Analysis of stress-induced gene expression in fish cell lines exposed to heavy metals and heat shock

Misra, Santosh; Zafarullah, Muhammad; Price-Haughey, Janet; Gedamu, Lashitew

doi:10.1016/0167-4781(89)90155-3

Cited by 96 publications

(35 citation statements)

References 33 publications

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“…Protection of the cells by a preceding cellular stress, probably due to the presence of residual heat shock proteins in the cell (Jaattela, 1999;Samali et al, 1999), was also observed on the integrated reporter gene. This response behavior is similar to that observed in other whole organisms (Krone and Heikkila, 1988;Misra et al, 1989;Arai et al, 1994) or in transient expression experiments (Vogel et al, 1997).…”

Section: Discussionsupporting

confidence: 88%

“…The expression of HSP70 proteins is regulated by a variety of toxic compounds (Morimoto, 1998), according to its function most often at sublethal levels, and their induction following exposure to environmental stressors has been increasingly studied in recent years. The methods used in these studies range from direct detection of the protein in extracts from cells or whole organisms by SDS-PAGE-gel electrophoresis (Misra et al, 1989), specific detection of HSP70 by Western blotting (Dunlap and Matsumura, 1997;De Wachter et al, 1998) or detection of the induced HSP70 mRNA levels by RT-PCR (Steiner et al, 1998). Reporter gene assays using mammalian cells containing an expression construct based on a HSP70 promoter have also been described (Todd et al, 1995;Vincent et al, 1997;Aı¨t-Aı¨ssa et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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A transformed fish cell line expressing a green fluorescent protein-luciferase fusion gene responding to cellular stress

Molina

Carpeaux

Martial

et al. 2002

Toxicology in Vitro

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We obtained a stable transformed fish (EPC) cell line containing a reporter gene under the control of the tilapia HSP70 promoter. Expression of the reporter gene, coding for a green fluorescent protein (GFP)-luciferase fusion protein, was assessed by measuring the luciferase enzymatic activity by luminometry and the GFP expression by fluorescence microscopy and flow cytometry. The clone was characterized for its capacity to respond to heat shock treatment. The results show high induction after 1 h at 37 C of treatment, up to 500-fold. In addition, its convenience to detect a large range of cellular stressors was evaluated. We observed high induction when Cd 2+ , Zn 2+ , Hg 2+ or Cu 2+ was added, but not Pb 2+ . In addition, activation of the reporter gene was observed in the presence of other compounds such as acetyl chloride, tetrachlorophenol, chloroacetamide and sodium arsenite. In conclusion, this cell line can be used as a rapid, cheap and easy biological test to determine cellular stress induced by environmental pollutants, alone or in conjunction with other, more specific assays. #

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

A transformed fish cell line expressing a green fluorescent protein-luciferase fusion gene responding to cellular stress

Molina

Carpeaux

Martial

et al. 2002

Toxicology in Vitro

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“…HSP70 expression differs among rainbow trout clonal lines, suggesting the genetic control of differences in HSP70 expression (Heredia-Middleton et al 2008). Trout cells have also been used in bioassays of heavy metal exposure in which the expression of HSP70 and metallothioneins was the indicator of exposure (Kothary and Candido 1982;Misra et al 1989). In these studies, HSP70 accumulated in juvenile trout tissues, including the gill and liver, in response to exposure to metal (Cd 2+ , Cu 2+ , Pb 2+ , Zn 2+ )-contaminated water and diet.…”

Section: -1 Hsp70 and Other Hsps In Rainbow Troutmentioning

confidence: 99%

Stress Protein HSP70 in Fish

Yamashita¹,

Yabu²,

Ojima³

2010

Aqua-BioSci. Monogr. (ABSM)

128

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Stress proteins (heat-shock proteins, HSPs), which comprise an evolutionally wellconserved protein family, are induced in response to a variety of stress conditions and metabolic insults. When cells are subjected to sudden environmental changes, stress proteins are induced and play a central role in cellular homeostasis. A response to sudden adverse environmental changes is referred to as the heat-shock or stress response and is accompanied by a rapid increase in the synthesis of stress proteins. Given the importance of stress proteins in thermal adaptation at the cellular level, we have studied the expression, regulation, and protective functions of the members of the HSP70 stress protein family under normal and stress conditions in a variety of fish species. HSP70/heat-shock cognate protein-70 (HSC70) plays essential roles in the receptor complex formation and activation of Activin/Nodal/transforming growth factor-β and bone morphogenetic protein receptors and facilitates Nodal signaling. In addition, chaperone-mediated autophagy assisted by HSP70/heat-shock cognate (HSC)70 may be responsible for the stress responses in fish cells. HSP70 and HSC70 translocated into the lysosomes were found to accelerate protein degradation and catabolism under both stressed and normal conditions.

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“…Various other physiological effects of Cd 2ϩ have been described. These include induction of single-strand DNA breakage (12,13), promotion of neoplastic transformation both in vitro and in vivo (14 -17), activation and translocation to the nucleus of protein kinase C (18 -20), increase in the intracellular level of inositol polyphosphates (21) and Ca 2ϩ (22)(23)(24)(25), induction of gene expression of heat shock protein (26,27), metallothionein (12,28,29), heme oxygenase (30,31), and transcriptional activation of protooncogenes such as c-jun, c-fos, and c-myc (29,(32)(33)(34).…”

mentioning

confidence: 99%

Role of ATM in Oxidative Stress-mediated c-Jun Phosphorylation in Response to Ionizing Radiation and CdCl2

Lee

Dritschilo

Jung

2001

Journal of Biological Chemistry

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Ionizing radiation-induced phosphorylation of the transcription factor c-Jun is impaired in cells derived from individuals with ataxia telangiectasia (AT), in which the ATM gene is mutated. We demonstrate here that ATM modulates c-Jun phosphorylation following exposure to ionizing radiation as well as treatment with CdCl 2 , a potent pro-oxidant. Exposure of AT and control fibroblasts to CdCl 2 induced a biphasic increase in cJun phosphorylation on serine residues 63 and 73, with the extent of the second phase being markedly greater in AT cells than in control cells. Heme oxygenase-1, a marker of oxidative stress, was also significantly induced in AT fibroblasts. Expression of recombinant ATM in AT fibroblasts, however, reduced the extent of the effects of CdCl 2 on both c-Jun phosphorylation and heme oxygenase-1 induction. Our data suggest that ATM contributes to oxidative stress-mediated signaling that leads to c-Jun phosphorylation by acting as a sensor of ionizing radiation-induced oxidative stress and by modulating intracellular redox homeostasis.

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Analysis of stress-induced gene expression in fish cell lines exposed to heavy metals and heat shock

Cited by 96 publications

References 33 publications

A transformed fish cell line expressing a green fluorescent protein-luciferase fusion gene responding to cellular stress

A transformed fish cell line expressing a green fluorescent protein-luciferase fusion gene responding to cellular stress

Stress Protein HSP70 in Fish

Role of ATM in Oxidative Stress-mediated c-Jun Phosphorylation in Response to Ionizing Radiation and CdCl2

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