Antioxidant enzymatic defenses and oxidative damage in Dentex dentex fed on different dietary macronutrient levels

Comparative Biochemistry and Physiology - C Toxicology and Pharmacology

Volumn 150, Issue 4, 2009, Pages 537-545

  Pérez Jiménez, Amalia ^a   Hidalgo, M Carmen ^a   Morales, Amalia E ^a   Arizcun, Marta ^b   Abellán, Emilia ^b   Cardenete, Gabriel ^a  

^a UNIVERSITY OF GRANADA   (Spain)

^b Instituto Español de Oceanografía   (Spain)

Author keywords

Antioxidant enzymes; Common dentex; Lipid peroxidation; Macronutrients; Protein oxidation; SOD isoenzymes

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; COPPER ZINC SUPEROXIDE DISMUTASE I; COPPER ZINC SUPEROXIDE DISMUTASE II; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; ISOENZYME; MANGANESE SUPEROXIDE DISMUTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTIOXIDANT ACTIVITY; ARTICLE; CONTROLLED STUDY; DENSITOMETRY; DENTEX DENTEX; DIETARY INTAKE; ELECTROPHORESIS; ENZYME ACTIVITY; ERYTHROCYTE; FAST MUSCLE; FAT INTAKE; FISH; HEART; LIPID PEROXIDATION; MACRONUTRIENT; NONHUMAN; OXIDATIVE STRESS; PERCIFORMES; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTAKE; WESTERN BLOTTING;

DENTEX; DENTEX DENTEX;

EID: 70149100838     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2009.07.011     Document Type: Article

References (64)

