Comparison of T3-associated 49- and 43-kilodalton cell surface molecules on individual human T-cell clones: evidence for peptide variability in T-cell receptor structures.
Comparison of T3-associated 49- and 43-kilodalton cell surface molecules on individual human T-cell clones: evidence for peptide variability in T-cell receptor structures.
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人类 T 细胞克隆个体上 T3 相关 49 道尔顿和 43 道尔顿细胞表面分子的比较：T 细胞受体结构中肽变异性的证据。
DOI：
10.1073/pnas.80.13.4104
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发表时间：
1983
影响因子：
11.1
通讯作者：
Schlossman,SF
中科院分区：
文献类型：
--
作者：
Reinherz,EL;Meuer,SC;Fitzgerald,KA;Hussey,RE;Hodgdon,JC;Acuto,O;Schlossman,SF
抗Ti1a和抗tI1b两种单抗可定义CT8III的克隆性独特的表面受体，CT8III是一种人细胞溶解T淋巴细胞，专用于I类主要组织相容基因产物。在本报告中，这种表面结构被表征，并与所有成熟人类T淋巴细胞上存在的20kDa(KDa)T3糖蛋白有关。结果表明，抗克隆型抗体与CT8III独有表达的49 kDa和43 kDa亚基的二硫键连接的异源二聚体上的表位发生反应。这种结构与细胞膜中的T3有关。在另外8个克隆上也检测到了类似的与T3相关的49/43 kDa分子，尽管这些克隆不表达抗Ti1a或抗tI1b所定义的决定簇。通过探测来自同一供体的不同特异性的克隆与抗T3抗体，有可能比较这些与T3相关的异源二聚体。生化分析表明，经胰凝乳杆菌酶或葡萄球菌蛋白酶V8消化后，49/43 kDa结构具有等电点可变性，而T3分子本身不具有等电点可变性和独特的肽谱。这些发现支持49/43 kDa异源二聚体含有T细胞抗原受体结构的可变区的观点。
Two monoclonal antibodies, anti-Ti1A and anti-Ti1B, were shown to define the clonally unique surface receptor on CT8III, a human cytolytic T lymphocyte specific for a class I major histocompatibility gene product. In the present report, this surface structure was characterized and related to the 20-kilodalton (kDa) T3 glycoprotein present on all mature human T lymphocytes. The results demonstrated that the anti-clonotypic antibodies react with an epitope on a disulfide-linked heterodimer of 49- and 43-kDa subunits exclusively expressed by CT8III. This structure is associated with T3 in the cell membrane. Similar T3-associated 49/43-kDa molecules were detected on eight additional clones, although these did not express the determinant defined by anti-Ti1A or anti-Ti1B. By probing clones of differing specificities derived from the same donor with anti-T3, it was possible to compare these T3-associated heterodimers. Biochemical analysis indicated that the 49/43-kDa structures, but not the T3 molecules themselves, had isoelectric point variability and unique peptide maps after digestion with chymotrypsin or staphylococcal protease V8. These findings support the idea that the 49/43-kDa heterodimer contains the variable region of the T cell's antigen receptor structure.