Friedrich B, Cantrell D A, Gullberg M
Unit of Applied Cell and Molecular Biology, University of Umeå, Sweden.
Eur J Immunol. 1989 Jan;19(1):17-23. doi: 10.1002/eji.1830190104.
Phosphorylation of protein kinase C (PKC) substrates in T lymphocytes was analyzed after stimulation with specific pairs of anti-CD2 monoclonal antibodies (mAb) or an anti-CD3 mAb. The results show that the appropriate stimulation of both CD2 or CD3 antigens results in phosphorylation of a 80-kDa putative PKC substrate and that this phosphorylation event is sensitive to a PKC inhibitor, sphinganine. CD2- and CD3-dependent phosphorylation was found to be strongly dependent on an extensive cross-linking of surface antigens. The biological importance of cross-linking of CD2 and CD3 was also evident for other biological responses such as interleukin 2 production and induction of an autocrine growth response. Finally, we also present evidence for interaction between the CD2 and CD3 signal transducing pathways.
在用特定的抗CD2单克隆抗体（mAb）对或抗CD3 mAb刺激后，分析了T淋巴细胞中蛋白激酶C（PKC）底物的磷酸化情况。结果表明，对CD2或CD3抗原的适当刺激会导致一种80 kDa推定PKC底物的磷酸化，并且这种磷酸化事件对PKC抑制剂鞘氨醇敏感。发现CD2和CD3依赖性磷酸化强烈依赖于表面抗原的广泛交联。CD2和CD3交联的生物学重要性对于其他生物学反应如白细胞介素2的产生和自分泌生长反应的诱导也很明显。最后，我们还提供了CD2和CD3信号转导途径之间相互作用的证据。
