Characteristic induction of 70,000 da-heat shock protein and metallothionein by zinc in HeLa cells.

The synthesis of a 70,000 dalton-heat shock protein (hsp70) is one of several heat shock proteins induced in HeLa cells during the incubation in medium containing zinc sulphate. The synthesis of hsp70 was increased in the presence of 200 microM zinc sulphate and above, but not at 100 microM zinc sulphate. On the other hand, the synthesis of metallothionein was activated in the presence of 100 microM zinc sulphate and above. Uptake of zinc into the cells depended on the concentration of zinc sulphate in the medium. The separation of intracellular zinc into three fractions by gel filtration chromatography; high molecular, metallothionein, and low molecular fractions, showed that zinc in the low molecular weight and metallothionein fractions was elevated in the presence of 100 microM zinc sulphate in the medium, whereas increase in the zinc content of the high molecular weight fraction occurred at 200 microM zinc sulphate and above. Inhibition of cell growth and cellular protein synthesis was also observed at 200 microM zinc sulphate and above, but not at 100 microM. From these findings, since the induction of hsp70 synthesis and inhibition of cell growth occurred concomitantly with the increase of zinc in the high and low molecular weight fractions, hsp70 seemed not to function in the detoxification of zinc, but it may participate in the repair of zinc-induced damage.