Different activity of glyoxalase system enzymes in specimens of Sparus auratus exposed to sublethal copper concentrations

Chemico-Biological Interactions

Volumn 142, Issue 3, 2003, Pages 297-305

  Antognelli, Cinzia ^a   Romani, Rita ^a   Baldracchini, Francesca ^a   De Santis, Alessandra ^a   Andreani, Giulia ^b   Talesa, Vincenzo ^a  

^a UNIVERSITY OF PERUGIA   (Italy)

^b UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

Copper toxicity; Glyoxalase I; Glyoxalase II; Lactate dehydrogenase; Sparus auratus

Indexed keywords

COPPER; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTATE DEHYDROGENASE; LACTOYLGLUTATHIONE LYASE; SEA WATER;

ANIMAL TISSUE; ARTICLE; BIOACCUMULATION; BRAIN LEVEL; CELL LEVEL; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME LOCALIZATION; FAST MUSCLE; FISH; GLYCOLYSIS; LIVER LEVEL; NONHUMAN; TISSUE DISTRIBUTION;

ANIMALS; BRAIN; COPPER; GLUTATHIONE; GLYCOLYSIS; L-LACTATE DEHYDROGENASE; LACTOYLGLUTATHIONE LYASE; LIVER; MUSCLES; PYRUVALDEHYDE; SEA BREAM; THIOLESTER HYDROLASES;

ANIMALIA; OSTEICHTHYES; SPARUS AURATA;

EID: 0037420967     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00124-2     Document Type: Article

References (37)

