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First published online January 3, 2006
Journal of Experimental Biology 209, 353-363 (2006)
Published by The Company of Biologists 2006
doi: 10.1242/jeb.01977
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Oxidative stress during stressful heat exposure and recovery in the North Sea eelpout Zoarces viviparus L.

Katja Heise1, Susana Puntarulo2, Mikko Nikinmaa3, Doris Abele1,* and Hans-O. Pörtner1

1 Alfred-Wegener Institute for Polar and Marine Research, Physiology of Marine Animals, Am Handelshafen 12, 27570 Bremerhaven, Germany
2 Physical Chemistry-PRALIB, School of Pharmacy and Biochemistry, University of Buenos Aires, Junin 956, C 1113 AAD Buenos Aires, Argentina
3 Laboratory of Animal Physiology, Department of Biology, University of Turku, FIN20014 Turku, Finland



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Fig. 1. Superoxide dismutase (SOD) activity in Z. viviparus liver samples after 2 h of exposure to 18°, 22° and 26°C and after 24 h recovery (recov.) from the respective temperature. Enzyme activity was measured at 20°C. Values are means ± s.d., N=3-5; *significantly different from the unstressed group, P<0.05.

 


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Fig. 2. Glutathione redox chemistry in Z. viviparus liver samples after 2 h of exposure to 18°, 22° and 26°C and after 24 h recovery (recov.) from these temperatures. (A) Oxidized glutathione (GSSG) content. (B) Redox potential {Delta}E at in situ temperature and in situ intracellular pH (adopted from Sartoris et al., 2003Go; Larsen et al., 1997Go), calculated after Schaffer and Buettner (2001). Values are means ± s.d., N=4-7; *significantly different from the unstressed group, {dagger}significantly different from the respective recovery group, P<0.05.

 


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Fig. 3. Oxidative stress markers in Z. viviparus liver samples after 2 h of exposure to 18°, 22° and 26°C and after 24 h recovery (recov.) from these temperatures. (A) Tert-butyl hydroperoxide (tBOOH)-initiated chemiluminescence indicating imbalance between pro- and antioxidant processes. (B) Thiobarbituric reactive substances (TBARS) content, indicating lipid peroxidation. (C) Carbonyl content, indicating protein oxidation. Values are means ± s.d., N=4-6; *significantly different from the unstressed group, {dagger}significantly different from the respective recovery group, P<0.05.

 


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Fig. 4. DNA binding activity of HIF-1 in Z. viviparus whole cell extracts from the liver after 2 h of exposure to 18°, 22° and 26°C and after 24 h recovery (recov.) from these temperatures. (A) Signal intensity of HIF-1 DNA binding to the human erythropoietin enhancer. Lanes 1: unstressed; 2: 1°C; 3: 1°C recovery; 4: 5°C; 5: 5°C recovery; 6: 18°C; 7: 18°C recovery; 8: 22°C; 9: 22°C recovery; 10: 26°C; 11: 26°C recovery; data taken from the heat stress experiment (this study) and from cold stress (K. Heise, S. Puntarulo, M. Nikinmaa, M. Lucassen, H.-O. Pörtner and D. Abele, unpublished data). (B) HIF-1 DNA binding. Values are means ± s.d., N=4-5; *significantly different from the unstressed group, P<0.05. (C) Linear regression demonstrating increased HIF-1 DNA binding at a more reduced redox environment (y=0.065x-7.593; r2=0.3, N=50, P<0.05, Statview 5.0). Data taken from the heat stress experiment (this study) and from cold stress (K. Heise, S. Puntarulo, M. Nikinmaa, M. Lucassen, H.-O. Pörtner and D. Abele, unpublished data).

 


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Fig. 5. Glutathione redox chemistry in Z. viviparus liver samples after 2 h of exposure to 18°C and after 2, 8 or 12 h of recovery (recov.). (A) Reduced glutathione (GSH) content. (B) Oxidized glutathione (GSSG) content. (C) Total glutathione content (2GSSG+GSH). (D) Glutathione redox ratio (2GSSG/GSH). (E) Redox potential ({Delta}E) at in situ temperature and in situ intracellular pH (adopted from Sartoris et al., 2003Go; Larsen et al., 1997Go), calculated after Schaffer and Buettner (2001). Values are means ± s.d., N=4-5; *significantly different from the unstressed group, P<0.05.

 


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Fig. 6. Oxidative stress markers in Z. viviparus liver samples after 2 h of exposure to 18°C as well as after 2, 8 or 12 h of recovery (recov.). (A) Tert-butyl hydroperoxide (tBOOH)-initiated chemiluminescence, indicating imbalance between pro- and antioxidant processes. (B) Carbonyl content, indicating protein oxidation. Values are means ± s.d., N=3-5; *significantly different from the unstressed group, P<0.05.

 

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© The Company of Biologists Ltd 2006