ISOLATION OF THE CYCLOSPORINE-SENSITIVE T-CELL TRANSCRIPTION FACTOR NFATP

ISOLATION OF THE CYCLOSPORINE-SENSITIVE T-CELL TRANSCRIPTION FACTOR NFATP
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DOI:
10.1126/science.8235597
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发表时间:
1993-10-29
期刊:
影响因子:
56.9
通讯作者:
HOGAN, PG
HOGAN, PG
中科院分区:
综合性期刊1区
文献类型:
--
作者:
MCCAFFREY, PG;LUO, C;HOGAN, PG

文献摘要

被引文献

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活化T细胞核因子(NFAT)是一种转录因子,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FK 506的靶点。在这里,纯化的NFATp从鼠T细胞和分离的互补DNA克隆编码NFATp的报道。一种截短形式的NFATp,在细菌中表达为重组蛋白,特异性结合到鼠IL-2启动子的NFAT位点,并与重组c-Fos和c-Jun形成转录活性复合物。NFATp的分子克隆应该允许对T细胞转录因子进行详细分析,T细胞转录因子对免疫应答的启动至关重要。
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 c-Fos and c-Jun. Antisera to tryptic peptides of the purified protein or to the 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.