Abstract
The activity of several cuproenzymes in relation to the immune system was examined in serum and blood cells from bovines with molybdenum-induced copper deficiency. Five female cattle were given molybdenum (30 ppm) and sulfate (225 ppm) to induce experimental secondary copper deficiency. Ceruloplasmin activity was determined in serum. The Cu,Zn-superoxide dismutase and cytochrome c oxidase activities were measured in peripheral blood lymphocytes, neutrophils, and monocyte-derived macrophages. Copper deficiency was confirmed from decreased serum copper levels and the animals with values less than 5.6 µmol/L were considered deficient. The content of intracellular copper decreased between 40% and 70% in deficient cells compared with the controls. In copper-deficient animals, the serum ceruloplasmin activity decreased to half of the control value. Both of them, the Cu,Zn-superoxide dismutase and the cytochrome c oxidase activities, undergo a significant reduction in leukocytes, showing differences among diverse cell populations. We concluded that the copper deficiency alters the activity of several enzymes, which mediate antioxidant defenses and ATP formation. These effects may impair the cell immune functionality, affecting the bactericidal capacity and making the animals more susceptible to infection.
Similar content being viewed by others
References
J. R. Prohaska, Biochemical functions of copper in animals, in Essential and Toxic Elements in Human Health and Disease, A. S. Prasad, ed., Alan R. Liss, New York (1988).
F. Malatesta, G. Antonini, P. Sarti, and M. Brunori, Structure and function of a molecular machine: cytochrome c oxidase, Biophys. Chem. 54, 1–33 (1995).
J. M. McCord and I. Fridovich, Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein), J. Biol. Chem. 244, 1581–1588 (1969).
L. Ryden, Ceruloplasmin, Copper Proteins and Copper Enzymes, R. Contie, ed., CRC, Boca Raton, FL, pp. 37–100 (1981).
B. M. Babior, R. S. Kipnes, and J. T. Curnutte, Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent, J. Clin. Invest. 52, 741–744 (1973).
B. Halliwell and J. M. C. Gutterridge, Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts, Arch. Biochem. Biophys. 246, 501–514 (1986).
L. De Chatelet, Initiation of the respiratory burst in human polymorphonuclear neutrophils: a critical review, J. Reticuloendot. Soc. 24, 73–91 (1978).
J. D. Allen and M. Gawthorne, Involvement of the solid phase of rumen digesta in the interaction between copper, molybdenum and sulphur in sheep, Br. J. Nutr. 58, 265–272 (1987).
H. A. Ravin, An improved colorimetric enzymatic assay of ceruloplasmin, J. Lab. Clin. Med. 58, 161–168 (1961).
O. Barta, L. Shaffer, and L. J. Huang, Separation of lymphocytes, monocytes and neutrophils, in Laboratory Techniques of Veterinary Immunology, O. Barta, ed., C. C. Thomas, Springfield, IL (1984).
D. I. Bounous, F. M. Enright, K. A. Gossett, C. M. Berry, and M. T. Kearney, Comparison of oxidant production by bovine neutrophils and monocyte-derived macrophages stimulated with Brucella abortus strain 2308, Inflammation 16, 215–225 (1992).
C. Beauchamp and I. Fridovich, Superoxide dismutase: improved assays and an assay applicable to acrylamide gels, Anal. Biochem. 44, 276–287 (1971).
S. J. Cooperstein and A. Lazarow, A microspectrophotometric method for the determination of cytochrome oxidase, J. Biol. Chem. 189, 665–670 (1951).
H. J. Cohen, P. E. Newburger, M. E. Chovaniec, J. C. Whitin, and E. R. Simons, Opsonized zymosan-stimulated granulocytes. Activation and activity of the superoxidegenerating system and membrane potential changes, Blood 58, 975–982 (1981).
J. P. Kehler, Free radicals as mediators of tissue injury and desease, Crit. Rev. Toxicol. 23, 21–48 (1993).
J. M. McCord, Human disease, free radicals and the oxidant/antioxidant balance, Clin. Biochem. 26, 351–357 (1993).
S. P. Wolff, A. Garner, and R. T. Dean, Free radicals, lipids and protein degradation, Trends Biochem. Sci. 11, 27–31 (1986).
M. J. H. Smith, Prostaglandins and the polymorphonuclear leukocyte, Agents Actions 6, 91–103 (1979).
S. I. Cerone, A. S. Sansinanea, S. A. Streitenberger, M. C. Garcia, and N. J. Auza, Bovin neutrophil functionality in molibdenum-induced copper deficiency, Nutr. Res. 18, 557–566 (1998).
S. I. Cerone, A. S. Sansinanea, and N. J. Auza, Copper deficiency alters the immune response of bovine, Nutr. Res. 15, 1333–1341 (1995).
J. R. Prohaska, S. W. Downing, and O. A. Lukasewycz, Chronic dietary copper deficiency alters biochemical and morphological properties of mouse lymphoid tissues, J. Nutr. 113, 1583–1590 (1983).
W. Tao, M. J. Corbett, and W. Pickett, Monomeric Bovine IgG2 is a potent stimulus for bovine neutrophils, J. Leukocyte Biol. 58, 203–208 (1995).
R. Boyne and J. R. Arthur, Effects of selenium and copper deficiency on neutrophil function in cattle, J. Comp. Pathol. 91, 271–276 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Cerone, S.I., Sansinanea, A.S., Streitenberger, S.A. et al. Cytochrome c oxidase, Cu,Zn-superoxide dismutase, and ceruloplasmin activities in copper-deficient bovines. Biol Trace Elem Res 73, 269–278 (2000). https://doi.org/10.1385/BTER:73:3:269
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1385/BTER:73:3:269