Paraquat and menadione exposure of rainbow trout (Oncorhynchus mykiss) - Studies of effects on the pentose-phosphate shunt and thiamine levels in liver and kidney

Chemico-Biological Interactions

Volumn 142, Issue 3, 2003, Pages 269-283

  Åkerman, Gun ^a   Amcoff, Patric ^b   Tjärnlund, Ulla ^a   Fogelberg, Kajsa ^a   Torrissen, Ole ^c   Balk, Lennart ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^c INSTITUTE OF MARINE RESEARCH   (Norway)

Author keywords

Early mortality syndrome; Fish reproduction; Glucose 6 phosphate dehydrogenase; Glutathione reductase; M74; Paraquat; Thiamine; Transketolase; Vitamin B1

Indexed keywords

COCARBOXYLASE; ETHOXYRESORUFIN DEETHYLASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE REDUCTASE; MENADIONE; PARAQUAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIAMINE; TRANSKETOLASE;

AEROBIC METABOLISM; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; ARTIFICIAL DIET; CONTROLLED STUDY; ENZYME ACTIVITY; EXPOSURE; FOOD COMPOSITION; KIDNEY; LIVER LEVEL; MUSCLE LEVEL; NONHUMAN; OXIDATION REDUCTION REACTION; PENTOSE PHOSPHATE CYCLE; RAINBOW TROUT; TISSUE LEVEL; XENOBIOTIC METABOLISM;

ANIMALS; FEMALE; GLUCOSEPHOSPHATE DEHYDROGENASE; GLUTATHIONE REDUCTASE; KIDNEY; LIVER; MALE; NADP; ONCORHYNCHUS MYKISS; OXIDATION-REDUCTION; PARAQUAT; PENTOSE PHOSPHATE PATHWAY; THIAMINE; TRANSKETOLASE; VITAMIN K 3; XENOBIOTICS;

MYKISS; ONCORHYNCHUS MYKISS; SALMONIDAE;

EID: 0037420965     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00122-9     Document Type: Article

References (45)

