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Cobalt–deficiency–induced hyperhomocysteinaemia and oxidative status of cattle

Published online by Cambridge University Press:  09 March 2007

G. I. Stangl*
Affiliation:
Institute of Nutrition Sciences, Technical University of Munich, 85350 Freising-Weihenstephan, Germany
F. J. Schwarz
Affiliation:
Institute of Nutrition Sciences, Technical University of Munich, 85350 Freising-Weihenstephan, Germany
B. Jahn
Affiliation:
Institute of Nutrition Sciences, Technical University of Munich, 85350 Freising-Weihenstephan, Germany
M. Kirchgessner
Affiliation:
Institute of Nutrition Sciences, Technical University of Munich, 85350 Freising-Weihenstephan, Germany
*
*Corresponding author: Dr Gabriele I. Stangl, fax +49 8161 715367, email [email protected]
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Abstract

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In ruminants, Co is required for the synthesis of vitamin B12, which in turn is needed for the resynthesis of methionine by methylation of homocysteine and thus, cobalamin deficiency may induce hyperhomocysteinaemia which is brought into context with perturbations of the antioxidative–prooxidative balance. The present study was conducted to explore whether Co deficiency in cattle is also associated with homocysteine-induced disturbances of oxidative status. Co deficiency was induced in cattle by feeding two groups of animals on either a basal maize-silage-based diet that was moderately low in Co (83 μg Co/kg DM), or the same diet supplemented with Co to a total of 200 μg Co/kg DM, for 43 weeks. Co deficiency was apparent from a reduced vitamin B12 status in serum and liver and an accumulation of homocysteine in plasma which was in excess of 4·8 times higher in Co-deprived cattle than in controls. The much increased level of circulating homocysteine did not indicate severe disturbances in antioxidant–prooxidant balance as measured by individual markers of lipid peroxidation, protein oxidation, and the antioxidative defence system. There were no quantitative difference in plasma thiol groups, nor were there significant changes in concentrations of α-tocopherol, microsomal thiobarbituric acid-reactive substances and carbonyl groups in liver. However, there was a trend toward increased plasma carbonyl levels indicating a slight degradation of plasma proteins in the hyperhomocysteinaemic cattle. Analysis of the hepatic catalase (EC 1.11.1.6) activity revealed an 11 % reduction in Co-deficient cattle relative to the controls. These results indicate that long-term moderate Co deficiency may induce a severe accumulation of plasma homocysteine in cattle, but considerable abnormalities in oxidative status failed to appear.

