Relationship between the induction of proteins in the HSP70 family and thermosensitivity in two species of Oryzias (Pisces)

Arai, Ayami; Mikami, Hiroshi; Naruse, Kiyoshi; Shima, Akihiro

doi:10.1016/0305-0491(94)90127-9

Cited by 18 publications

(7 citation statements)

References 10 publications

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“…A heat shock response, notably of HSP70, has been demonstrated in a number of studies using fish cells (Arai et al, 1994;Airaksinen et al, 1998Airaksinen et al, , 2003 and also in whole animal experiments with marine (Dietz and Somero, 1992) and freshwater fish (Molina et al, 2000), exposed to a variety of stresses including heat (for a review, see Iwama et al, 1998). We found only insignificantly elevated HSP70 levels after recovery from 26°C, which supports the view that no major inactivation of native proteins had occurred at this temperature.…”

Section: Discussionsupporting

confidence: 84%

Oxidative stress during stressful heat exposure and recovery in the North Sea eelpoutZoarces viviparusL.

Heise

Puntarulo

Nikinmaa

et al. 2006

Journal of Experimental Biology

183

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SUMMARY The interplay between antioxidants, heat shock proteins and hypoxic signaling is supposed to be important for passive survival of critical temperature stress, e.g. during unfavorable conditions in hot summers. We investigated the effect of mild (18°C), critical (22°C) and severe(26°C) experimental heat stress, assumed to induce different degrees of functional hypoxia, as well as the effect of recovery following heat stress on these parameters in liver samples of the common eelpout Zoarces viviparus. Upon heat exposure to critical and higher temperatures we found an increase in oxidative damage markers such as TBARS (thiobarbituric reactive substances)and a more oxidized cellular redox potential, combined with reduced activities of the antioxidant enzyme superoxide dismutase at 26°C. Together, these point to higher oxidative stress levels during hyperthermia. In a recovery-time series, heat-induced hypoxia and subsequent reoxygenation upon return of the fishes to 12°C led to increased protein oxidation and chemiluminescence rates within the first 12 h of recovery, therein resembling ischemia/reperfusion injury in mammals. HSP70 levels were found to be only slightly elevated after recovery from sub-lethal heat stress, indicating minor importance of the heat shock response in this species. The DNA binding activity of the hypoxia-inducible transcription factor (HIF-1) was elevated only during mild heat exposure(18°C), but appeared impaired at more severe heat stress. We suppose that the more oxidized redox state during extreme heat may interfere with the hypoxic signaling response.

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Section: Discussionsupporting

confidence: 84%

Oxidative stress during stressful heat exposure and recovery in the North Sea eelpoutZoarces viviparusL.

Heise

Puntarulo

Nikinmaa

et al. 2006

Journal of Experimental Biology

183

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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: 87%

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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“…Interestingly, Hsc71, the cognate form of Hsp70 that is expressed constitutively and is not inducible in most taxa, was induced in G. mirabilis. The upregulation of Hsc71 has also been shown in medaka (Arai et al, 1994) and Atlantic salmon (Lund et al, 2002). The induction of Hsc71 may be related to a stressrelated increase in the requirement for chaperoning of nascent polypeptides during protein biosynthesis, a primary role of Hsc71 under normal conditions.…”

Section: Thermally Responsive Changes In Gene Expression Cluster 1: Pmentioning

confidence: 91%

The cellular response to heat stress in the gobyGillichthys mirabilis: a cDNA microarray and protein-level analysis

Buckley

Gracey

Somero

2006

Journal of Experimental Biology

239

221

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SUMMARY The cellular response to stress relies on the rapid induction of genes encoding proteins involved in preventing and repairing macromolecular damage incurred as a consequence of environmental insult. To increase our understanding of the scope of this response, a cDNA microarray, consisting of 9207 cDNA clones, was used to monitor gene expression changes in the gill and white muscle tissues of a eurythermic fish, Gillichthys mirabilis(Gobiidae) exposed to ecologically relevant heat stress. In each tissue, the induction or repression of over 200 genes was observed. These genes are associated with numerous biological processes, including the maintenance of protein homeostasis, cell cycle control, cytoskeletal reorganization,metabolic regulation and signal transduction, among many others. In both tissues, the molecular chaperones, certain transcription factors and a set of additional genes with various functions were induced in a similar manner;however, the majority of genes displayed tissue-specific responses. In gill,thermal stress induced the expression of the major structural components of the cytoskeleton, whereas these same genes did not respond to heat in muscle. In muscle, many genes involved in promoting cell growth and proliferation were repressed, perhaps to conserve energy for repair and replacement of damaged macromolecules, but a similar repression was not observed in the gill. Many of the observed changes in gene expression were similar to those described in model species whereas many others were unexpected. Measurements of the concentrations of the protein products of selected genes revealed that in each case an induction in mRNA synthesis correlated with an increase in protein production, though the timing and magnitude of the increase in protein was not consistently predicted by mRNA concentration, an important consideration in assessing the condition of the stressed cell using transcriptomic analysis.

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Relationship between the induction of proteins in the HSP70 family and thermosensitivity in two species of Oryzias (Pisces)

Cited by 18 publications

References 10 publications

Oxidative stress during stressful heat exposure and recovery in the North Sea eelpoutZoarces viviparusL.

Oxidative stress during stressful heat exposure and recovery in the North Sea eelpoutZoarces viviparusL.

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

The cellular response to heat stress in the gobyGillichthys mirabilis: a cDNA microarray and protein-level analysis

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