Recombinant Heat Shock Protein 27 (HSP27/HSPB1) protects against Cadmium-induced oxidative stress and toxicity in human cervical cancer cells

ALVAREZ - OLMEDO DG; BIAGGIO VS; KUMBANDINGA J; GOMEZ NN; CHUNHUA C; CIOCCA DR; ZARAH B; FANELLI MA; O´BRIEN E

CELL STRESS & CHAPERONES.

SPRINGER

Lugar: Berlin; Año: 2017

1355-8145

Cadmium(Cd) is a non-essential metal, carcinogenic and an important environmentalpollutant that is up-taken by living organisms through the diet, smoke andoccupational exposure. Although the physiological effects of Cd in humans havebeen extensively studied, the molecular mechanisms involved in Cd toxicity arenot fully understood, due in part to the pleiotropic pathways and targetsaffected by Cd. Moreover,the mitigation actions during Cd toxicity are based oncheaters and there are still not specific treatments for Cd toxicity. The aim of this work was to investigate some of the mechanisms involved in cadmiumtoxicity, and to evaluate the cytoprotective function of HSP27 in acute Cdtoxicity. Our results showed that the harmful effects of Cd were related to the induction ofoxidative stress, in particular due to peroxynitrite production and with thereduction of the cellular HSP27. Cd induced ROS formation, peroxynitriteformation, lipid peroxidation and protein nitration. After 1 h of Cd treatment,doses of 5 uM increase NO bioavailability while doses higher of Cd 50 uMreduceit. This is the first time a relationship between Cd-induced toxicity andperoxynitrite production is described.In fact, the addition of SIN-1 to theculture medium decreased HSP27 levels, similar to the treatment with Cd 100 uMduring 24 h, confirming that PN is responsible of HSP27 reduction. Cell-deathinduced by Cd can be counteracted by blocking NO production or applying apre-treatment with rHSP27/rC1 to restore cell viability.