1. Åkerman G., Balk L. Descriptive studies of mortality and morphological disorders on early life stages of Cod and Salmon originating from the Baltic Sea. McDonald G., Fitzsimons J.D., Honeyfield D.C., Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea. 1998;41-61 American Fisheries Society Symposium 21, Bethesda, Maryland.
2. 1) concentrations in salmon (Salmo salar), brown trout (Salmo trutta) and cod (Gadus morhua) from the Baltic Sea. Ambio. 28:1999;48-54.
3. Fisher J.P., Fitzsimons J.D., Combs G.F., Spitsbergen J.M. Naturally occurring thiamine deficiency causing reproductive failure in Finger Lakes Atlantic salmon and Great Lakes lake trout. Trans. Am. Fish. Soc. 125:1996;167-178.
4. Fisher J.P., Brown S.B., Wooster G.W., Bowser P.R. Maternal blood, egg and larval thiamin levels correlate with larval survival in landlocked Atlantic salmon (Salmo salar). J. Nutr. 128:1998;2456-2466.
5. Fitzsimons J.D. The effect of B-vitamins on a swim-up syndrome in Lake Ontario lake trout. J. Great Lakes Res. 21:1995;286-289.
6. Marcquenski S.V. Early mortality syndrome (EMS) in salmonid fishes from the Great Lakes. Rolland R.M., Gilbertson M., Peterson R.E., Chemically Induced Alterations in Functional Development and Reproduction of Fishes. 1997;135-152 SETAC (Society of Environmental Toxicology and Chemistry), Pensacola, Florida.
7. J. Lundström, Clinical and pathological studies of Baltic salmon suffering from Yolk sac fry mortality, in: G. McDonald, J.D. Fitzsimons, D.C. Honeyfield (Eds.), Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea1, American Fisheries Society, Symposium 21, Bethesda, Maryland, 1998, pp. 62-72.
8. P. Amcoff, H. Börjeson, R. Eriksson, L. Norrgren, Effects of thiamine treatments on survival of M74-affected feral Baltic Salmon, in: G. McDonald, J.D. Fitzsimons, D.C. Honeyfield (Eds.), Early Life Stage Mortality Syndrome in Fishes of the Great Lakes and Baltic Sea, American Fisheries Socitey Symposium 21, Bethesda, Maryland, 1998, pp. 31-40
9. Börjeson H., Amcoff P., Ragnarsson B., Norrgren L. Reconditioning of sea-run Baltic salmon (Salmo salar) that have produced progeny with the M74 syndrome. Ambio. 28:1999;30-36.
10. Koski P., Pakarinen M., Nakari T., Soivio A., Hartikainen K. Treatment with thiamine hydrochloride and astaxanthine for the prevention of yolk-sac mortality in Baltic salmon fry (M74 syndrome). Dis. Aquat. Org. 37:1999;209-220.
11. Amcoff P., Åkerman G., Börjeson H., Tjärnlund U., Norrgren L., Balk L. Hepatic activities of thiamine-dependent enzymes, glucose 6-phosphate dehydrogenase and cytochrome P4501A in Baltic salmon (Salmo salar) yolk-sac fry after thiamine treatment. Aquat. Toxicol. 48:2000;391-402.
12. Pettersson A., Lignell A. Astaxanthin deficiency in eggs and fry of Baltic salmon (Salmo salar) with the M74 syndrome. Ambio. 28:1999;43-47.
13. H. Börjeson, L. Förlin, L. Norrgren, Investgations of antioxidants and prooxidants in salmon affected by the M74 syndrome, in: B.E. Bengtsson, C. Hill, S. Nellbring (Eds.), Report from the Second Workshop on Reproduction Disturbances in Fish, Stockholm, Swedish Environmental Protection Agency Report, 4534, Sweden, 1996, pp. 95-96.
14. Pickova J., Kiessling A., Pettersson A., Dutta P.C. Fatty acid and carotenoid composition of eggs from two nonanadromous Atlantic salmon stocks of cultured and wild origin. Fish Physiol. Biochem. 21:1999;147-156.
15. Lundström J., Carney B., Amcoff P., Pettersson A., Börjeson H., Förlin L., Norrgren L. Antioxidative systems, detoxifying enzymes and thiamine levels in Baltic salmon (Salmo salar) that develop M74. Ambio. 28:1999;24-29.
16. Amcoff P., Åkerman G., Tjärnlund U., Börjeson H., Norrgren L., Balk L. Physiologial, biochemical, and morphological studies of Baltic salmon yolk-sac fry with an experimental thiamine deficiency: relations to the M74 syndrome. Aquat. Toxicol. 16:2002;15-23.
17. Pesonen M., Andersson T.B., Sorri V., Korkalainen M. Biochemical and ultrastructural changes in the liver of Baltic salmon sac fry suffering from high mortality (M74). Environ. Toxicol. Chem. 18:1999;1007-1013.
18. Mathews C.K., van Holde K.E. Biochemistry. 1990;The Benjamin/Cummings Publishing Company, Redwood City, CA.
19. G. Åkerman, U. Tjärnlund, E. Noaksson, L. Balk, Evidence for anthropogenic substances causing thiamine deficiency in fish larvae when using model substances, Annual Meeting of SETAC-Europe, Bordeaux, France 14 1998 (Abstract).
20. Smeets E.H.J., Muller H., de Wael J. A NADH-dependent transketolase assay in erythrocyte hemolysates. Clin. Chim. Acta. 33:1971;379-386.
21. Tate J.R., Nixon P.F. Measurement of Michaelis constant for human erythrocyte transketolase and thiamin diphosphate. Anal. Biochem. 160:2001;78-87.
