Kabakov A E, Gabai V L
Medical Radiology Research Center, Obninsk, Russia.
Experientia. 1993 Aug 15;49(8):706-13. doi: 10.1007/BF01923956.
Ehrlich carcinoma and EL-4 thymoma ascites cells were subjected in vitro to heat shock, ATP depletion, oxidative stress, Ca2+ overloading and iodoacetamide treatment. After the transient stresses, Triton (X-100)insoluble (TIS) fractions were isolated from the cells and analysed by electrophoresis and immunoblotting. All stresses used caused rapid aggregation of cell proteins. This was manifested in a significant rise in protein content in the TIS fractions. The protein increase was mostly due to an increase in the insolubility of actin, 57 kDa protein of intermediate filaments, 70 kDa heat shock protein (HSP 70), and some specific proteins whose insolubilization was a characteristic sign for each type of cell injury. Different survival rates in the cell lines after either stress correlated well with differences in their TIS protein accretion. Possible mechanisms for stress-induced protein aggregation and its relationship with cell viability are suggested.
将艾氏腹水癌和EL-4胸腺瘤腹水细胞在体外进行热休克、ATP耗竭、氧化应激、Ca2+超载和碘乙酰胺处理。短暂应激后，从细胞中分离出Triton（X-100）不溶性（TIS）组分，并通过电泳和免疫印迹进行分析。所有使用的应激均导致细胞蛋白质快速聚集。这表现为TIS组分中蛋白质含量显著增加。蛋白质增加主要是由于肌动蛋白、中间丝的57 kDa蛋白质、70 kDa热休克蛋白（HSP 70）以及一些特定蛋白质的不溶性增加，这些蛋白质的不溶性增加是每种细胞损伤类型的特征性标志。应激后细胞系中不同的存活率与其TIS蛋白积聚的差异密切相关。文中提出了应激诱导蛋白质聚集的可能机制及其与细胞活力的关系。
