Chloramphenicol influence on antioxidant enzymes with preliminary approach on microsomal CYP1A immunopositive-protein in Chamelea gallina

Chemosphere

Volumn 73, Issue 3, 2008, Pages 272-280

  Monari, M ^a   Foschi, J ^a   Cortesi, P ^a   Rosmini, R ^a   Cattani, O ^a   Serrazanetti, G P ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

CAT; Chamelea gallina; Chloramphenicol; Cu Zn SOD; CYP1A immunopositive protein; Mn SOD

Indexed keywords

DETOXIFICATION; MANGANESE; MANGANESE COMPOUNDS; OXYGEN; PROTEINS;

ADRIATIC; ANTIOXIDANT ENZYMES; CAT; CATALASE (CAT); CHAMELEA GALLINA; CHLORAMPHENICOL; CU/ZN-SOD; CYP1A IMMUNOPOSITIVE-PROTEIN; CYTOCHROME P-450; MN-SOD; PRELIMINARY APPROACH; PROTEIN SYNTHESIS; ROS PRODUCTION; SUPER OXIDE DISMUTASE;

ANTIBIOTICS;

CATALASE; CHLORAMPHENICOL; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME P450 1A; MANGANESE SUPEROXIDE DISMUTASE; MICROSOME ENZYME; REACTIVE OXYGEN METABOLITE;

ANTIBIOTICS; ANTIOXIDANT; BIVALVE; DETOXIFICATION; ENZYME ACTIVITY; GENE EXPRESSION; INHIBITION; PROTEIN;

ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; BIVALVE; CHAMELEA GALLINA; CONTROLLED STUDY; CYP1A1 GENE; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENZYME ACTIVITY; ENZYME INHIBITION; NONHUMAN; OXIDATIVE STRESS; PROMOTER REGION; PROTEIN EXPRESSION; SPECTROPHOTOMETRY; WESTERN BLOTTING;

ANIMALS; ANTI-BACTERIAL AGENTS; ANTIOXIDANTS; BIVALVIA; BLOTTING, WESTERN; CATALASE; CHLORAMPHENICOL; CYTOCHROME P-450 ENZYME SYSTEM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MICROSOMES; SUPEROXIDE DISMUTASE;

BIVALVIA; CHAMELEA GALLINA; MOLLUSCA;

EID: 50049097154     PISSN: 00456535     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2008.06.033     Document Type: Article

References (78)