22. Taketa K., Watanabe A. Interconvertible microheterogeneity of glucose 6-phosphate dehydrogenase in rat liver. Biochim. Biophys. Acta. 235:1971;19-26.
23. Prough R.A., Burke M.D., Mayer R.T. Direct fluorometric methods for measuring mixed-function oxidase activity. Fleischer S., Packer L., Methods in Enzymology, (LII:C). 1978;372-377 Academic Press, New York.
24. Carlberg I., Mannervik B. Purification and characterization of flavoenzyme glutathione reductase from rat liver. J. Biol. Chem. 250:1975;5475-5480.
25. Lowry O.H., Roseborough N.J., Farr A.L., Randall R.J. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
26. Roser L., Andrist A.H., Harrington W.H., Naito H.K., Lonsdale D. Determination of urinary thiamine by high-pressure liquid chromatography utilizing the thiochrome fluorescent method. J. Chromat. 146:1978;43-53.
27. Masumoto T., Hardy R.W., Casillas E. Comparison of transketolase activity and thiamin pyrophosphate levels in erythrocytes and liver of rainbow trout (Salmo gairdneri) as indicators of thiamin status. J. Nutr. 117:1987;1422-1426.
28. Sabate L., Franco R., Canela E.I., Centelles J.J., Cascante M. A model of the pentose-phosphate pathway in rat-liver cells. Mol. Cell. Biochem. 142:1995;9-17.
29. Balk L., Ericson G., Lindesjöö E., Pettersson I., Tjärnlund U., Åkerman G. Effects of Exhaust from Two-Stroke Outboard Engines on Fish. 528:1994;1-66 Nordic Council of Ministers, Copenhagen, Denmark.
30. Vigano L., Arillo A., Bagnaso M., Bennicelli C., Melodia F. Xenobiotic metabolizing enzymes in uninduced and induced rainbow trout (Oncorhynchus mykiss) - effects of diets and food deprivation. Comp. Biochem. Physiol., PTC. 104:1993;51-55.
31. Blom S., Andersson T.B., Förlin L. Effects of food deprivation and handling stress on head kidney 17 alpha-hydroxyprogesterone 21-hydroxylase activity, plasma cortisol and the activities of liver detoxification enzymes in rainbow trout. Aquat. Toxicol. 48:2000;265-274.
32. Barroso J.B., Peragon J., Contreras-Jurado C., Garcia-Salguero L., Corpas F.J., Esteban F.J., Peinado M.A., De La Higuera M., Lupianez J.A. Impact of starvation-refeeding on kinetics and protein expression of trout liver NADPH-production systems. Am. J. Physiol.-Regul. Integr., C. 43:1998;R1578-R1587.
33. Bus J.S., Gibson J.E. Paraquat: model for oxidant-initiated toxicity. Environ. Health Perspect. 55:1984;37-46.
34. Bus J.S., Cagen S.Z., Olgaard M., Gibson J.E. Mechanism of paraquat toxicity in mice and rats. Toxicol. Appl. Pharmacol. 35:1976;501-513.
35. Fisher A.B., Reicherter J. Pentose pathway of glucose-metabolism in isolated granular pneumocytes-metabolic-regulation and stimulation by paraquat. Biochem. Pharmacol. 33:1984;1349-1353.
36. Rose M.S., Smith L.L., Wyatt I. Relevance of pentose-phosphate pathway stimulation in rat lung to mechanism of paraquat toxicity. Biochem. Pharmacol. 25:1976;1763-1767.
37. Brigelius R., Lenzen R., Sies H. Increase in hepatic mixed disulfide and glutathione disulfide levels elicited by paraquat. Biochem. Pharmacol. 31:1982;1637-1641.
38. Reddy K.A., Litov R.E., Omaye S.T. Effect of pretreatment with antiinflammatory agents on paraquat toxicity in the rat. Res. Commun. Chem. Pathol. Pharmacol. 17:1977;87-100.
39. Pedrajas J.R., Peinado J., Lopez Barea J. Oxidative stress in fish exposed to model xenobiotics. Oxidatively modified forms of Cu, Zn-superoxide dismutase as potential biomarkers. Chem. Biol. Interact. 98:1995;267-282.
40. Gabryelak T., Klekot J. The effect of paraquat on the peroxide metabolism enzymes in erythrocytes of freshwater fish species. Comp. Biochem. Physiol., C. 81:1985;415-418.
41. Förlin L., Blom S., Celander M., Sturve J. Effects on UDP glucuronosyl transferase, glutathione transferase, DT-diaphorase and glutathione reductase activities in rainbow trout liver after long-term exposure to PCB. Mar. Environ. Res. 42:1996;213-216.
42. Petrivalsky M., Machala M., Nezveda K., Piacka V., Svobodova Z., Drabek P. Glutathione-dependent detoxifying enzymes in rainbow trout liver: search for specific biochemical markers of chemical stress. Environ. Toxicol. Chem. 16:1997;1417-1421.
43. Celander M., Näf C., Broman D., Förlin L. Temporal aspects of induction of hepatic cytochrome P450 1A and conjugating enzymes in the viviparous blenny (Zoarces viviparus) treated with petroleum hydrocarbons. Aquat. Toxicol. 29:1994;183-196.
44. Lemaire P., Matthews A., Förlin L., Livingstone D.R. Stimulation of oxyradical production of hepatic microsomes of flounder (Platichthys flesus) and perch (Perca fluviatilis) by model and pollutant xenobiotics. Arch. Environ. Contam. Toxicol. 26:1994;191-200.
45. Cadenas E. Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem. Pharmacol. 49:1995;127-140.