1. Aebi H. Catalase in vitro. Methods Enzymol. 105 (1984) 121-126
2. Álvarez M.J., Lopez-Bote C.J., Díez A., Corraze G., Arzel J., Dias J., Kaushik S.J., and Bautista J.M. Dietary fish oil and digestible protein modify susceptibility to lipid peroxidation in the muscle of rainbow trout (Oncorhynchus mykiss) and sea bass (Dicentrarchus labrax). Br. J. Nutr. 80 (1998) 281-289
3. Álvarez M.L., López-Bote C.J., Díez A., Corraze G., Arzel J., Dias J., Kaushik S.J., and Bautista J.M. The partial substitution of digestible protein with gelatinized starch as an energy source reduces susceptibility to lipid oxidation in rainbow trout (Oncorhynchus mykiss) and sea bass (Dicentrarchus labrax) muscle. J. Anim. Sci. 77 (1999) 3322-3329
4. AOAC. Official Methods of Analysis. Association of Official Analytical Chemists, Gaithersburg, Maryland, USA (2000) 1018 pp.
5. Bao Y., Li L., Wu Q., and Zhang G. Cloning, characterization, and expression analysis of extracellular copper/zinc superoxide dismutase gene from bay scallop Argopecten irradians. Fish Shellfish Immunol. (2009) 10.1016/j.fsi.2008.11.014
6. Beauchamp C.O., and Fridovich I. Superoxide dismutase: improved assays and assay applicable to acrylamide gels. Anal. Biochem. 44 (1971) 276-287
7. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye-binding. Anal. Biochem. 72 (1976) 248-254
8. Brouwer M., Brouwer T.H., Grater W., and Brown-Peterson N.B. Replacement of a cytosolic copper/zinc superoxide dismutase by a novel cytosolic manganese superoxide dismutase in crustaceans that use copper (haemocyanin) for oxygen transport. Biochem. J. 374 (2003) 219-228
9. Buege J.A., and Aust S.D. Microsomal lipid peroxidation. Methods Enzymol. 52 (1978) 302-310
10. Capo C., Stroppolo M.E., Galtieri A., Lania A., Costanzo S., Petruzzelli R., Calabrese L., Polticelli F., and Desideri A. Characterization of Cu, Zn superoxide dismutase from the bathophile fish Lampanyctus crocodilus. Comp. Biochem. Physiol. B 117 (1997) 403-407
11. Davis B.J. Disc electrophoresis-II: method and application to human serum protein. Ann. N.Y. Acad. Sci. 121 (1964) 404-427
12. Due A.V., Petersen S.V., Valnickova Z., Østergaard L., Oury T.D., Crapo J.D., and Enghild J.J. Extracellular superoxide dismutase exists as an octamer. FEBS Lett. 580 (2006) 1485-1489
13. Fattman C.L., Schaefer L.M., and Oury T.D. Extracellular superoxide dismutase in biology and medicine. Free Radic. Biol. Med. 35 (2003) 236-256
14. Flohé L., and Günzler W.A. Assay of glutathione peroxidase. Methods Enzymol. 105 (1984) 115-121
15. Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., and Crapo J.D. Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization. Am. J. Respir. Cell Mol. Biol. 17 (1997) 393-403
16. Fridovich I. Biological effects of the superoxide radical. Arch. Biochem. Biophys. 247 (1986) 1-11
17. Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64 (1995) 97-112
18. González M., Romestand B., Fievet J., Huvet A., Lebart M.C., Gueguen Y., and Bachère E. Evidence in oyster of a plasma extracellular superoxide dismutase which binds LPS. Biochem. Biophys. Res. Commun. 338 (2005) 1089-1097
19. Halliwell B., and Gutteridge J.M.C. Free Radicals in Biology and Medicine. 4th Ed. (2007), Oxford University Press, New York
20. Hidalgo M.C., Expósito A., Palma J.M., and de la Higuera M. Oxidative stress generated by dietary Zn-deficiency: studies in rainbow trout (Oncorhynchus mykiss). Int. J. Biochem. Cell Biol. 34 (2002) 183-193
21. Hjalmarsson K., Marklund S.L., Engström A., and Edlund T. Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 6340-6344
22. Johansson M.W., Holmblad T., Thörnqvist P.O., Cammarata M., and Parrinello N. A cell-surface superoxide dismutase is a binding protein for peroxinectin, a cell-adhesive peroxidase in crayfish. J. Cell Sci. 112 (1999) 917-925
23. Kawaguchi T., Noji S., Uda T., Nakashima Y., Takeyasu A., Kawai Y., Takagi H., Tohyama M., and Taniguchi N. A monoclonal antibody against COOH-terminal peptide of human liver manganese superoxide dismutase. J. Biol. Chem. 264 (1989) 5762-5767
