Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 Sep 15;174(3):883–892. doi: 10.1042/bj1740883

Effect of zinc status of rats on the synthesis and degradation of copper-induced metallothioneins.

I Bremner, G Hoekstra, N T Davies, B W Young
PMCID: PMC1185993  PMID: 728094

Abstract

Injection of Zn2+-adequate and Zn2+-deficient rats with Cu2+ stimulated the incorporation of l-[35S]cysteine into a low-molecular-weight Cu2+-binding protein in both liver and kidney. No significant incorporation of l-[4,5-3H]leucine into this protein occurred, confirming the previous claim that it was metallothionein and not some other leucine-rich protein. The half-life of the protein was found to be 16.9 +/- 1.0 (S.E.)h in the liver of Zn2+-adequate rats but only 12.3 +/- 0.5h in Zn2+-deficient animals. The degradation rate of the metallothionein was similar to the rate of disappearance of Cu2+ and Zn2+ from the protein, indicating that the release of mental from the protein and its catabolism occurred simultaneously. There was no significant difference in the half-lives of the hepatic or renal copper-thioneins in Zn2+-adequate rats.

Full text

PDF
884

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bloomer L. C., Sourkes T. L. The effect of copper loading on the distribution of copper in rat liver cytosol. Biochem Med. 1973 Aug;8(1):78–91. doi: 10.1016/0006-2944(73)90011-2. [DOI] [PubMed] [Google Scholar]
  2. Bremner I., Davies N. T. Studies on the appearance of a hepatic copper-binding protein in normal and zinc-deficient rats. Br J Nutr. 1976 Jul;36(1):101–112. doi: 10.1079/bjn19760061. [DOI] [PubMed] [Google Scholar]
  3. Bremner I., Davies N. T. The induction of metallothionein in rat liver by zinc injection and restriction of food intake. Biochem J. 1975 Sep;149(3):733–738. doi: 10.1042/bj1490733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bremner I. The relationship between the zinc status of pigs and the occurrence of copper- and Zn-binding proteins in liver. Br J Nutr. 1976 Mar;35(2):245–252. doi: 10.1079/bjn19760028. [DOI] [PubMed] [Google Scholar]
  5. Bremner I., Young B. W. Copper thionein in the kidneys of copper-poisoned sheep. Chem Biol Interact. 1977 Oct;19(1):13–23. doi: 10.1016/0009-2797(77)90039-4. [DOI] [PubMed] [Google Scholar]
  6. Bremner I., Young B. W. Isolation of (copper, zinc)-thioneins from the livers of copper-injected rats. Biochem J. 1976 Aug 1;157(2):517–520. doi: 10.1042/bj1570517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bremner I., Young B. W. Isolation of (copper, zinc-) thioneins from pig liver. Biochem J. 1976 Jun 1;155(3):631–635. doi: 10.1042/bj1550631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Böhlen P., Stein S., Dairman W., Udenfriend S. Fluorometric assay of proteins in the nanogram range. Arch Biochem Biophys. 1973 Mar;155(1):213–220. doi: 10.1016/s0003-9861(73)80023-2. [DOI] [PubMed] [Google Scholar]
  9. Chen R. W., Whanger P. D., Weswig P. H. Biological function of metallothionein. I. Synthesis and degradation of rat liver metallothionein. Biochem Med. 1975 Feb;12(2):95–105. doi: 10.1016/0006-2944(75)90100-3. [DOI] [PubMed] [Google Scholar]
  10. Chvapil M. New aspects in the biological role of zinc: a stabilizer of macromolecules and biological membranes. Life Sci. 1973 Oct 16;13(8):1041–1049. doi: 10.1016/0024-3205(73)90372-x. [DOI] [PubMed] [Google Scholar]