1. Aebi H. Catalase. In: Bergmayer H.U. (Ed). Methods of Enzymatic Analysis vol. 2 (1974), Springer, New York 673-683
2. Barker C.W., Fagan J.B., and Pasco D.S. Interleukin-1b suppresses the induction of P4501A1 and P4501A2 mRNAs in isolated hepatocytes. J. Biol. Chem. 267 (1992) 8050-8055
3. Barker C.W., Fagan J.B., and Pasco D.S. Down-regulation of P450 1A1 and P450 1A2 mRNA expression in isolated hepatocytes by oxidative stress. J. Biol. Chem. 269 (1994) 3985-3990
4. Barra D., Schinina M.E., Simmaco M., Bannister J.W., Bannister W.H., Rotilio G., et al. The primary structure of 675 human liver manganese superoxide dismutase. J. Biol. Chem. 259 (1984) 12595-12601
5. Brooks S.P., de Zwaan A., van den Thillart G., Cattani O., Cortesi P., and Storey K.B. Differential survival of Venus gallina and Scapharca inaequivalvis during anoxic stress: covalent modification of phosphofructokinase and glycogen phosphorilase during anoxia. J. Comp. Phys. B 161 (1991) 207-212
6. Chan P., Liao S.S., Hsu C.T., Lee Y.S., Brian T., Kuo J.S., et al. Superoxide dismutase gene expression and activity in the brain of spontaneously hypertensive rats and normotensive rats. Chin. Med. J. (Engl.) 112 (1999) 1119-1124
7. Clark I.A., Cowedn W.B., and Hunt N.H. Free radical-induced pathology. Med. Res. Rev. (1985) 5297-5332
8. Costello M.J., Grant A., Davies I.M., Cecchini S., Papoutsoglou S., Quigley D., et al. The control of chemicals used in aquaculture in Europe. J. Appl. Ichthyol. 17 (2001) 173-180
9. Crapo C., McCord A., and Fridovich I. Preparation and assay of superoxide dismutases. Methods Enzymol. 53 (1978) 382-393
10. Crapo, J.D., Oury, T., Rabouille, C., Slot, J.W., Chang, L.-Y., 1992. Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. P. Nat. Acad. Sci. USA 89, 10405-10409.
11. Crawford D.R., and Davies K.J. Adaptive response and oxidative stress. Environ. Health Perspect. 102 (1994) 25-28
12. Danis B., Goriely S., Dubois P., Fowler S.W., Flamand V., and Warnau M. Contrasting effects of coplanar versus non-coplanar PCB congeners on immunomodulation and CYP1A levels (determined using an adapted ELISA method) in the common sea star Asterias rubens L. Aquat. Toxicol. 69 (2004) 371-383
13. de Zwaan A., Cortesi P., Van der Thillart G., Roos J., and Storey K.B. Differential sensitivity to hypoxia by two tolerant marine molluscs: a biochemical analysis. Mar. Biol. 111 (1991) 343-351
14. de Zwaan A., Cattani O., Vitali G., and Cortesi P. Influence of incubation conditions on the anoxic survival of marine bivalves Static and semi-static incubations. Mar. Ecol- Prog. Ser. 211 (2001) 169-179
15. de Zwaan A., Babarro J.M.F., Monari M., and Cattani O. Anoxic survival potential of bivalves: (arte)facts. Comp. Biochem. Phys. A 131 3 (2002) 615-624
16. Farombi E.O., Nwankwo J.O., Wara S.H., Odutola B., and Emersole G.O. Chloramphenicol and ampicillin-induced changes in rat hepatic esterase and amidase activities. Biosci. Rep. 20 (2000) 13-19
17. Farombi E.O. Antioxidant and hepatic lipid peroxidation in chloramphenicol-treated rats. Tohoku J. Exp. Med. 194 (2001) 91-98
18. Farombi E.O., Adaramoye O.A., and Emerole A.G. Influence of chloramphenicol on rat hepatic microsomal components and biomarkers of oxidative stress: protective role of antioxidant. Pharmacol. Toxicol. 31 (2002) 129-134
19. Fridovich I. In: Oberley L.W. (Ed). Superoxide dismutase. Measuring the activity of superoxide dismutases: an embarrassment of riches. vol. 1 (1982), CRC Press, Boca Raton, Florida 69-77
20. Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64 (1995) 97-112
