A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins
A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins
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DOI：
10.1074/jbc.271.25.14717
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发表时间：
1996-06-21
影响因子：
4.8
通讯作者：
Quigley, JP
中科院分区：
文献类型：
--
作者：
Armstrong, PB;Swarnakar, S;Quigley, JP
多种无脊椎动物都具有具有唾液酸识别能力的血浆凝集素，这些凝集素中研究最好的一种是鲎毛素，它是蛋白质五聚蛋白家族的成员，在美洲鲎（美洲鲎）的血浆中发现。五聚蛋白、鲎林通过磷酸乙醇胺琼脂糖上的连续亲和层析纯化，分离五聚蛋白并将鲎林与血浆中其他唾液酸结合凝集素分离，然后使用胎球蛋白-琼脂糖，结合鲎林并将其与鲎毛 C 反应蛋白（血浆中最丰富的五聚蛋白）分离。鲎的血浆，通过磷酸乙醇胺琼脂糖传代而耗尽五聚蛋白或通过胎球蛋白琼脂糖传代而耗尽唾液酸结合凝集素的血浆缺乏溶血活性，纯化的鲎木素在浓度为3-5nM时发生溶血。鲎血浆和鲎C反应蛋白的其他唾液酸结合凝集素是非溶血性的。鲎木林的外源细胞溶解作用代表了血浆凝集素的一种新功能，也是鲎木林第一个有记录的功能。
A variety of invertebrates possess plasma lectins with sialic acid recognition capabilities, One of the best studied of these lectins is limulin, which is a member of the pentraxin family of proteins and is found in the plasma of the American horseshoe crab, Limulus polyphemus, We find that limulin is one of several sialic acid-binding lectins of limulus plasma and is present at a much lower abundance than Limulus C-reactive protein, the other plasma pentraxin, Limulin was purified by sequential affinity chromatography on phosphorylethanolamine agarose, which isolates the pentraxins and separates limulin from the other sialic acid-binding lectins of the plasma, followed by fetuin-Sepharose, which binds limulin and separates it from Limulus C-reactive protein, the most abundant pentraxin of the plasma, We show here that limulin is the mediator of the Ca+2-dependent hemolytic activity found in the plasma of Limulus, Plasma that was depleted in the pentraxins by passage over phosphorylethanolamine-agarose or was depleted in the sialic acid-binding lectins by passage over fetuin Sepharose lacked hemolytic activity, Purified limulin was hemolytic at concentrations of 3-5 nM. The other sialic acid-binding lectins of Limulus plasma and Limulus C-reactive protein were nonhemolytic. Foreign cell cytolysis by limulin represents a novel function for a plasma lectin and is the first documented function for limulin.