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Abstract
Hep G2 cells do not synthesize heat-shock proteins when incubated with ADP-iron, under conditions that can trigger lipoperoxidation. However, exposure of these cells to added 4-hydroxynonenal (HNE), one of the main products of lipoperoxidation, induces the synthesis of hsp70, the most conserved among heat-shock proteins. HNE acts mainly on transcription: in Hep G2 cells the increase in the steady-state level of hsp70 mRNA is detectable by two different hybridization techniques.