Induction of stress proteins in chicken embryo cells by low‐level zinc contamination in amino acid‐free media

Whelan, Sandra A.; Hightower, Lawrence E.

doi:10.1002/jcp.1041220207

Cited by 19 publications

(12 citation statements)

References 25 publications

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“…These levels are within the range reported to induce HSP72 in several cell types (Caltabiano et al, 1986;Misra et al, 1989;Nover, 1984;Whelan and Hightower, 1985), suggesting that release of endogenous zinc may contribute to the induction of heat shock proteins observed in brain after seizures or ischemia. As a separate consideration, zinc is an agent that could potentially be used to induce stress protein expression in brain and thereby facilitate study of possible protective effects of these proteins.…”

Section: Introductionsupporting

confidence: 78%

“…This toxicity increased two to threefold in media free of amino acids or serum. As noted by Whelan and Hightower (1985), zinc can complex to amino acids, especially cysteine, histidine, and glutamine, such that the presence of these amino acids even at low levels may markedly decrease the concentration of free zinc. We also observed a great decrease in apparent toxicity when zinc solutions were stored a t concentrations below 500 pM.…”

Section: Discussionmentioning

confidence: 99%

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Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Swanson

Sharp

1992

Glia

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Zinc is a potent inducer of the 72 kD heat shock protein (HSP72). In brain, pathological conditions such as ischemia and seizures increase extracellular zinc. The present study examines the effect of zinc on HSP72 expression in rat primary cortical astrocyte culture. Astrocytes were grown to confluence and exposed to zinc chloride in CO2-equilibrated Earle's buffered salt solution. Expression of HSP72 was examined using immunocytochemistry. HSP72 was induced with zinc concentrations of 5 to 100 microM after 4 h exposures, or 200 to 300 microM after 15 min exposures. At the lower concentrations expression occurred in small clusters of contiguous cells. At concentrations high enough to cause cell death, HSP72-positive astrocytes formed a continuous margin around patches of dead cells. These patterns of HSP72 expression are similar to the patterns seen after cerebral ischemia in vivo. Exposure to zinc at 100 microM for 4 h or 400 microM for 15 min caused greater than 90% cell death. Increases in extracellular zinc may contribute to HSP72 induction and astrocyte death under ischemia and other pathological conditions in brain.

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Section: Introductionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Swanson

Sharp

1992

Glia

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“…Amino acid deprivation studies using culture media supplemented with serum, no matter how the serum is dialyzed, is accompanied by a possible contamination of amino acids of various-sized polypeptides released by proteolysis, and some may be utilized by the cells (Piez et al, 1960). Whelan and Hightower (1985) demonstrated that a contaminant, probably zinc, only becomes a serious problem when amino acids, especially cysteinel cystine and histidine (which are most effective in blocking the induction of stress protein by zinc), are omitted or depleted from the medium. However, in the 3Y1, decrease in cell number under simultaneous limitation of all amino acids was less and much more gradual than that seen under limitation of Cys alone (Fig.…”

Section: Discussionmentioning

confidence: 99%

Influence of the deprivation of a single amino acid on cellular proliferation and survival in rat 3Y1 fibroblasts and their derivatives transformed by a wide variety of agents

Tanaka

Zaitsu

Onodera

et al. 1988

Journal Cellular Physiology

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We compared proliferation and survival of various syngeneic transformed cell lines under conditions of depletion of 15 amino acids in Dulbecco-Eagle's medium. We used a normal fibroblast line 3Y1 and 22 transformed sublines of 3Y1 which had been induced by one of seven transforming agents--simian virus 40, mouse polyomavirus, adenovirus type 12, E1A gene of adenovirus type 12, cDNA of Harvey murine sarcoma virus, Rous sarcoma virus, or N-methyl-N'-nitro-N-nitrosoguanidine. Unlike other untransformed cells examined (mouse BALB/c-3T3 line, mouse NIH-3T3 line, and primary Fischer rat embryo fibroblasts), 3Y1 ceased to proliferate and accumulated in a viable state with a G1-phase DNA content under 14 singular deprivations of amino acid. None of the transformed 3Y1 lines completely arrested in the G1 phase of the cell cycle and each showed different levels of survival, depending on each transforming agent. As for transformed 3Y1 cells induced by a given virus or a given transforming gene, any one of the three sublines shared the same trend with respect to proliferation and survival. Transformed derivatives induced by N-methyl-N'-nitro-N-nitrosoguanidine showed almost the same trend in proliferation, but the patterns of survival were not uniform. Our observations suggest that the unique responses of 3Y1 to amino acid depletion are differently modified by different transforming agents.

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“…In cultured animal cells, several seminal studies using isothermal treatments with amino acid analogs (Hightower 1980) or low concentrations of zinc (Whelan and Hightower 1985) caused expression of molecular chaperones. In a similar manner, isothermal treatments of human cells with Hsp90 inhibitors, UV light, elesclomol, or cigarette smoke best recapitulated the expression pattern of heat shock by inducing a similar subset of about 45 out of 167 chaperome genes (Supplemental Fig.…”

Section: Most Hsps Are Not Chaperones and Most Chaperones Are Not Hspsmentioning

confidence: 99%

Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells

Finka

Mattoo

Goloubinoff

2011

Cell Stress and Chaperones

134

152

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Molecular chaperones are central to cellular protein homeostasis. In mammals, protein misfolding diseases and aging cause inflammation and progressive tissue loss, in correlation with the accumulation of toxic protein aggregates and the defective expression of chaperone genes. Bacteria and non-diseased, non-aged eukaryotic cells effectively respond to heat shock by inducing the accumulation of heat-shock proteins (HSPs), many of which molecular chaperones involved in protein homeostasis, in reducing stress damages and promoting cellular recovery and thermotolerance. We performed a meta-analysis of published microarray data and compared expression profiles of HSP genes from mammalian and plant cells in response to heat or isothermal treatments with drugs. The differences and overlaps between HSP and chaperone genes were analyzed, and expression patterns were clustered and organized in a network. HSPs and chaperones only partly overlapped. Heat-shock induced a subset of chaperones primarily targeted to the cytoplasm and organelles but not to the endoplasmic reticulum, which organized into a network with a central core of Hsp90s, Hsp70s, and sHSPs. Heat was best mimicked by isothermal treatments with Hsp90 inhibitors, whereas less toxic drugs, some of which nonsteroidal anti-inflammatory drugs, weakly expressed different subsets of Hsp chaperones. This type of analysis may uncover new HSP-inducing drugs to improve protein homeostasis in misfolding and aging diseases.

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Induction of stress proteins in chicken embryo cells by low‐level zinc contamination in amino acid‐free media

Cited by 19 publications

References 25 publications

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture

Influence of the deprivation of a single amino acid on cellular proliferation and survival in rat 3Y1 fibroblasts and their derivatives transformed by a wide variety of agents

Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells

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