Hostname: page-component-cd9895bd7-fscjk Total loading time: 0 Render date: 2024-12-26T19:12:40.619Z Has data issue: false hasContentIssue false
  • English
  • Français

The genetic control of red cell glutathione deficiencies in Finnish Landrace and Tasmanian Merino sheep and in crosses between these breeds

Published online by Cambridge University Press:  27 March 2009

Elizabeth M. Tucker ,
L. Kilgour  and
J. D. Young
L. Kilgour
Affiliation:
A.R.C. Institute of Animal Physiology, Babraham, Cambridge CB2 4AT
J. D. Young
Affiliation:
A.R.C. Institute of Animal Physiology, Babraham, Cambridge CB2 4AT
Get access Rights & Permissions [Opens in a new window]

Summary

Finnish Landrace sheep with low red cell GSH concentrations resulting from a defective transport system for certain arnino acids were crossed with Tasmanian Merino sheep with a red cell GSH deficiency due to impaired activity of the enzyme γ-glutamyl cysteine synthetase. Inheritance data showed that the two types of GSH deficiency were under independent genetic control. In the Finnish Landrace breed, the gene coding for the transport defect (Trn) was inherited as an autosomal recessive and sheep homozygous for this gene had high red cell concentrations of lysine and ornithine (Ly ×) as well as low levels of GSH. In the Tasmanian Merino breed the GSH deficiency behaved as if controlled by an autosomal dominant gene (GSHL). Backcross breeding experiments resulted in lambs which had inherited both types of GSH deficiency. Evidence suggested that such ‘double low’ GSH lambs had an impaired viability. In Tasmanian Merinos the GSH deficiency was established prior to birth. Newborn Finnish Landrace lambs were clearly separable into two types on the basis of their red cell lysine and ornithine content but not on their GSH concentrations.

Type
Research Article
Information
The Journal of Agricultural Science , Volume 87 , Issue 2 , October 1976 , pp. 315 - 323
Copyright
Copyright © Cambridge University Press 1976

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., Duron, O. & Kelly, B. M. (1963). Improved method for the determination of blood glutathione. Journal of Laboratory and Clinical Medicine 61, 882–8.Google ScholarPubMed
Board, P. G., Roberts, J. & Evans, J. V. (1974). The genetic control of erythrocyte reduced glutathione in Australian Merino sheep. Journal of Agricultural Science, Cambridge 82, 395–8.CrossRefGoogle Scholar
Boivin, P. & Galand, C. (1965). La synthese du glutathion au cours de l'anémie hémolytique congénitale avec déficit en glutathion réduit. Nouvelle revue francaise d'hématologie 5, 707–20.Google Scholar
Eagleton, G. E., Hall, J. G. & Russell, W. S. (1970). An estimation of dominance at the locus controlling blood potassium in sheep. Animal Blood Groups and Biochemical Genetics 1, 135–43.CrossRefGoogle Scholar
Ellory, J. C, Tucker, E. M. & Deverson, E. V. (1972). The identification of ornithine and lysine at high concentrations in the red cells of sheep with an inherited deficiency of glutathione. Biochimica et biophysica acta 279, 481–3.CrossRefGoogle ScholarPubMed
Konrad, P. N., Richards, F., Valentine, W. N. & Paglia, D. E. (1972). γ-Glutamyl cysteine synthetase deficiency. A cause of hereditary hemolytio anaemia. New England Journal of Medicine 286, 557–61.CrossRefGoogle Scholar
Minnich, V., Smith, M. B., Brauner, M. J. & Majerus, P. W. (1971). Glutathione biosynthesis in human erythrocytes. 1. Identification of the enzymes of glutathione synthesis in hemolysates. Journal of Clinical Investigation 50, 507–13.CrossRefGoogle Scholar
Paniker, N. V. & Beutler, E. (1972). The effect of methylene blue and diaminodiphenylsulfone on red cell reduced glutathione synthesis. Journal of Laboratory and Clinical Medicine 80, 481–7.Google Scholar
Tucker, E. M. (1974). A shortened life span of sheep red cells with a glutathione deficiency. Research in Veterinary Science 16, 19–22.CrossRefGoogle ScholarPubMed
Tucker, E. M. (1975). The life span of glutathionedefioient red cells in Tasmanian Merino sheep. Research in Veterinary Science 19, 343–4.CrossRefGoogle ScholarPubMed
Tucker, E. M., Ellory, J. C. & Kilgour, L. (1973). Determinations of amino acid, cation and reduced glutathione levels in the red cells of Awassi sheep (Ovis aries). Comparative Biochemistry & Physiology 46A, 103–7.CrossRefGoogle Scholar
Tucker, E. M. & Kilgour, L. (1970). An inherited glutathione deficiency and a concomitant reduction in potassium concentration in sheep red cells. Experientia 26, 203–4.CrossRefGoogle Scholar
Tucker, E. M. & Kilgour, L. (1972). A glutathione deficiency in the red cells of certain Merino sheep. Journal of Agricultural Science, Cambridge 79, 515–16.CrossRefGoogle Scholar
Tucker, E. M. & Kilgour, L. (1973). The effect of anaemia on sheep with inherited differences in red cell reduced glutathione (GSH) concentrations. Research in Veterinary Science 14, 306–11.CrossRefGoogle ScholarPubMed
Young, J. D., Ellory, J. C. & Tucker, E. M. (1975). Amino acid transport defect in glutathione-deficient sheep erythrocytes. Nature 254, 156–7.CrossRefGoogle ScholarPubMed
Young, J. D., Ellory, J. C. & Tucker, E. M. (1976). Amino acid transport in normal and glutathionedeficient sheep erythrocytes. Biochemical Journal 154, 43–8.CrossRefGoogle ScholarPubMed
Young, J. D. & Nimmo, I. A. (1975). GSH biosynthesis in glutathione-deficient erythrocytes from Finnish Landrace and Tasmanian Merino sheep. Biochimica et biophysica acta 404, 132–41.CrossRefGoogle ScholarPubMed
Young, J. D., Nimmo, I. A. & 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 et biophysica acta 404, 124–31.CrossRefGoogle ScholarPubMed