Oxidative stress induces a subset of heat shock proteins in rat hepatocytes and MH1C1 cells.
Lipoperoxidative damage caused by exposure of isolated hepatocytes or cultivated hepatoma cells to ADP-iron or to 4-hydroxynonenal induces the synthesis of some proteins which are different under these two conditions but are always a subset of the proteins induced in each type of cells upon heat-shock (heat-shock proteins). For at least one of these proteins (hsp 31), induced by 4-hydroxynonenal, the increase is dose-dependent and the effect of heat and the chemical seems to be additive. Lipoperoxidation may be implicated in the induction of some of the heat shock proteins, but reproduces only incompletely the response of protein synthesis typical of heat-shock conditions.
Cajone
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F
Istituto di Patologia Generale dell'Universita' degli Studi di Milano, Italy.
Bernelli-Zazzera
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A
D000244:Adenosine Diphosphate / Q000031:analogs & derivatives / Q000494:pharmacology; D000447:Aldehydes / Q000494:pharmacology; D000818:Animals; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D008054:Lipid Peroxides / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D014407:Tumor Cells, Cultured
D000447:Aldehydes; D006360:Heat-Shock Proteins; D008054:Lipid Peroxides; C029936:adenosine diphosphate-ferric chelate; D000244:Adenosine Diphosphate; C027576:4-hydroxy-2-nonenal