Effect of immunoglobulin class and affinity on the initiation of complement-dependent damage to liposomal model membranes sensitized with dinitrophenylated phospholipids.
Effect of immunoglobulin class and affinity on the initiation of complement-dependent damage to liposomal model membranes sensitized with dinitrophenylated phospholipids.
复制标题
免疫球蛋白类别和亲和力对二硝基苯化磷脂致敏的脂质体模型膜补体依赖性损伤启动的影响。
DOI：
10.1021/bi00744a034
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发表时间：
1973
期刊：
影响因子：
2.9
通讯作者：
S. Kinsky
中科院分区：
文献类型：
--
作者：
H. Six;K. Uemura;S. Kinsky
霍华德河Six，Kei-ichi Uemura和Stephen C. Kinsky* 摘要：本研究的主要目的是确定一些因素，这些因素决定了必须将多少抗原掺入脂质体模型膜中，以使它们对经典补体途径的免疫损伤敏感。脂质体被先前描述的磷脂衍生物二硝基苯磷脂酰乙醇胺（I）或新合成的类似物二硝基苯氨基己酰基磷脂酰乙醇胺（II）主动敏化。通过在豚鼠补体和各种高度纯化的兔IgG和IgM抗二硝基苯基抗体存在下释放捕获的葡萄糖标记物来测定免疫损伤，所述抗体的特征在于它们对e-Dnp-赖氨酸的结合常数（Af 0）：高亲和力抗体的K 0为1081。mol-1和低亲和力抗体的K 0为10 1。mol-1.从用恒定量II致敏的脂质体中释放葡萄糖所需的高亲和力IgG抗体少于从用相同量I致敏的脂质体中释放葡萄糖所需的高亲和力IgG抗体;相反，在掺入显著少于I的量的II时，发生由固定浓度的高亲和力IgG抗体引发的标记物损失。由于II在结构上与e-Dnp-赖氨酸（免疫原中的主要抗原决定簇）的关系比I更密切，因此这些结果支持了早期的建议，即抗体亲和力起着重要作用。直接测量通过用每种二硝基化合物增敏的脂质体对低和高亲和力IgG抗体的吸收。
Howard R. Six, Kei-ichi Uemura, and Stephen C. Kinsky* abstract: The principal goal of this investigation was to ex-amine some of the factors that determine how much antigen must be incorporated into liposomal model membranesto render them susceptible to immune damage by the classical complement pathway. Liposomes were actively sensitized either with a previously described phospholipid derivative, dinitrophenylphosphatidylethanolamine (I), or a new syn-thetic analog, dinitrophenylaminocaproylphosphatidylethanol-amine (II). Immune damage was assayed by the release of trapped glucose marker in the presence of guinea pig complement and various highly purified rabbit IgG and IgM antidinitrophenyl antibodies which were characterized by their association constant (Af0) for e-Dnp-lysine: high-affinity anti-bodies had a K0 of 1081. mol-1 and low-affinity antibodies had a K0 of 10 1. mol-1. Less high-affinity IgG antibody was re-quired for glucose release from liposomes sensitized with a constant amount of II than from liposomes sensitized with the same amount of I; conversely, loss of marker initiated by a fixed concentration of high-affinity IgG antibody occurred upon the incorporation of significantly smaller quantities of II than I. Because II is more closely related in structure to e-Dnp-lysine (the predominant antigenic determinant in the immunogen) than is I, these resultstherefore support an earlier suggestion that antibody affinity plays an important role. Di-rect measurement of low-and high-affinity IgG antibody ab-sorption by liposomessensitized with each of the dinitro-