Type
Short communication
Copyright
Copyright © The Nutrition Society 2000

References

Aebi, H (1970) Catalase. In Methods of Enzymatic Analysis, pp. 636641 [Bergmeyer, HU, editor]. Weinheim: Verlag Chemie.Google Scholar
Balz, MK, Schulte, E & Thier, HP (1993) Simultaneous determination of α-tocopheryl acetate, tocopherols and tocotrienols by HPLC with fluorescence detection in foods. Fat Science Technology 95, 215220.Google Scholar
Blom, HJ, Kleinveld, HA, Boers, GH, Demacker, PNM, Hak-Lemmers, HLM, Pothoff, MTWB Te Poele & Trijebels, JMF (1995) Lipid peroxidation and susceptibility of low-density lipoprotein to in vitro oxidation in hyperhomocysteinaemia. European Journal of Clinical Investigation 25, 149154.CrossRefGoogle ScholarPubMed
Brown, JCW & Strain, JJ (1990) Effect of dietary homocysteine on copper status in rats. Journal of Nutrition 120, 10681074.CrossRefGoogle ScholarPubMed
Cao, G & Cutler, RG (1995) Difficulties in measuring reactive protein carbonyls in tissues using 2,4-dinitrophenylhydrazine. Archives of Biochemistry and Biophysics 320, 106114.CrossRefGoogle ScholarPubMed
Cohen, G, Dembiec, D & Marcus, J (1970) Measurement of catalase activity in tissue extracts. Analytical Biochemistry 34, 3038.CrossRefGoogle ScholarPubMed
Cornwell, PE, Morgan, SL & Vaughn, WH (1993) Modification of a high-performance liquid chromatographic method for assay of homocysteine in human plasma. Journal of Chromatography 617, 136139.CrossRefGoogle ScholarPubMed
Dudman, NP, Wilcken, DE & Stocker, R (1993) Circulating lipid hydroperoxide levels in human hyperhomocysteinemia. Relevance to development of arteriosclerosis. Arteriosclerosis and Thrombosis 13, 512516.CrossRefGoogle ScholarPubMed
Duncan, IF, Greentree, PL & Ellis, KJ (1986) Cobalt deficiency in cattle. Australian Veterinary Journal 63, 127128.CrossRefGoogle ScholarPubMed
Fukunaga, K, Suzuki, T & Takama, K (1993) Highly sensitive high-performance liquid chromatography for the measurement of malondialdehyde in biological samples. Journal of Chromatography 621, 7781.CrossRefGoogle ScholarPubMed
Guttormsen, AB, Schneede, J, Ueland, PM & Refsum, H (1996) Kinetics of total plasma homocysteine in subjects with hyperhomocysteinemia due to folate or cobalamine deficiency. American Journal of Clinical Nutrition 63, 194202.CrossRefGoogle ScholarPubMed
Hu, ML (1994) Measurement of protein thiol groups and glutathione in plasma. Methods in Enzymology 233, 380385.CrossRefGoogle ScholarPubMed
Kennedy, DG, Young, PB, Blanchflower, WJ, Scott, JM, Weir, DG, Molloy, AM & Kennedy, S (1994) Cobalt-vitamin B12 deficiency causes lipid accumulation, lipid peroxidation and decreased α-tocopherol concentrations in the liver of sheep. International Journal for Vitamin and Nutrition Research 64, 270276.Google ScholarPubMed
Mele, MC & Meucci, E (1996) Homocysteine and oxidative modifications of plasma proteins. Amino Acids (Vienna) 11, 99104.CrossRefGoogle ScholarPubMed
Musewe, VO & Gombe, S (1980) Plasma vitamin B12 and reproductive performance of cows on cobalt deficient pastures in the Rift Valley of Kenya. International Journal for Vitamin and Nutrition Research 50, 272282.Google ScholarPubMed
National Research Council (1996) Nutrient Requirements of Beef Cattle. Washington, DC: National Academy Press.Google Scholar
Preibisch, G, Küffner, C & Elstner, EF (1993) Biochemical model reactions on the prooxidative activity of homocysteine. Zeitschrift für Naturforschung 48c, 5862.CrossRefGoogle ScholarPubMed
Price, J, Ueno, S & Wood, SG (1993) Recent developments in the assay of plasma vitamin B12 in cattle. In Trace Elements in Man and Animals — TEMA 8, pp. 317318 [Anke, M, Meissner, D and Mills, CF, editors]. Gersdorf: Verlag Media Touristik.Google Scholar
Reznick, AZ & Packer, L (1994) Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods in Enzymology 233, 357363.CrossRefGoogle ScholarPubMed
Smith, K, Krohn, RJ, Hermanson, GT, Mallia, AK, Garnter, FH, Provenzano, MD, Fujimoto, EK, Goeke, M, Olson, BJ & Klenk, DC (1975) Measurement of protein using bicinchoninic acid. Analytical Biochemistry 150, 7685.CrossRefGoogle Scholar
Stangl, GI, Schwarz, FJ & Kirchgessner, M (1999) Cobalt deficiency effects on trace elements, hormones and enzymes involved in energy metabolism of cattle. International Journal for Vitamin and Nutrition Research 69, 120126.CrossRefGoogle ScholarPubMed
Ubbink, JB, Vermaak, WJH & Bissbort, S (1991) Rapid high-performance liquid chromatographic assay for total homocysteine levels in human serum. Journal of Chromatography 565, 441446.CrossRefGoogle ScholarPubMed
Ueland, PM, Mansoor, MA, Guttormsen, AB, Muller, F, Aukrust, P, Pefsum, H & Svardal, AM (1996) Reduced, oxidized and protein-bound forms of homocysteine and other aminothiols in plasma comprise the redox thiol status — a possible element of the extracellular antioxidant defense system. Journal of Nutrition 126, 1281S1284S.CrossRefGoogle ScholarPubMed
Van Der Westhuyzen, J, Van Tonder, SV, Gibson, JE, Kilroe-Smith, TA & Metz, J (1985) Plasma amino acids and tissue methionine levels in fruit bats (Rousettus aegyptiacus) with nitrous oxide-induced vitamin B12 deficiency. British Journal of Nutrition 53, 657662.CrossRefGoogle ScholarPubMed
Young, PB, Kennedy, S, Molloy, AM, Scott, JM, Weir, DG & Kennedy, DG (1997) Lipid peroxidation induced in vivo by hyperhomocysteinaemia in pigs. Atherosclerosis 129, 6771.CrossRefGoogle ScholarPubMed