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To identify proteins involved in cellular adaptive responses to zinc, acomparative proteome analysis between a previously developed high zinc- andcadmium- resistant human epithelial cell line (HZR) and the parental HeLa cellshas been carried out. Differentially produced proteins included co-chaperones,proteins associated with oxido-reductase activities, and ubiquitin. Biochemicalpathways to which these proteins belong were probed for their involvement inthe resistance of both cell lines against cadmium toxicity. Among endoplasmicreticulum stressors, thapsigargin sensitized HZR cells, but not HeLa cells, tocadmium toxicity more acutely than tunicamycin, implying that these cellsheavily relied on proper intracellular calcium distribution. The similarsensitivity of both HeLa and HZR cells to inhibitors of the proteasome, such asMG-132 or lactacystin, excluded improved proteasome activity as a mechanismassociated with zinc adaptation of HZR cells. The enzyme4-hydroxyphenylpyruvate dioxygenase was overproduced in HZR cells as comparedto HeLa cells. It transforms 4-hydroxyphenylpyruvate to homogentisate in thesecond step of tyrosine catabolism. Inhibition of 4-hydroxyphenylpyruvatedioxygenase decreased the resistance of HZR cells against cadmium, but not thatof HeLa cells, suggesting that adaptation to zinc overload and increased4-hydroxyphenylpyruvate removal are linked in HZR cells

Zinc adaptation and resistance to cadmium toxicity in mammalian cells. Molecular insight by proteomic analysis