Li Z, Wu W, Kemp O, Stephen M, Manolios N
Department of Rheumatology, Royal North Shore Hospital, New South Wales, 2065, Australia.
Cell Immunol. 1998 Dec 15;190(2):101-11. doi: 10.1006/cimm.1998.1383.
Complementary DNAs encoding the T-cell antigen receptor (TCR)-alpha and mutant TCR-beta chains, lacking the interchain disulfide bond-related cysteine, were introduced into a TCR-alpha and -beta protein-deficient T-cell line. TCR-alpha and the mutant TCR-beta chains assembled with the CD3-epsilon, -gamma, -delta, and -zeta subunits and were efficiently transported to the cell surface; however, the hybrid TCR molecules exhibited a diminished response to T-cell activation by major histocompatibility complex-bound antigen, superantigen, and TCR cross-linking. These results suggest that the interchain disulfide bond between the TCR clonotypic chains is not required for TCR assembly and cell surface expression, but it plays an important role in maintaining the functional integrity of the TCR complex.
编码T细胞抗原受体（TCR）α链和缺乏链间二硫键相关半胱氨酸的突变型TCRβ链的互补DNA被导入到缺乏TCRα和β蛋白的T细胞系中。TCRα和突变型TCRβ链与CD3ε、γ、δ和ζ亚基组装在一起，并有效地转运到细胞表面；然而，杂合TCR分子对主要组织相容性复合体结合抗原、超抗原和TCR交联引起的T细胞活化反应减弱。这些结果表明，TCR克隆型链之间的链间二硫键对于TCR组装和细胞表面表达不是必需的，但它在维持TCR复合体的功能完整性方面起着重要作用。