24. Letendre J., Chouquet B., Rocher B., Manduzio H., Leboulenger F., and Durand F. Differential pattern of Cu/Zn superoxide dismutase isoforms in relation to tidal spatio-temporal changes in the blue mussel Mytilus edulis. Comp. Biochem. Physiol. C 148 (2008) 211-216
25. Levine R.L., Garland D., Oliver C.N., Amici A., Climent I., Lenz A.G., Ahn B.W., Shaltiel S., and Stadtman E.R. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol. 186 (1990) 464-478
26. Lin Y.C., Vaseeharan B., and Chen J.C. Identification of the extracellular copper-zinc superoxide dismutase (ecCuZnSOD) gene of the mud crab Scylla serrata and its expression following beta-glucan and peptidoglycan injections. Mol. Immunol. 45 (2008) 1346-1355
27. Lygren B., and Hemre G.I. Influence of dietary carbohydrate on antioxidant enzyme activities in liver of Atlantic salmon (Salmo salar L.). Aquac. Int. 9 (2002) 421-427
28. Manduzio H., Monsinjon T., Galap C., Leboulenger F., and Rocher B. Seasonal variations in antioxidant defences in blue mussels Mytilus edulis collected from a polluted area: major contributions in gills of an inducible isoform of Cu/Zn-superoxide dismutase and of glutathione S-transferase. Aquat. Toxicol. 70 (2004) 83-93
29. Marklund S.L. Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 7634-7638
30. Marklund S.L. Properties of extracellular superoxide dismutase from human lung. Biochem. J. 220 (1984) 269-272
31. Martínez-Álvarez R., Morales A., and Sanz A. Antioxidant defenses in fish: biotic and abiotic factors. Rev. Fish Biol. Fisher. 15 (2005) 75-88
32. McCord J.M., and Fridovich I. Superoxide dismutase: an enzymic function for erythrocuprein. J. Biol. Chem. 244 (1969) 6049-6055
33. Monari M., Matozzo V., Foschi J., Cattani O., Serrazanetti G.P., and Marin M.G. Effects of high temperatures on functional responses of haemocytes in the clam Chamelea gallina. Fish Shellfish Immun. 22 (2007) 98-114
34. Morales A.E., Pérez-Jiménez A., Hidalgo M.C., Abellán E., and Cardenete G. Oxidative stress and antioxidant defenses after prolonged starvation in Dentex dentex liver. Comp. Biochem. Physiol. C 139 (2004) 153-161
35. Olsen R.E., Løvaas E., and Lie Ø. The influence of temperature, dietary polyunsaturated fatty acids, α-tocopherol and spermine on fatty acid composition and indices of oxidative stress in juvenile Arctic charr, Salvelinus alpinus (L.). Fish Physiol. Biochem. 20 (1999) 13-29
36. Ookawara T., Imazeki N., Matsubara O., Kizaki T., Oh-Ishi S., Nakao C., Sato Y., and Ohno H. Tissue distribution of immunoreactive mouse extracellular superoxide dismutase. Am. J. Physiol., Cell Physiol. 275 (1998) C840-C847
37. Oommen O.V., Sreejith P., Beyo R.S., Divya L., Vijayasree A.S., and Manju M. Thyroid hormones regulate mitochondrial respiration as well as antioxidant defense in teleosts too!. J. Endocrinolog. Reprod. 10 (2006) 96-105
38. Orbea A., Fahimi H.D., and Cajaraville M.P. Immunolocalization of four antioxidant enzymes in digestive glands of mollusks and crustaceans and fish liver. Histochem. Cell Biol. 114 (2000) 393-404
39. Osatomi K., Masuda Y., Hara K., and Ishihara T. Purification, N-terminal amino acid sequence, and some properties of Cu, Zn-superoxide dismutase from Japanese flounder (Paralichthys olivaceus) hepato-pancreas. Comp. Biochem. Physiol. B 128 (2001) 751-760
40. Pascual P., Pedrajas J.R., Toribio F., López-Barea J., and Peinado J. Effect of food deprivation on oxidative stress biomarkers in fish (Sparus aurata). Chem.-Biol. Interact. 145 (2003) 191-199
41. Pedrajas J.R., Peinado J., and López-Barea J. Purification of Cu,Zn-superoxide dismutase isoenzymes from fish liver: appearance of new isoforms as a consequence of pollution. Free Radic. Res. Commun. 19 (1993) 29-41
42. Pedrajas J.R., Gavilanes F., López-Barea J., and Peinado J. Incubation of superoxide dismutase with malondialdehyde and 4-hydroxy-2-nonenal forms new active isoforms and adducts. An evolution of xenobiotics in fish. Chem.-Biol. Interact. 116 (1998) 1-17
43. Pérez-Jiménez A., Hidalgo M.C., Morales A.E., Arizcun M., Abellán E., and Cardenete G. Use of different combinations of macronutrients in diets for dentex (Dentex dentex). Effects on intermediary metabolism. Comp. Biochem. Physiol. A 152 (2009) 314-321