21. Froglia C. Clam fisheries with hydraulic dredges in the Adriatic Sea. In: Caddy J.F. (Ed). Marine invertebrate fisheries: their assessment and management (1989), John Wiley & Sons, Inc. 507-523
22. Gomirato G., and Nigro N. An antioxidant in pediatrics. Minerva Pediatr. 48 (1996) 321-324
23. Gonzalez F.J. Role of cytochromes P450 in chemical toxicity and oxidative stress: studies with CYP2E1. Mutat. Res. 569 (2005) 101-110
24. Grøsvik B.E., Jonsson H., Ortega M.J., Roepstorff P., and Goksøyr A. CYP1A-immunopositive proteins in bivalves identified as cytoskeletal and major vault proteins. Aquat. Toxicol. 79 (2006) 334-340
25. Halliwell B., and Gutteridge J.M.C. Free Radicals in Biology and Medicine (2000), Oxford University Press Inc, New York
26. Harris E.D. Regulation of antioxidant enzymes. FASEB J. 6 (1992) 2675-2681
27. Holt D.E., Harvey D., and Hurley R. Chloramphenicol toxicity. Adv. Drug. React. Toxicol. Rev. 12 (1993) 83-95
28. Holt D.E., Ryder T.A., Fairbairn A., Hurley R., and Harvey D. The myelotoxicity of chloramphenicol: in vitro and in vivo studies: I. In vitro effects on cells in culture. Human Exp. Toxicol. 16 (1997) 570-576
29. Isildar M., Jimenez J.J., Arimura G.K., and Yunis A. DNA damage in intact cells induced by bacterial metabolites of chloramphenicol. Am. J. Hematol. 28 (1988) 40-46
30. Iizuka S., Taniguchi N., and Makita A. Enzyme-linked immunosorbent assay for human manganese-containing superoxide dismutase and its content in lung cancer. J. Nat. Cancer Inst. 72 (1984) 1043-1049
31. Karbowski M., Kurono C., Nishizawa Y., Horie Y., Soji T., and Wakabayashi T. Induction of megamitochondria by some chemicals inducing oxidative stress in primary cultured rat hepatocytes. Biochem. Biophys. Acta 1349 (1997) 242-250
32. Karbowski M., Kurono C., Wozniak M., Ostrowski M., Teranishi M., Soji T., et al. Cycloheximide and 4-OH-TEMPO suppress chloramphenicol-induced apoptosis in RL-34 cells via the suppression of the formation of Megamitochondria. Biochem. Biophys. Acta 1449 (1999) 25-40
33. Kinnula V.L., and Crapo J.D. Superoxide dismutase in malignant cells and human tumors. Free Radical Biol. Med. 36 (2004) 718-744
34. Kitamura T., Ando J., Ishihara R., Takano S., Iijima T., Nishimura S., et al. Lack of carcinogenicity of thiamphenicol in F344 rats. Food Chem. Toxicol. 35 (1997) 1075-1080
35. Kraner J.C., Morgan E.T., and Halper J.R. Selective suppression of rat hepatic cytochrome P450 2C11 by chloramphenicol. J. Pharmacol. Exp. Ther. 270 (1994) 1367-1372
36. Liu L., Bridges R.J., and Eyer C.L. Effect of cytochrome P450 1A induction on oxidative damage in rat brain. Mol. Cell. Biochem. 223 (2001) 89-94
37. Livingstone D.R. Response of microsomal NADPH-cytocrome c reductase activity and cytocrome P450 in digestive glands of Mytilus edulis and Littorina littorea to environmental and experimental exposure to pollutants. Mar. Ecol-Prog. Ser. 46 (1988) 37-43
38. Livingstone D.R. The fate of organic xenobiotics in aquatic ecosystems: quantitative and qualitative differences in biotransformation by invertebrates and fish. Comp. Biochem. Phys. A 120 (1998) 43-49
39. Livingstone D.R. Contaminant-stimulated reactive oxygen species production and oxidative damage in aquatic organisms. Mar. Pollut. Bull. 42 (2001) 656-666
40. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall J. Protein measure with the folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
41. Manduzio H., Monsinjon T., Rocher B., Leboulenger F., and Galap C. Characterization of an inducible isoform of the Cu/Zn superoxide dismutase in the blue mussel Mytilus edulis. Aquat. Toxicol. 64 (2003) 73-83
