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DAF对结合于替代途径激活剂的补体酶的活性降低。与因子H的相似性。

Reduced activity of DAF on complement enzymes bound to alternative pathway activators. Similarity with Factor H.

作者信息

Pangburn M K

机构信息

Department of Biochemistry, University of Texas Health Science Center, Tyler 75710.

出版信息

Immunology. 1990 Dec;71(4):598-600.

PMID:1703989
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1384886/
Abstract

Attachment of C3b to activators of the alternative pathway of complement results in a decrease in regulatory activity expressed by Factor H. Decay-accelerating factor (DAF) and Factor H were found to exhibit quantitatively similar decreases in regulatory activity toward the C3 convertase (C3b,Bb) bound to activators, such as zymosan (Zym) and rabbit erythrocytes (ER), compared to non-activators, such as sheep (ES) and bovine (EB) erythrocytes. Purified DAF and Factor H, in 0.1% NP-40, were assayed by measuring the amount required to release 50% of the radiolabelled Bb in 10 min from C3b,Bb on Zym or cross-linked erythrocytes. The relative effectiveness (i.e. the restriction index, RI) of DAF for accelerating the decay of C3b,Bb on the various particles was: ES (1.0), ER (0.04) and Zym (0.03). The RI for Factor H was: ES (1.0), ER (0.04) and Zym (0.07). The rate of decay of C3b,Bb induced by DAF and Factor H showed similar restriction. The results suggest that the regulatory properties of DAF are reduced if the cells on which it resides become activators of the alternative pathway as a result of transformation, virus infection or surface alteration. These findings may explain reports of dysfunctional DAF on alternative pathway-activating cells.

摘要

补体替代途径激活剂上C3b的附着导致补体因子H所表达的调节活性降低。与非激活剂（如绵羊红细胞（ES）和牛红细胞（EB））相比，发现衰变加速因子（DAF）和因子H对结合在激活剂（如酵母聚糖（Zym）和兔红细胞（ER））上的C3转化酶（C3b，Bb）的调节活性呈现出数量上相似的降低。通过测量在10分钟内从Zym或交联红细胞上的C3b，Bb释放50%放射性标记的Bb所需的量，对0.1%NP - 40中的纯化DAF和因子H进行了测定。DAF加速C3b，Bb在各种颗粒上衰变的相对有效性（即限制指数，RI）为：ES（1.0），ER（0.04）和Zym（0.03）。因子H的RI为：ES（1.0），ER（0.04）和Zym（0.07）。DAF和因子H诱导的C3b，Bb衰变速率显示出相似的限制。结果表明，如果DAF所驻留的细胞由于转化、病毒感染或表面改变而成为替代途径的激活剂，其调节特性会降低。这些发现可能解释了关于替代途径激活细胞上功能失调的DAF的报道。

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本文引用的文献

1
Activation of the alternative complement pathway: recognition of surface structures on activators by bound C3b.替代补体途径的激活：结合的C3b识别激活物上的表面结构。
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2
Raji cell injury and subsequent lysis by the purified cytolytic alternative pathway of human complement.人补体的纯化溶细胞替代途径对拉吉细胞的损伤及随后的裂解。
Clin Immunol Immunopathol. 1980 Mar;15(3):384-96. doi: 10.1016/0090-1229(80)90050-1.
3
Affected erythrocytes of patients with paroxysmal nocturnal hemoglobinuria are deficient in the complement regulatory protein, decay accelerating factor.阵发性夜间血红蛋白尿患者的受累红细胞缺乏补体调节蛋白衰变加速因子。
Proc Natl Acad Sci U S A. 1983 Aug;80(16):5066-70. doi: 10.1073/pnas.80.16.5066.
4
Deficiency of an erythrocyte membrane protein with complement regulatory activity in paroxysmal nocturnal hemoglobinuria.阵发性夜间血红蛋白尿中具有补体调节活性的红细胞膜蛋白缺乏。
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5
Isolation of a human erythrocyte membrane glycoprotein with decay-accelerating activity for C3 convertases of the complement system.一种对补体系统C3转化酶具有衰变加速活性的人红细胞膜糖蛋白的分离。
J Immunol. 1982 Jul;129(1):184-9.
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Analysis of recognition in the alternative pathway of complement. Effect of polysaccharide size.
J Immunol. 1989 Apr 15;142(8):2766-70.
7
Production of mouse monoclonal antibodies that detect distinct neoantigenic epitopes on bound C3b and iC3b but not on the corresponding soluble fragments.产生能检测结合型C3b和iC3b上不同新抗原表位，但不能检测相应可溶性片段上的新抗原表位的小鼠单克隆抗体。
Mol Immunol. 1987 May;24(5):487-94. doi: 10.1016/0161-5890(87)90023-x.
8
Discrimination between activators and nonactivators of the alternative pathway of complement: regulation via a sialic acid/polyanion binding site on factor H.补体替代途径激活剂与非激活剂的鉴别：通过因子H上的唾液酸/多聚阴离子结合位点进行调节
Proc Natl Acad Sci U S A. 1990 May;87(10):3982-6. doi: 10.1073/pnas.87.10.3982.
9
Surface-associated heparin inhibits zymosan-induced activation of the human alternative complement pathway by augmenting the regulatory action of the control proteins on particle-bound C3b.表面相关肝素通过增强控制蛋白对颗粒结合C3b的调节作用，抑制酵母聚糖诱导的人替代补体途径的激活。
J Exp Med. 1979 Nov 1;150(5):1202-15. doi: 10.1084/jem.150.5.1202.
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J Exp Med. 1979 Sep 19;150(3):445-54. doi: 10.1084/jem.150.3.445.