44. Pérez-Jiménez A., Hidalgo M.C., Morales A.E., Arizcun M., Abellán E., and Cardenete G. Growth performance, feed utilization and body composition of Dentex dentex fed on different macronutrient combinations. Aquac. Res. (2009) 10.1111/j.1365-2109.2009.02312.x
45. Petersen S.V., Oury T., Oestergaard L., Valnickova Z., Wegrzyn J., Thogersen I.B., Jacobsen C., Bowler R.P., Fattman C.L., and Crapo J.D. Extracellular superoxide dismutase (EC-SOD) binds to type I collagen and protects against oxidative fragmentation. J. Biol. Chem. 279 (2004) 13705-13710
46. Poston H.A., Combs G.F., and Leibovitz L. Vitamin E and selenium inter- relations in the diet of Atlantic salmon (Salmo salar): gross, histological, and biochemical deficiency signs. J. Nutr. 106 (1976) 892-904
47. Radi A.A.R., Hay D.Q., Matokovics B., and Gabrielak T. Comparative antioxidant enzyme study in freshwater fish with different types of feeding behaviour. Comp. Biochem. Physiol. B 81 (1985) 395-399
48. Radi A.A.R., Matkovics B., and Csengeri I. Comparative studies of the phospholipid fatty acids and the antioxidant enzyme activities in fish with different feeding habits. Comp. Biochem. Physiol. B 87 (1987) 49-54
49. Rueda-Jasso R., Conceição L.E.C., Dias J., De Coen W., Gomes E., Rees J.F., Soares F., Dinis M.T., and Sorgeloos P. Effect of dietary non-protein energy levels on condition and oxidative status of Senegalese sole (Solea senegalensis) juveniles. Aquaculture 231 (2004) 417-433
50. Sagone A.L., Greenwald J., Kraut E.H., Bianchine J., and Singh D. Glucose: A role as a free radical scavenger in biological systems. J. Lab. Clin. Med. 101 (1983) 97-103
51. Sentman M.L., Granström M., Jakobson H., Reaume A., Basu S., and Marklund S.L. Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 281 (2006) 6904-6909
52. Sies H. Oxidative stress: introductory remarks. In: Sies H. (Ed). Oxidative stress (1985), Academic Press, London 1-8
53. Sies H., and Stahl W. Vitamins E and C, β-carotene, and other carotenoids as antioxidants. Am. J. Clin. Nutr. 62 (1995) 1315S-1321S suppl
54. Stéphan G., Guillaume J., and Lamour F. Lipid peroxidation in turbot (Scophthalmus maximus) tissue: effect of dietary vitamin E and dietary n-6 or n-3 polyunsaturated fatty acids. Aquaculture 130 (1995) 251-268
55. Tocher D.R., Mourente G., Van der Eecken A., Evjemo J.O., Díaz E., Bell J.G., Geurden I., Lavens P., and Olsen Y. Effects of dietary vitamin E on antioxidant defence mechanisms of juvenile turbot (Scophthalmus maximus L.), halibut (Hippoglossus hippoglossus L.) and sea bream (Sparus aurata L.). Aquac. Nutr. 8 (2002) 195-207
56. Trenzado C.E., Morales A.E., Palma J.M., and de la Higuera M. Blood antioxidant defenses and hematological adjustments in crowded/uncrowded rainbow trout (Oncorhynchus mykiss) fed on diets with different levels of antioxidant vitamins and HUFA. Comp. Biochem. Physiol. C 149 (2009) 440-447
57. Tukey J.W. Comparing individual means in the analysis of variance. Biometrics 5 (1949) 99-114
58. Weisiger R.A., and Fridovich I. Superoxide dismutase: organelle specificity. J. Biol. Chem. 248 (1973) 3582-3592
59. Winston G.W., and Di Giulio R.T. Prooxidant and antioxidant mechanisms in aquatic organisms. Aquat. Toxicol. 19 (1991) 137-161 ç
60. Wuerges J., Lee J.W., Yim Y.I., Yim H.S., Kang S.O., and Carugo K.D. Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 8569-8574
61. Van Kampen E.J., and Zijlstra W.J. Standardization of hemoglobinometry. Clin. Chim. Acta 6 (1961) 538-544
62. Yao C.L., Wang A.L., Wang Z.Y., Wang W.N., and Sun R.Y. Purification and partial characterization of Cu, Zn superoxide dismutase from haemolymph of Oriental river prawn Macrobrachium nipponense. Aquaculture 270 (2007) 559-565
63. Yano S. Multiple isoelectric variants of copper, zinc-superoxide dismutase from rat liver. Arch. Biochem. Biophys. 219 (1990) 60-69
64. Zelko I.N., Mariani T.J., and Folz R.J. Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and ECSOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 33 (2002) 337-349