Modulation of the stress response during apoptosis and necrosis induction in cadmium-treated U-937 human promonocytic cells.

摘要: Abstract Treatment for 2 h with 200 μM cadmium chloride, followed by recovery, caused apoptosis and induced heat-shock protein 70 (HSP70) expression in U-937 promonocytic cells. However, pre-incubation the GSH depleting agent l -buthionine-[ S,R ]-sulfoximine (BSO, 1 mM 24 h) necrosis instead of failed to induce HSP70 expression. This failure was a consequence depletion, since BSO allowed or even potentiated induction when used combination heat shock (2 at 42.5°C) 50 cadmium, which apoptosis. The administration N -acetyl- -cysteine (NAC) beginning recovery after BSO/200 treatment prevented execution restored apoptosis, but did not restore induction, indicating that inhibition is an early regulated event. contrasted capacity NAC prevent alterations other proteins, namely suppression Bax increase Bcl-2 HSP-60 Finally, it observed rapidly increased mRNA level stimulated factor (HSF1) trimerization binding, these effects were BSO. Taken together, results indicate stress response compatible cadmium-treated specifically due HSF1 activation.