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目的:检测己糖激酶-Ⅱ基因在直肠癌组织中表达,探讨其与患者预后的关系。方法:通过逆转录聚合酶链反应(RT-PCR)、蛋白质印迹方法、免疫组织化学方法了解己糖激酶-Ⅱ在直肠癌100例组织中表达,探讨与肿瘤病理因素关系。结果:RT-PCR和蛋白质印迹法结果显示直肠癌组织阳性表达己糖激酶-Ⅱ在RNA水平显著高于正常组织阳性表达。直肠癌组织中己糖激酶-Ⅱ表达阳性率显著高于对照组(P<0.01)。肿瘤大小、分化程度、合并肿瘤分期与己糖激酶-Ⅱ的表达呈正相关(P值分别为P=0.001,P=0.000,P=0.019),而淋巴转移与否与己糖激酶-Ⅱ的表达无相关性(P=0.815)。结论:直肠癌组织中HK-Ⅱ呈高表达,HK-Ⅱ抑制剂能抑制肿瘤糖酵解从而抑制肿瘤生长、增殖,促进肿瘤凋亡,为肿瘤治疗提供契机。  相似文献   
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Research has shown that cancer cells exhibit multiple deregulated pathways, involving proliferation, migration and cell death. Heat-shock-proteins have evolved as “central regulators” and are implicated in the modulation of these pathways and in organelle-specific signaling. In this instance, heat-shock-proteins (Hsps) assist cancer cells in the maturation of proteins. Hsp90 is of particular interest because its enzymatic ATPase activity is elevated in malignant cells as compared to non-neoplastic counterparts. Consistent with its high-activity in cancer cells, Hsp90 stabilizes a considerable number of proteins being instrumental in carcinogenesis and the maintenance and growth of highly malignant cancers. Among its distribution Hsp90 is also localized within mitochondria of neoplastic cells of various origin, interacting with another chaperone, TRAP1 (Tumor necrosis factor type 1 receptor-associated protein or Heat-shock-protein 75) to antagonize the cell death promoting properties of the matrix protein, Cyclophilin-D. Several preclinical studies, including in vivo studies in both orthotopic and genetic animal models, have confirmed that targeting mitochondrial Hsp90 may be a novel efficient treatment method for highly recalcitrant tumors. This review summarizes the most recent findings of mitochondrial Hsp90 signaling and its potential implications for cancer therapy.  相似文献   
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