Veillette A, Bookman M A, Horak E M, Bolen J B
Laboratory of Tumor Virus Biology, National Cancer Institute, Bethesda, Maryland 20892.
Cell. 1988 Oct 21;55(2):301-8. doi: 10.1016/0092-8674(88)90053-0.
The CD4 and CD8 T cell antigens are thought to transduce an independent signal during the process of T cell activation. We report our evaluation of the possible involvement of the lymphocyte-specific tyrosine kinase p56lck in these transduction pathways. Our data demonstrate that p56lck is specifically modulated with either CD4 or CD8 following antibody-mediated cross-linking of these molecules and that a large fraction of the total cellular lck protein can be coimmunoprecipitated with these surface glycoproteins. These results suggest that p56lck is functionally and physically associated with CD4/CD8 in normal murine T lymphocytes and support the concept that an independent signal is transduced by the interaction of these surface molecules with major histocompatibility complex determinants.
CD4和CD8 T细胞抗原被认为在T细胞激活过程中传递独立信号。我们报告了对淋巴细胞特异性酪氨酸激酶p56lck可能参与这些转导途径的评估。我们的数据表明，在抗体介导的这些分子交联后，p56lck会随CD4或CD8特异性调节，并且细胞总lck蛋白的很大一部分可与这些表面糖蛋白共免疫沉淀。这些结果表明，p56lck在正常小鼠T淋巴细胞中与CD4/CD8在功能和物理上相关联，并支持这样的概念，即这些表面分子与主要组织相容性复合体决定簇的相互作用传递独立信号。