42. Mates J.M., and Sanchez-Jimenez F. Antioxidant enzymes and their implications in pathophysiologic processes. Front. Biosci. 4 (1999) 339-345
43. Matsuhashi T., Liu X.R., Nishizawa Y., Usukura J., Wozniak M., and Wakabayashi T. Mechanism of the formation of megamitochondria in the mouse liver induced by chloramphenicol. Toxicol. Lett. 86 (1996) 47-54
44. Michiels C., and Remacle J. Use of the inhibition of enzymatic antioxidant systems in order to evaluate their physiological importance. Eur. J. Biochem. 177 (1988) 435-441
45. Miller K.A., Assunçaõ M.G.L., Dangerfield N.J., Bandiera S.M., and Ross P.S. Assessment of cytochrome P450 1A in harbour seals (Phoca vitulina) using a minimally-invasive biopsy approach. Mar. Environ. Res. 60 (2005) 153-169
46. MIPA VI (2005). Interaction between bacteria and bivalves of commercial interest in eutrophic areas. Evaluation of structural and functional aspects and effects on survival. Ministero delle politiche Agricole e Forestali, VI Piano Triennale n° 6-C-66.
47. Miranda C.L., Henderson M.C., and Buhler D.R. Evaluation of chemicals as inhibitors of trout cytochrome P450s. Toxicol. Appl. Pharm. 148 (1998) 37-244
48. Moazed D., and Noller H.F. Chloramphenicol, erythromycin, carbomycin and vernamycin B protectoverlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochemie 69 (1987) 879-884
49. Monari M., Matozzo V., Foschi J., Marin M.G., and Cattani O. Exposure to anoxia of the clam, Chamelea gallina II: modulation of superoxide dismutase activity and expression in haemocytes. J. Exp. Mar. Biol. Ecol. 325 (2005) 175-188
50. 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 Immunol. 22 (2007) 98-114
51. Monari M., Cattani O., Serrazanetti G.P., Selli A., Pagliuca G., Zironi E., et al. Effect of exposure to benzo[a]pyrene on SODs, CYP1A1/1A2-and CYP2E1 immunopositive proteins in blood clam Scapharca inaequivalvis. Mar. Environ. Res. 63 (2007) 200-218
52. Monari M., Serrazanetti G.P., Foschi J., Ma tozzo V., Marin M.G., and Cattani O. Effects of salinity on the clam Chamelea gallina haemocytes. Part II: superoxide dismutase response. Mar. Biol. 151 (2007) 1059-1068
53. Morel Y., and Barouki R. Down-regulation of cytochrome P450 1A1 gene promoter by oxidative stress: critical contribution of NFI. J. Biol. Chem. 273 (1998) 26969-26976
54. Morel Y., Mermod N., and Barouki R. An autoregulatory loop controlling CYP1A1 gene expression: role of H2O2 and NFI. Mol. Cell. Biol. 19 (1999) 6825-6832
55. Ortiz-Delgado J.B., Segner H., and Sarasquete C. Cellular distribution and induction of CYP1A following exposure of gilthead seabream, Sparus aurata, to waterborne and dietary benzo(a)pyrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin: An immunohistochemical approach. Aquat. Toxicol. 75 (2005) 144-161
56. Peters L.D., Nasci C., and Livingstone D.R. Immunochemical investigation of cytochrome P450 forms/epitopes (CYP1A, 2B, 2E, 3A and 4A) in digestive gland of Mytilus sp. Comp. Biochem. Phys. C 121 (1998) 361-369
57. Petska S. Inhibitors of ribosome functions. Annu. Rev. Microbiol. 25 (1971) 1580
58. Porter T.D., and Coon M.J. Cytochrome P450 Multiplicity of isoforms, substrates, and catalytic regulatory mechanisms. J. Biol. Chem. 266 (1991) 13469-13472
59. Rendic S., and Di Carlo F.J. Human cytochrome P450 enzymes: a status report summarizing their reactions, substrates, inducers, and inhibitors. Drug Metab. Rev. 29 (1997) 413-580
60. Rewitz K.F., Styrishave B., Lobner-olesen A., and Andersen O. Marine invertebrate Cytochrome P450: emerging insights from vertebrate and insect analogies. Comp. Biochem. Phys. C 143 (2006) 363-381
