title: Resistance of Ehrlich tumor cells to apoptosis can be due to accumulation of heat shock proteins.
abstract: Previously we have found that stationary Ehrlich ascites carcinoma (EAC) cells in vivo accumulated heat shock proteins (HSPs) and became resistant to necrotic death induced by prolonged energy deprivation of hyperthermia. Here we report that apoptotic death induced by nutrient starvation, transient ATP depletion, heat shock and a microtubule-disrupting drug, vinblastine, was also suppressed in stationary EAC cells comparing with exponential cells. When exponential (sensitive) cells were subjected to short-term heating with recovery to accumulate inducible form of HSP70, they also became resistant to all of the employed apoptosis-inducing exposures, and an inhibitor of cytosolic protein synthesis, cycloheximide, prevented acquisition of the resistance. It is suggested that in vivo accumulation of HSPs in stationary tumor cells can be endogenous protective device against apoptotic death induced by starvation or some anticancer treatments.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000972:Antineoplastic Agents, Phytogenic / Q000494:pharmacology*; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology*; D002453:Cell Cycle / Q000187:drug effects / Q000502:physiology; D002843:Chromatin / Q000187:drug effects / Q000648:ultrastructure; D004273:DNA, Neoplasm / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D051379:Mice; D008810:Mice, Inbred C57BL; D008870:Microtubules / Q000187:drug effects; D014747:Vinblastine / Q000494:pharmacology*
chemical_list: D000972:Antineoplastic Agents, Phytogenic; D002843:Chromatin; D004273:DNA, Neoplasm; D006360:Heat-Shock Proteins; D014747:Vinblastine; D000255:Adenosine Triphosphate