Hostname: page-component-cd9895bd7-dzt6s Total loading time: 0 Render date: 2024-12-24T13:00:41.676Z Has data issue: false hasContentIssue false
  • English
  • Français

Ontogenic changes in hepatic glutathione and metallothionein in rats and the effect of a low-sulphur-containing diet

Published online by Cambridge University Press:  09 March 2007

Misako Taniguchi  and
M. George Cherian
Misako Taniguchi
Affiliation:
Department of Food and Nutrition, Nakamura Gakuen College, Jonan-Ku, Fukuoka 814, Japan
M. George Cherian
Affiliation:
Department of Pathology, University of Western Ontario, London, Ontario N6A 5C1, Canada
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Metallothionein contains about 30% cysteine and is a major protein in newborn rat liver. This protein and glutathione constitute two major intracellular cysteine pools in newborn rat liver. When pregnant rats were fed on a soya-bean-protein diet, low in sulphur amino acids, the hepatic glutathione levels of the dams were decreased. However, this did not affect the levels of glutathione or metallothionein in the pups. The activity of the glutathione-degrading enzyme γ-glutamyltransferase (EC 2.3.2.2) in the livers of pups was maximum at birth and gradually decreased with age when the hepatic glutathione was transported to the kidney. In the pups born from dams fed on soya-bean-protein diet the decline in the hepatic enzyme activity was delayed, suggesting a continued degradation of glutathione in the liver. These results suggest that even with a maternal nutritional deficiency of sulphur amino acids, the transfer of cysteine to the fetus is not impaired. However, the hepatic intra-organ degradation of glutathione is continued in these pups for a prolonged period after birth compared with pups born from control mothers. The increased degradation of glutathione in the liver may be essential to meet the requirement of cysteine in pups born from dams fed on the soya-bean-protein diet.

Keywords

GlutathioneMetallothioneinSulphur metabolismRat
Type
Mineral Nutrition
Information
British Journal of Nutrition , Volume 63 , Issue 1 , January 1990 , pp. 97 - 103
Copyright
Copyright © The Nutrition Society 1990