61. Risso-de Faverney C., Lafaurie M., Girare J.P., and Rahmani R. The nitroxide stable radical tempo prevents metal-induced inhibition of CYP1A1 expression and induction. Toxicol. Lett. 111 (2000) 219-227
62. Schlunzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R., et al. Structural basis fort he interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413 (2001) 814-821
63. Sen C.K., and Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 10 (1996) 709-720
64. Solé M., and Livingstone D.R. Components of the cytochrome P450-dependent monooxygenase system and 'NADPH-independent benzo[a]pyrene hyroxylase' activity in a wide range of marine invertebrate species. Comp. Biochem. Phys. C 141 (2005) 20-31
65. Somjetlerdcharoen, A., 2002. Chloramphenicol concerns in shrimp culture. Aquacolture, Asia 7, pp. 51-54.
66. Stegeman, J.J., Hahn, M.E., 1994. In: Malins D.C., Ostrander G.K. (Eds.), Biochemistry and molecular biology of monooxygenases: current perspectives of forms, function and regulation of cytochrome P450 in aquatic species. Aquatic Toxicology, Molecular Biochemical and Cellular perspectives. London Lewis, pp. 87-206.
67. Teo S., Pohl L., and Halpert J. Production of superoxide anion radicals during the oxidative metabolism of amino-chloramphenicol. Biochem. Pharmacol. 35 (1986) 4584-4586
68. Teramitsu H., Yamamoto Y., Chiba I., Iwata H., Tenace S., Fujise Y., et al. Identification of novel cytochrome P450 1A genes from five marine mammal species. Aquat. Toxicol. 51 (2000) 145-153
69. Tilley R.E., Kemp G.D., Teramitsu I., and Hall A.J. Isolation of two cytochrome P450 cDNAs, CYP1A1 and CYP1A2, from harp seal (Phoca groenlandica) and grey seal (Halichoerus grypus). Comp. Biochem. Phys. C 132 (2002) 181-191
70. Turton J.A., Yallop D., Andrews C.M., Fagg R., York M., and Williams T.C. Haemotoxicity of chloramphenicol succinate in the CD-1 mouse and Wistar Hanover rat. Human Exp. Toxicol. 18 (1999) 566-567
71. Wakabayashi T., Adachi K., Matsuhashi T., Wozniak M., Antosiewicz J., and Karbowski M. Suppression of the formation of megamitochondria by scavengers for free radicals. Mol. Aspect Med. 18 (1997) 51-61
72. Wakabayashi T., and Karbowski M. Structural changes of mitochondria related to apoptosis. Biol. Signal Recept. 10 (2001) 26-56
73. Wiesner L., Powell W.H., Karchner S.I., Franks D.G., Cooper E.L., Kauschke E., et al. Oxidants and antioxidants in aquatic animals. Comp. Biochem. Phys. C 100 (1991) 173-176
74. Wootton A.N., Herring C., Spry J.A., Wiseman A., Livingstone D.R., and Goldfarb P.S. Evidence for the existence of cytochrome P450 gene families (CYP1A, 3A, 4A, 11A) and modulation of gene expression (CYP1A) in the mussel Mytilus spp. Mar. Environ. Res. 39 (1995) 21-26
75. Yoo H.Y., Chang M.S., and Rho H.M. The activation of the rat copper/zinc superoxide dismutase gene by hydrogen peroxide through the hydrogen-peroxide-responsive element and by paraquat and heat shock through the same heat shock element. J. Biol. Chem. 274 (1999) 23887-23892
76. Yu Q., and Rengel Z. Micronutrient deficiency influences plant growth and activities of superoxide dismutases in narrow-leafed Lupins. Ann. Bot-London 83 (1999) 175-182
77. Yunis A.A. Differential in-vitro toxicity of chloramphenicol, nitroso-chloramphenicol, and thiamphenicol. Sex. Transm. Dis. 11 (1984) 340-342
78. 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 EC-SOD (SOD3) gene structures, evolution and expression. Free. Radical Biol. Med. 33 (2002) 337-349