体结合特性。NEX-1与含有磷脂酰丝氨酸的脂质体结合。用Biacore计算的表观K(D)为4.4 nm。与哺乳动物膜联蛋白相比，Nex-1磷脂结合的特异性相似，而K(D)值大一个数量级。通过亲和层析和固相分析研究了Nex-1糖胺聚糖结合的特异性。NEX-1与肝素、硫酸肝素和硫酸软骨素结合，但不与软骨素和化学N-或O-脱硫肝素结合。除磷脂外，硫酸乙酰肝素和/或软骨素(硫酸盐)可能是Nex-1的内源性配体，可能位于Perlecan上。
Annexins are structurally related proteins that bind phospholipids in a calcium-dependent manner. Recently, we showed that annexins IV, V, and VI also bind glycosaminoglycans in a calcium-dependent manner. Annexins are widely distributed from lower to higher eukaryotes, and the nematode Caenorhabditis elegans has been found to contain Nex-1, an annexin homologue. Here, we characterize the ligand-binding properties of Nex-1 using recombinant Nex-1. Nex-1 binds to liposomes containing phosphatidylserine. The apparent K(d) was calculated by Biacore to be 4.4 nM. Compared to mammalian annexins, the Nex-1 phospholipid-binding specificities were similar whereas the K(d) values were one order of magnitude larger. The Nex-1 glycosaminoglycan-binding specificities were investigated by affinity chromatography and solid-phase assays. Nex-1 binds to heparin, heparan sulfate, and chondroitin sulfate but not to chondroitin and chemically N- or O-desulfated heparin. Besides phospholipids, heparan sulfate and/or chondroitin (sulfate), probably on perlecan, could be endogenous ligands of Nex-1.