References

REFERENCES

Andrews, G., Gallant, K.R. & Cherian, M.G. (1987). Regulation of the ontogeny of rat liver metallothionein mRNA by zinc. European Journal of Biochemistry 166, 527–531.CrossRefGoogle ScholarPubMed
Bell, J.U. (1979). Native metallothionein levels in rat hepatic cytosol during perinatal development. Toxicology and Applied Pharmacology 50, 101–107.CrossRefGoogle ScholarPubMed
Curthoys, N.P. (1986). Interorgan flux of glutathione. Federation Proceedings, 45, 2166–2169.Google Scholar
Gallant, K.R. & Cherian, M.G. (1986). Influence of maternal mineral deficiency on the hepatic metallothionein and zinc in newborn rats. Biochemistry and Cell Biology 64, 8–12.CrossRefGoogle ScholarPubMed
Gaull, G., Sturman, J.A. & Räihä, N.C.R. (1972). Development of mammalian sulfur metabolism: Absence of cystathionase in human fetal tissues. Pediatric Research 6, 538–547.CrossRefGoogle ScholarPubMed
Heinonen, K. (1973). Studies on cystathionase activity in rat liver and brain during development. Biochemistry Journal 136, 1011–1015.CrossRefGoogle ScholarPubMed
Higashi, T. & Tateishi, N. (1978). Physiological significance of elevation of liver γ-glutamyltranspeptidase in late pregnancy. In Function of Glutathione in Liver and Kidney, pp. 22–26 [Sies, H. and Wendel, A., editors]. Amsterdam: Springer.CrossRefGoogle Scholar
Inoue, M. & Morino, Y. (1981). Inactivation of renal γ-glutamyltransferase by 6-diazo-5 oxo-L-nonleucyl glycine, an inactive precursor of affinity labelling reagent inactivates γ-glutamyltransferase. Proceedings of the National Academy of Sciences, USA 78, 46–49.CrossRefGoogle Scholar
Inoue, M., Shinozuka, S. & Morino, Y. (1986). Mechanism of renal peritubular extraction of plasma glutathione. European Journal of Biochemistry 157, 605–609.CrossRefGoogle ScholarPubMed
Kaplowitz, N., Aw, T.Y. & Ookhtens, M. (1985). The regulation of hepatic glutathione. Annual Review of Pharmacology and Toxicology 25, 715–744.CrossRefGoogle ScholarPubMed
Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
McIntyre, T.M. & Curthoys, N.P. (1979). Comparison of the hydrolytic and transfer activities of rat renal γ-glutamyl-transpeptidase. Journal of Biological Chemistry 254, 6499–6504.CrossRefGoogle Scholar
Meister, A. & Anderson, M.E. (1983). Glutathione. Annual Review of Biochemistry 52, 711–760.CrossRefGoogle ScholarPubMed
Onosaka, S. & Cherian, M.G. (1982). Comparison of metallothionein determination by polarographic and cadmium saturation methods. Toxicology and Applied Pharmacology 63, 270–274.CrossRefGoogle ScholarPubMed
Panemangalore, M., Banerjee, D., Onosaka, S. & Cherian, M.G. (1983). Changes in the intracellular accumulation and distribution of metallothionein in rat liver and kidney during postnatal development. Developmental Biology 97, 95–102.CrossRefGoogle ScholarPubMed
Rogers, Q.R. & Harper, A.E. (1965). Amino acid diets and maximal growth in the rat. Journal of Nutrition 87, 267–273.CrossRefGoogle ScholarPubMed
Sakamoto, Y., Higashi, T. & Tateishi, N. (1983). Factors involved in the appearance and switch-off of hepatic γ-glutamyl transpeptidase. Gann Monograph on Cancer Research 29, 281–288.Google Scholar
States, B., Foreman, J.W. & Segal, S. (1987). Cysteine and glutathione levels in developing rat kidney and liver. Pediatric Research 22, 605–608.CrossRefGoogle ScholarPubMed
Szasz, G. (1969). A kinetic photometric method for serum γ-glutamyl-transpeptidase. Clinical Chemistry 15, 124–136.CrossRefGoogle ScholarPubMed
Taniguchi, M. & Inoue, M. (1986). Ontogenic changes in metabolism and transport of glutathione in the rat. Journal of Biochemistry 100, 1457–1463.CrossRefGoogle ScholarPubMed
Tateishi, N., Higashi, T., Naruse, A., Nakashima, K., Shiozaki, H. & Sakamoto, Y. (1977). Rat liver glutathione: Possible role as a reservoir of cysteine. Journal of Nutrition 107, 51–60.CrossRefGoogle ScholarPubMed
Tateishi, N., Higashi, T., Shinya, S., Naruse, A. & Sakamoto, Y. (1974). Studies on the regulation of glutathione level in rat liver. Journal of Biochemistry 75, 93–104.CrossRefGoogle ScholarPubMed
Templeton, D.M., Banerjee, D. & Cherian, M.G. (1985). Metallothionein synthesis and localization in relation to metal storage in rat liver during gestation. Canadian Journal of Biochemistry and Cell Biology 63, 16–22.CrossRefGoogle ScholarPubMed
Tietze, F. (1969). Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Analytical Biochemistry 27, 502–522.CrossRefGoogle ScholarPubMed
Wong, K. & Klaassen, C.D. (1979). Isolation and characterization of metallothionein which is highly concentrated in newborn rat liver. Journal of Biological Chemistry 254, 12399–12403.CrossRefGoogle ScholarPubMed
Zlotkin, S.H. & Anderson, G.H. (1982). The development of cystathionase activity during the first year of life. Pediatric Research 16, 65–68.CrossRefGoogle ScholarPubMed