McCaffrey P G, Luo C, Kerppola T K, Jain J, Badalian T M, Ho A M, Burgeon E, Lane W S, Lambert J N, Curran T
Division of Tumor Virology, Dana-Farber Cancer Institute, Boston, MA.
Science. 1993 Oct 29;262(5134):750-4. doi: 10.1126/science.8235597.
Nuclear factor of activated T cells (NFAT) is a transcription factor that regulates expression of the cytokine interleukin-2 (IL-2) in activated T cells. The DNA-binding specificity of NFAT is conferred by NFATp, a phosphoprotein that is a target for the immunosuppressive compounds cyclosporin A and FK506. Here, the purification of NFATp from murine T cells and the isolation of a complementary DNA clone encoding NFATp are reported. A truncated form of NFATp, expressed as a recombinant protein in bacteria, binds specifically to the NFAT site of the murine IL-2 promoter and forms a transcriptionally active complex with recombinant protein fragment react with T cell NFATp. The molecular cloning of NFATp should allow detailed analysis of a T cell transcription factor that is central to initiation of the immune response.
活化T细胞核因子（NFAT）是一种转录因子，可调节活化T细胞中细胞因子白细胞介素-2（IL-2）的表达。NFAT的DNA结合特异性由NFATp赋予，NFATp是一种磷蛋白，是免疫抑制化合物环孢菌素A和FK506的作用靶点。本文报道了从小鼠T细胞中纯化NFATp以及分离编码NFATp的互补DNA克隆。以截短形式在细菌中表达的重组蛋白NFATp能特异性结合小鼠IL-2启动子的NFAT位点，并与重组蛋白片段形成转录活性复合物，该重组蛋白片段可与T细胞NFATp发生反应。NFATp的分子克隆将有助于对免疫反应起始过程中起核心作用的T细胞转录因子进行详细分析。