  11. Drum D. E., Harrison J. H., 4th, Li T. K., Bethune J. L., Vallee B. L. Structural and functional zinc in horse liver alcohol dehydrogenase. Proc Natl Acad Sci U S A. 1967 May;57(5):1434–1440. doi: 10.1073/pnas.57.5.1434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Drysdale J. W., Munro H. N. Regulation of synthesis and turnover of ferritin in rat liver. J Biol Chem. 1966 Aug 10;241(15):3630–3637. [PubMed] [Google Scholar]
  13. Evans G. W. Copper homeostasis in the mammalian system. Physiol Rev. 1973 Jul;53(3):535–570. doi: 10.1152/physrev.1973.53.3.535. [DOI] [PubMed] [Google Scholar]
  14. Feldman S. L., Cousins R. J. Degradation of hepatic zinc-thionein after parenteral zinc administration. Biochem J. 1976 Dec 15;160(3):583–588. doi: 10.1042/bj1600583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Glass R. D., Doyle D. On the measurement of protein turnover in animal cells. J Biol Chem. 1972 Aug 25;247(16):5234–5242. [PubMed] [Google Scholar]
  16. Goldberg A. L., Dice J. F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem. 1974;43(0):835–869. doi: 10.1146/annurev.bi.43.070174.004155. [DOI] [PubMed] [Google Scholar]
  17. Hartmann H. J., Weser U. Copper-thionein from fetal bovine liver. Biochim Biophys Acta. 1977 Mar 28;491(1):211–222. doi: 10.1016/0005-2795(77)90057-5. [DOI] [PubMed] [Google Scholar]
  18. Irons R. D., Smith J. C. Isolation of a non-thionein copper-binding protein from liver of copper-injected rats. Chem Biol Interact. 1977 Jul;18(1):83–89. doi: 10.1016/0009-2797(77)90143-0. [DOI] [PubMed] [Google Scholar]
  19. Madapallimatam G., Riordan J. R. Antibodies to low molecular weight copper binding protein from liver. Biochem Biophys Res Commun. 1977 Aug 22;77(4):1286–1293. doi: 10.1016/s0006-291x(77)80119-8. [DOI] [PubMed] [Google Scholar]
  20. PISCATOR M. OM KADMIUM I NORMALA MAENNISKONJURAR SAMT REDOGOERELSE FOER ISOLERING AV METALLOTHIONEIN UR LEVER FRAN KADMIUMEXPONERADE KANINER. Nord Hyg Tidskr. 1964;45:76–82. [PubMed] [Google Scholar]
  21. Premakumar R., Winge D. R., Wiley R. D., Rajagopalan K. V. Copper-induced synthesis of copper-chelatin in rat liver. Arch Biochem Biophys. 1975 Sep;170(1):267–277. doi: 10.1016/0003-9861(75)90117-4. [DOI] [PubMed] [Google Scholar]
  22. Richards M. P., Cousins R. J. Influence of parenteral zinc and actinomycin D on tissue zinc uptake and the synthesis of a zinc - binding protein. Bioinorg Chem. 1975 Apr;4(3):215–224. doi: 10.1016/s0006-3061(00)80104-0. [DOI] [PubMed] [Google Scholar]
  23. Richards M. P., Cousins R. J. Metallothionein and its relationship to the metabolism of dietary zinc in rats. J Nutr. 1976 Nov;106(11):1591–1599. doi: 10.1093/jn/106.11.1591. [DOI] [PubMed] [Google Scholar]
  24. Riordan J. R., Gower I. Purification of low molecular weight copper proteins from copper loaded liver. Biochem Biophys Res Commun. 1975 Sep 16;66(2):678–686. doi: 10.1016/0006-291x(75)90563-x. [DOI] [PubMed] [Google Scholar]
  25. Shaikh Z. A., Smith J. C. The biosynthesis of metallothionein rat liver and kidney after administration of cadmium. Chem Biol Interact. 1976 Dec;15(4):327–336. doi: 10.1016/0009-2797(76)90138-1. [DOI] [PubMed] [Google Scholar]
  26. Williams R. B., Mills C. F. The experimental production of zinc deficiency in the rat. Br J Nutr. 1970 Dec;24(4):989–1003. doi: 10.1079/bjn19700102. [DOI] [PubMed] [Google Scholar]
  27. Winge D. R., Premakumar R., Wiley R. D., Rajagopalan K. V. Copper-chelatin: purification and properties of a copper-binding protein from rat liver. Arch Biochem Biophys. 1975 Sep;170(1):253–266. doi: 10.1016/0003-9861(75)90116-2. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES