Multiple forms of complement C3 in trout that differ in binding to complement activators
Multiple forms of complement C3 in trout that differ in binding to complement activators
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DOI：
10.1073/pnas.93.16.8546
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发表时间：
1996-08-06
影响因子：
11.1
通讯作者：
Lambris, JD
中科院分区：
文献类型：
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作者：
Sunyer, JO;Zarkadis, IK;Lambris, JD
到目前为止，在所有其他被分析的物种中，补体成分C3的功能活跃项作为单个基因的产物存在。我们现在已经在鲑鱼中鉴定了三种功能C3蛋白(C3-1、C3-3和C3-4)，它们是至少两个不同的C3基因的产物。这三种蛋白质都由α-链和β-链组成，并且在α-链中含有硫酯键。然而，它们在凝胶迁移率、糖基化、与单特异性C3抗体的反应性以及与不同表面(酵母多糖、大肠杆菌、红细胞)结合的相对能力上存在差异。氨基酸序列比较表明，C3-3与C3-4的氨基酸序列相似性为87/91%，而C3-3和C3-4与C3-1的氨基酸序列相似性分别为51.5/65.5%和60/73%。因此，鲑鱼拥有多种形式的功能性C3，这些C3代表几个不同基因的产物，并且它们与各种补体激活剂共价结合的能力不同。
In all other species analyzed to date, the functionally active Term of complement component C3 exists as the product of a single gene. We have now identified and characterized three functional C3 proteins (C3-1, C3-3, and C3-4) in trout that are the products of at least two distinct C3 genes. All three proteins are composed of an alpha- and a beta-chain and contain a thioester bond in the alpha-chain. However, they differ in their electrophoretic mobility, glycosylation, reactivity with monospecific C3 antibodies, and relative ability to bind to various surfaces (zymosan, Escherichia coli, erythrocytes). A comparison of the partial amino acid sequences of the three proteins showed that the amino acid sequence identified/similarity of C3-3 to C3-4 is 87/91%, while that of C3-3 and C3-4 to C3-1 is 51.5/65.5% and 60/73% respectively. Thus, trout possess multiple forms of functional C3 that represent the products of several distinct genes and differ in their ability to bind covalently to various complement activators.