Structure and function of C8 in the membrane attack sequence of complement.
Structure and function of C8 in the membrane attack sequence of complement.
复制标题
补体膜攻击序列中 C8 的结构和功能。
DOI：
10.1007/978-3-642-73911-8_3
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发表时间：
1989
影响因子：
--
通讯作者：
Sodetz,JM
中科院分区：
文献类型：
--
作者：
Sodetz,JM
Complement-mediated cell lysis occurs as a result of interactions between complement proteins C5b, C6, C7, C8, and C9 to produce the membrane attack complex C5b-9 (Müller-Eberhard1986): $$ C5b\;\xrightarrow{{C6}}\;C5b - 6\;\xrightarrow{{C7}}\;C5b - 7\xrightarrow{{C8}}\;C5b - 8\;\xrightarrow{{nC9}}\;C5b - 9 $$ Assembly of C5b-9 begins with proteolytic conversion of C5 to C5b by the C5 convertases formed as a consequence of complement activation. Development of a transient binding site for C6 leads to formation of a stable C5b-6 dimer. Subsequent binding of C7 and formation of C5b-7 coincides with the expression of a high-affinity lipid-binding site that mediates a strong but noncovalent interaction between the nascent complex and target membranes. Binding of C8 yields the tetramolecular C5b-8 complex. Although capable of slowly lysing erythrocytes and some nucleated cells, C5b-8 functions primarily as a receptor for C9 and thereby mediates formation of the more lytically effective C5b-9 complex. The number of C9 molecules per complex differs depending on C9 input and conditions of formation. The ultrastructure varies accordingly from what are functional lesions with one or a few C9s to highly organized porelike structures formed by polymerization of as many as 16 C9s per C5b-8. Facts and controversies about the function of C9 and the stoichiometry, structure, and mechanism of action of C5b-9 are summarized in other reports (Podack1986;Müller-Eberhard1986;Esser1987;Stanley, this volume).
Complement-mediated cell lysis occurs as a result of interactions between complement proteins C5b, C6, C7, C8, and C9 to produce the membrane attack complex C5b-9 (Müller-Eberhard1986): $$ C5b\;\xrightarrow{{C6}}\;C5b - 6\;\xrightarrow{{C7}}\;C5b - 7\xrightarrow{{C8}}\;C5b - 8\;\xrightarrow{{nC9}}\;C5b - 9 $$ Assembly of C5b-9 begins with proteolytic conversion of C5 to C5b by the C5 convertases formed as a consequence of complement activation. Development of a transient binding site for C6 leads to formation of a stable C5b-6 dimer. Subsequent binding of C7 and formation of C5b-7 coincides with the expression of a high-affinity lipid-binding site that mediates a strong but noncovalent interaction between the nascent complex and target membranes. Binding of C8 yields the tetramolecular C5b-8 complex. Although capable of slowly lysing erythrocytes and some nucleated cells, C5b-8 functions primarily as a receptor for C9 and thereby mediates formation of the more lytically effective C5b-9 complex. The number of C9 molecules per complex differs depending on C9 input and conditions of formation. The ultrastructure varies accordingly from what are functional lesions with one or a few C9s to highly organized porelike structures formed by polymerization of as many as 16 C9s per C5b-8. Facts and controversies about the function of C9 and the stoichiometry, structure, and mechanism of action of C5b-9 are summarized in other reports (Podack1986;Müller-Eberhard1986;Esser1987;Stanley, this volume).
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人类补体第八个组成部分中亚基的功能：选择性去除伽玛链表明它在细胞溶解中没有直接作用。
影响因子：
2.9
作者：
Brickner,A;Sodetz,JM
通讯作者：
Sodetz,JM
在细胞溶解过程中将末端补体蛋白直接插入细胞膜双层的证据。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Steckel,EW;Welbaum,BE;Sodetz,JM
通讯作者：
Sodetz,JM
人补体蛋白 C8 β 亚基的互补 DNA 和衍生氨基酸序列：鉴定与 α 亚基和 C9 的密切结构和祖先关系。
影响因子：
2.9
作者：
Howard,OM;Rao,AG;Sodetz,JM
通讯作者：
Sodetz,JM
有证据表明 C5b 识别并介导 C8 掺入补体溶细胞复合物。
DOI：
--
发表时间：
1987
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
--
作者：
Stewart,JL;Kolb,WP;Sodetz,JM
通讯作者：
Sodetz,JM
DOI：
10.1016/s0021-9258(17)39778-8
发表时间：
1984-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
E. Podack
通讯作者：
E. Podack