Induction of stress proteins in chicken embryo cells by low-level zinc contamination in amino acid-free media.
It has been reported that chicken embryo cells deprived of exogenous amino acids for 4 hours synthesize stress (heat-shock) proteins. Herein, we show that amino acid deprivation is not sufficient to cause induction of stress proteins. Zinc contaminating a component of commercial cell culture medium used to prepare amino acid-free medium was an inducer in our cultures. In the absence of exogenous amino acids, the concentration of zinc ions needed for half-maximal induction of stress proteins was an order of magnitude lower than the dose required for cells in complete medium. Histidine and cystine, which have high affinities for zinc ions, were the amino acids most effective in blocking the induction of stress proteins by zinc. Problems posed by heavy metal ions in culture media and biologic fluids for searches for in vivo inducers of the cellular stress (heat shock) response are discussed.
D000596:Amino Acids / Q000172:deficiency*; D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo / Q000166:cytology / Q000378:metabolism*; D003470:Culture Media; D004305:Dose-Response Relationship, Drug; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D015032:Zinc / Q000494:pharmacology*
D000596:Amino Acids; D003470:Culture Media; D006360:Heat-Shock Proteins; D015032:Zinc