Takayama H, Lee M H, Shirota-Someya Y
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
J Immunol. 1996 Nov 1;157(9):3943-8.
The Fas (CD95)-transmitted cell death signal has been reported to involve a protein tyrosine phosphatase, SHP-1. We analyzed the role of SHP-1 in the Fas-dependent as well as the perforin-dependent pathways of CTL-mediated killing using target cells prepared from SHP-1-deficient motheaten mice. Con A blast targets prepared from both a motheaten mouse and a phenotype-normal littermate were equally sensitive to the cytolysis and DNA fragmentation induced by both perforin-deficient Fas-dependent CTL and Fas ligand-deficient perforin-positive CTL. Fas-induced DNA degradation detected by the terminal deoxynucleotide transferase reaction was also observed in the killing of motheaten thymocytes by a Fas-based CTL as well as by anti-Fas mAb. These data cast doubt on the involvement of SHP-1 in Fas-induced lymphoid cell death.
据报道，Fas（CD95）传递的细胞死亡信号涉及一种蛋白酪氨酸磷酸酶SHP-1。我们使用从SHP-1缺陷的肌无力小鼠制备的靶细胞，分析了SHP-1在CTL介导杀伤的Fas依赖性以及穿孔素依赖性途径中的作用。从肌无力小鼠和表型正常的同窝仔鼠制备的伴刀豆球蛋白A刺激的靶细胞，对穿孔素缺陷的Fas依赖性CTL和Fas配体缺陷的穿孔素阳性CTL诱导的细胞溶解和DNA片段化同样敏感。在用基于Fas的CTL以及抗Fas单克隆抗体杀伤肌无力胸腺细胞时，也观察到了通过末端脱氧核苷酸转移酶反应检测到的Fas诱导的DNA降解。这些数据使人怀疑SHP-1是否参与Fas诱导的淋巴细胞死亡。