1. Camakaris J., Voskoboinik I., Mercer J.F. Molecular mechanism of copper homeostasis. Biochem. Biophys. Res. Commun. 261:1999;225-232.
2. Radisky D., Kaplan J. Regulation of transition metal transport across the yeast plasma membrane. J. Biol. Chem. 274:1999;4481.
3. Falahi-Ardakani A. Contamination of environment with heavy metals emitted from automotives. Ecotoxicol. Environ. Saf. 8:1984;152-161.
4. Kesseler A., Brand M.D. Quantitative determination of the regulation of oxidative phosphorylation by cadmium in potato tuber mitochondria. Eur. J. Biochem. 225:1994;923-935.
5. Lovley D.R., Coates J.D. Bioremediation of metal contamination. Curr. Opin. Biotechnol. 8:1997;285-289.
6. Medvedev N., Panichev N., Hyvarinen H. Level of heavy metals in seals of Lake Ladoga and the White Sea. Sci. Total Environ. 206:1997;95-105.
7. Kargin F. Metal concentrations in tissues of the freshwater fish Capoeta barroisi from the Seyhan River (Turkey). Bull. Environ. Contam. Toxicol. 60:1998;822-828.
8. Viarengo A. Heavy metals in marine invertebrates: mechanisms of regulation and toxicity at the cellular level. C.R.C. Rev. Aquat. Sci. 1:1989;295-317.
9. Regoli F., Principato G. Glutathione, glutathione-dependent and antioxidant enzymes in mussel, Mytilus galloprovincialis, exposed to metals under field and laboratory conditions: implications for the use of biochemical biomarkers. Aquat. Toxicol. 31:1995;143-164.
10. Regoli F. Lysosomal responses as a sensitive stress index in biomonitoring heavy metal pollution. Mar. Ecol. Prog. Ser. 84:1992;63-69.
11. Viarengo A., Canesi L., Pertica M., Poli G., Moore M.N., Orunesu M. Heavy metal effects on lipid peroxidation in the tissues of Mytilus galloprovincialis. Lam. Comp. Biochem. Physiol. 97C:1990;37-42.
12. Thornalley P.J. Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endoproduct receptor. Clin. Rev. Oncol./Hematol. 20:1995;99-128.
13. 2+. Exp. Cell Res. 100:1976;104-110.
14. Liliom K., Wagner G., Pacz A., Cascante M., Kovacs J., Ovadi J. Organization-dependent effects of toxic bivalent ions. Microtubule assembly and glycolysis. Eur. J. Biochem. 267:2000;4731-4739.
15. Clarkson T.W. Metal toxicity in the central nervous system. Environ. Health Persp. 75:1987;59-64.
16. Liliom K., Wagner G., Kovacs J., Comin B., Cascante M., Orosz F., Ovadi J. Combined enhancement of microtubule assembly and glucose metabolism in neuronal systems in vitro. Decreased sensitivity to copper toxicity. Biochem. Biophys. Res. Commun. 264:1999;605-610.
17. Lai J.C.K., Blass J.P. Neurotoxic effects of copper: inhibition of glycolysis and glycolytic enzymes. Neurochem. Res. 9:1984;1699-1710.
18. Jannaschik D., Burgos M., Centelles J.J., Ovadi J., Cascante M. Application of metabolic control analysis to the study of toxic effects of copper in muscle extracts. FEBS Lett. 445:1999;144-148.
19. Kalapos M.P. Methylglyoxal in living organisms. Chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 110:1999;145-175.
20. Dethloff G.M., Bailey H.C., Maier K.J. Effects of dissolved copper on select haematological parameters of wild rainbow trout (Oncorhynchus mykiss). Arch. Environ. Contam. Toxicol. 40:2001;371-380.
21. Bervoets L., Blust R., Verheyen R. Accumulation of metals in the tissues of three spined stickelback (Gasterosteus aculeatus) from natural fresh waters. Ecotoxicol. Environ. Saf. 48:2001;117-127.
22. Beaumont M.W., Butler P.J., Taylor E.W. Exposure of brown trout, Salmo trutta, to a sublethal concentration of copper in soft acidic water: effects upon muscle metabolism and membrane potential. Aquat. Toxicol. 51:2000;259-272.
23. Serra R., Carpenè E., Marcantonio A.G., Isani G. Cadmium accumulation and Cd-binding proteins in the bivalve Scapharca inaequivalvis. Comp. Biochem: Physiol. 111C:1995;165-174.
24. Racker E. On the mechanism of action of glyoxalase. J. Biol. Chem. 190:1951;685-696.
25. Talesa V., Uotila L., Koivusalo M., Principato G., Giovannini E., Rosi G. Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms. Biochim. Biophys. Acta. 955:1988;103-110.
26. Demetriou J.A., Drewes P.A., Gin. Enzymes J.B. Henry R.J., Cannon D.C., Winkelman J.W., Clinical Chemistry, principles and technics. 1974;815-831 Harper & Row, Hagerstown.
27. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
28. Carpenè E., Serra R., Manera M., Isani G. Seasonal changes of zinc, copper and iron in gilthead sea bream (Sparus aurata) fed fortified diets. Biol. Trace. Element Res. 69:1999;121-139.
29. Pelgrom S.M.G.J., Lamers L.P.M., Lock R.A.C., Balm P.H.M., Wendelaar Bonga S.E. Interactions between copper and cadmium modify metal organ distribution in mature tilapia, Oreochromis mossambicus. Environ. Pollut. 90:1995;415-423.
30. Roch M., McCarter J.A. Hepatic metallothionein production and resistance to heavy metals by rainbow trout (Salmo gairdneri). I. Exposed to an artificial mixture of zinc, copper and cadmium. Comp. Biochem. Physiol. 77C:1984;71-75.
31. Marr J.C.A., Bergman H.L., Lipton J., Hogstrand C. Differences in relative sensitivity of naïve and metals-acclimated brown and rainbow trout exposed to metals representative of the Clark Fork River, Montana. Can. J. Fish Aquat. Sci. 52:1995;2016-2030.
32. Olsvik P.A., Gundersen P., Andersen R.A., Zachariassen K.E. Metal accumulation and metallothionein in brown trout, Salmo trutta, from two Norwegian rivers differently contaminated with Cd, Cu and Zn. Comp. Biochem. Physiol. 128C:2001;189-201.
33. Overnell J., McIntosh R. The effect of supplementary dietary copper on copper and metallothionein levels in the fish, dab, Limanda limanda. Mar. Environ. Res. 26:1988;237-247.
34. Cousins R.J. Absorption, transport and hepatic metabolism of copper and zinc: special reference to metallothionein and ceruloplasmin. Physiol. Rev. 65:1985;238-309.
35. Bremner I. Interactions between metallothionein and trace elements. Prog. Food Nutr. Sci. 11:1987;1-37.
36. Meister A. On the biochemistry of glutathione. Taniguchi N., Higashi T., Sakamoto S., Meister A., Glutathione centennial. Molecular perspectives and clinical implications. 1989;3-22 Academic Press, San Diego.
37. Uotila L. Purification and properties of S-succinylglutathione hydrolase from human liver. J. Biol. Chem. 254:1979;7024-7029.