Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-19T12:32:29.587Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of blood glutathione status on the susceptibility of sheep to haemolytic anaemia induced by the brassica anti-metabolite, dimethyl disulphide

Published online by Cambridge University Press:  02 September 2010

A. J. Duncan ,
B. Roncin  and
D. A. Elston
A. J. Duncan
Affiliation:
Macaulay Land Use Research Institute, Craigiebuckler, Aberdeen AB9 2QJ
B. Roncin
Affiliation:
Ecole Superieure d'Agriculture, 55 Rue Rabelais BP 748, 49007 Angers, Cedex, France
D. A. Elston
Affiliation:
Scottish Agricultural Statistics Service, Craigiebuckler, Aberdeen AB9 2QJ
Get access

Abstract

The effect of erythrocyte glutathione status and breed on the susceptibility of adult female sheep to the haemolytic anaemia caused by the brassica anti-metabolite dimethyl disulphide (DMDS) was determined in a factorial experiment. Within each breed (Scottish Blackface or Finnish Landrace), six sheep of low glutathione status (<30 mg/100 ml red blood cells (RBC)) and six sheep of high glutathione status (>70 mg/100 ml RBC) were dosed twice daily with DMDS for 35 days (25 mmol per head per day). All sheep developed a classic haemolytic anaemia within 2 weeks of the start of DMDS dosing. Weekly haemoglobin concentrations and packed cell volume values were not affected by breed or glutathione status. Heinz body numbers rose to a higher maximum in low glutathione animals but were not affected by breed. The results call into question the relationship between total erythrocyte glutathione concentration and the resistance of erythrocytes to oxidative damage.

Keywords

glutathionehaemolytic anaemiaHeinz bodiesoxidantssheep
Type
Research Article
Information
Animal Science , Volume 60 , Issue 1 , February 1995 , pp. 93 - 98
Copyright
Copyright © British Society of Animal Science 1995

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Beutler, E., Duran, O. and Kelly, B. M. 1963. Improved method for the determination of blood glutathione. Journal of Laboratory and Clinical Medicine 61: 882–888.Google ScholarPubMed
Duncan, A. J. and Milne, J. A. 1993. Effects of oral administration of Brassica secondary metabolites, allyl cyanide, allyl isothiocyanate and dimethyl disulphide on the voluntary food intake and metabolism of sheep. British lournal of Nutrition 70: 631–645.CrossRefGoogle ScholarPubMed
Eaton, J. W., Hallaway, P. E. and Agar, N. S. 1994. Erythrocyte glutathione: an indispensable defense? In Progress in clinical and biological research. The red cell: seventh Ann Arbor conference. pp. 23–38. Alan R. Liss, Inc.Google Scholar
French, J. K., Winterbourn, C. C. and Carrell, R. W. 1978. Mechanism of oxyhaemoglobin breakdown on reaction with acetyl phenylhydrazine. Biochemical journal 173: 19–26.CrossRefGoogle Scholar
Goto, I., Agar, N. S. and Maede, Y. 1993. Relation between reduced glutathione content and Heinz body formation in sheep erythrocytes. American journal of Veterinary Research 54: 622–626.CrossRefGoogle ScholarPubMed
Greenhalgh, J. F. D., Sharman, G. A. M. and Aitken, J. N. 1969. Kale anaemia. I. The toxicity to various species of animal of three types of kale. Research in Veterinary Science 10: 64–72.CrossRefGoogle ScholarPubMed
Lawes Agricultural Trust. 1993. Genstat 5, release 2.2. Rothamsted Experimental Station, Harpenden.Google Scholar
McKenna, R., Kezdy, F. J. and Epps, D. E. 1991. Kinetic-analysis of the free-radical-induced lipid-peroxidation in human erythrocyte-membranes — evaluation of potential antioxidants using cis-parinaric acid to monitor peroxidation. Analytical Biochemistry 196: 443–450.CrossRefGoogle ScholarPubMed
McPhail, D. B., Morrice, P. C. and Duthie, G. G. 1993. Adaptation of the blood antioxidant defence mechanisms of sheep with a genetic lesion resulting in low red cell glutathione concentrations. Free Radical Research Communications 18: 177–181.CrossRefGoogle ScholarPubMed
McPhail, D. B. and Sibbald, A. M. 1992. The rôle of free radicals in brassica-induced anaemia of sheep: an ESR spin trapping study. Free Radical Research Communications 16: 277–284.CrossRefGoogle ScholarPubMed
Smith, R. H. 1974. Kale poisoning. Report of the Rowett Research Institute 30:112–131.Google Scholar
Steven, F. S., Griffin, M. M. and Smith, R. H. 1981. Disulphide exchange reactions in the control of enzymic activity. Evidence for the participation of dimethyl disulphide in exchanges. European Journal of Biochemistry 119: 75–78.CrossRefGoogle ScholarPubMed
Tucker, E. M., Kilgour, L. and Young, J. D. 1976. The genetic control of red cell glutathione deficiencies in Finnish Landrace and Tasmanian Merino sheep and in crosses between these breeds. Journal of Agricultural Science, Cambridge 87: 315–323.CrossRefGoogle Scholar
Tucker, E. M. and Kilgour, L. 1973. The effect of anaemia on sheep with inherited differences in red cell reduced glutathione (GSH) concentrations. Research in Veterinary Science 14: 306–311.CrossRefGoogle ScholarPubMed
Yamoto, O. and Maede, Y. 1992. Susceptibility to onion-induced haemolysis in dogs with hereditary high erythrocyte reduced glutathione and potassium concentrations. American Journal of Veterinary Research 53: 134–137.CrossRefGoogle ScholarPubMed
Young, J. D., Nimmo, I. A. and Hall, J. G. 1975. The relationship between GSH, GSSG and non-GSH thiol in GSH deficient erythrocytes from Finnish Landrace and Tasmanian Merino sheep. Biochimica el Biophysica Ada 404: 124–131.CrossRefGoogle ScholarPubMed
Young, J. D. and Tucker, E. M. 1983. Erythrocyte glutathione deficiency in sheep. In Functions of glutathione: physiological, toxicological and clinical aspects (ed. Larsson, A., Orrenius, S., Holmgren, A., Mannervik, B.), pp. 373–384. Raven Press, New York.Google Scholar