Premium
Induction of stress proteins in chicken embryo cells by low‐level zinc contamination in amino acid‐free media
Author(s) -
Whelan Sandra A.,
Hightower Lawrence E.
Publication year - 1985
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041220207
Subject(s) - amino acid , zinc , cystine , histidine , biochemistry , embryo , heat shock protein , inducer , chemistry , protein biosynthesis , chemically defined medium , biology , in vitro , microbiology and biotechnology , cysteine , enzyme , organic chemistry , gene
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.