Protein aggregation as primary and characteristic cell reaction to various stresses.
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.
Kabakov
A E
AE
Medical Radiology Research Center, Obninsk, Russia.
Gabai
V L
VL
D000199:Actins / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002286:Carcinoma, Ehrlich Tumor; D002470:Cell Survival; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006358:Hot Temperature; D007460:Iodoacetamide / Q000494:pharmacology; D051379:Mice; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D012995:Solubility; D013945:Thymoma; D013953:Thymus Neoplasms; D014407:Tumor Cells, Cultured
D000199:Actins; D006360:Heat-Shock Proteins; D009363:Neoplasm Proteins; D000255:Adenosine Triphosphate; D002118:Calcium; D007460:Iodoacetamide