Abaan Ogan D, Levenson Amy, Khan Osman, Furth Priscilla A, Uren Aykut, Toretsky Jeffrey A
Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC 20057, USA.
Oncogene. 2005 Apr 14;24(16):2715-22. doi: 10.1038/sj.onc.1208247.
Ewing's Sarcoma family tumors (ESFT) are characterized by a translocation t(11:22) forming an aberrant transcription factor EWS-FLI1. Protein tyrosine phosphatase L1 (PTPL1) was identified as a gene upregulated by EWS-FLI1 in transfected cells by microarray. Our results show that PTPL1 is a transcriptional target of EWS-FLI1 both by chromatin immunoprecipitation and promoter activation studies. We demonstrate that PTPL1 is highly expressed in ESFT cells and patient tumors compared with normal tissues, with a trend towards higher expression in metastatic versus primary tumors. Reduction of PTPL1 protein in ESFT cells correlated with a significant reduction in both monolayer and soft-agar cell growth. In addition, these PTPL1-reduced cells were more sensitive to etoposide-induced apoptosis than the controls. We therefore report a novel transcriptional activation of a phosphatase involved in the oncogenesis of ESFT. Increasing interest in specific phosphatase inhibitors would allow PTPL1 to be evaluated as a therapeutic target in ESFT.
尤因肉瘤家族性肿瘤(ESFT)的特征是发生11号与22号染色体易位,形成异常转录因子EWS-FLI1。通过微阵列分析,蛋白酪氨酸磷酸酶L1(PTPL1)被鉴定为在转染细胞中受EWS-FLI1上调的基因。我们的结果表明,通过染色质免疫沉淀和启动子激活研究,PTPL1是EWS-FLI1的转录靶点。我们证明,与正常组织相比,PTPL1在ESFT细胞和患者肿瘤中高表达,在转移性肿瘤与原发性肿瘤中呈现出更高表达的趋势。ESFT细胞中PTPL1蛋白的减少与单层细胞和软琼脂细胞生长的显著降低相关。此外,这些PTPL1减少的细胞比对照细胞对依托泊苷诱导的凋亡更敏感。因此,我们报道了一种参与ESFT肿瘤发生的磷酸酶的新型转录激活。对特异性磷酸酶抑制剂的兴趣日益增加,这将使PTPL1能够作为ESFT的治疗靶点进行评估。