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目的 研究诱导K5 6 2细胞分化和热应激过程中 ,JWA表达的特点 ,探讨JWA与热应激蛋白 (Hsp70 )表达的关系以及参与诱导分化和热应激可能的机制。方法 分别建立K5 6 2细胞诱导分化和热应激模型 ,采用Western blot方法检测JWA、Hsp70、热休克转录因子 (HSF1)、HSF2蛋白表达水平。结果 (1)佛波酯 (TPA ,10 0ng ml)、氯化高铁血红素 (hemin ,3× 10 - 5mol L)、阿糖胞苷 (Ara C ,80ng ml)、阿霉素 (adriamycin ,4× 10 - 8mol L)、全反式维甲酸 (ATRA ,1× 10 - 6 mol L)、三氧化二砷 (As2 O3,1× 10 - 6 mol L)分别诱导K5 6 2细胞 4 8h ,JWA、Hsp70蛋白表达水平均明显增加 ;HSF2在hemin、Ara C、ad riamycin诱导下表达增加 ;(2 )在 4 2℃不同时间 (10、2 0、30、4 5、6 0、90min)和不同温度 (39℃、4 2℃、4 5℃ )处理下 ,Hsp70表达水平的变化与JWA蛋白表达水平的变化趋势基本相似 ,且HSF1在热应激早期表达。结论 在诱导分化、热应激过程中 ,JWA与Hsp70蛋白表达水平均明显上调 ,且变化趋势有一定的相似 ,但所涉及的细胞内信号转导通路可能不是惟一的。JWA表达与HSF1或HSF2似乎没有直接的特征性联系。
Objective To study the characteristics of JWA expression in the process of inducing K562 cell differentiation and heat stress, and to explore the relationship between JWA and heat stress protein (Hsp70) expression and possible mechanisms involved in inducing differentiation and heat stress. Methods The differentiation and heat stress model of K562 cells were established respectively. Western blot was used to detect the expression of JWA, Hsp70, heat shock transcription factor (HSF1) and HSF2 protein. Results (1) phorbol ester (TPA, 100 ng ml), hemin (3×10 -5 mol L), cytarabine (Ara C, 80 ng ml), adriamycin (4) ×10 - 8 mol L), all-trans retinoic acid (ATRA, 1 × 10 - 6 mol L), arsenic trioxide (As2O3, 1 × 10 -6 mol L) induced K562 cells 48 h, JWA, Hsp70 protein Expression levels increased significantly; HSF2 expression increased with hemin, Ara C, ad riamycin induction; (2) at 4 2°C at different times (10, 20, 30, 45, 60, 90 min) and at different temperatures (39) Under the treatment of °C, 4 2°C and 45°C, the change of Hsp70 expression level was similar to that of JWA protein, and HSF1 was expressed in the early stage of heat stress. Conclusion During the process of differentiation and heat stress, the expression levels of JWA and Hsp70 protein were significantly upregulated, and the trends were similar, but the intracellular signal transduction pathways involved may not be unique. JWA expression does not seem to have a direct characteristic association with HSF1 or HSF2.