Skip to main content
SpringerLink
Log in

Effects of CO2 exposure on distribution of various forms of iron and copper in guinea-pig tissues

  • Full Papers
  • Published:
Experientia Aims and scope Submit manuscript

Summary

The effects on iron and copper distribution and metabolism of exposure to high levels of CO2 were studied in the guinea-pig. Mature, male animals were placed in an atmosphere of 15% CO2, 21% O2 (balance N2), and sacrificed from 1 h to 1 week thereafter. Total iron and copper concentrations of blood, liver, spleen and bone, as well as concentrations of heme and ferritin iron, were measured together with blood hematocrit, reticulocytes, plasma hemoglobin, plasma ceruloplasmin and copper concentrations. The results show clearly that rapid and sustained red cell damage or hemolysis ensued several h from the start of CO2 treatment. This resulted in loss of iron and copper from the blood, an influx of both elements into liver, spleen and bone, and a rise in plasma ceruloplasmin. Influx of iron into liver and spleen caused an accumulation of ferritin, the main site for iron storage in cells. Following the effect on red cells, there was an accumulation of heme iron, and a decreased hematocrit, best explained by a depressed activity of the reticuloendothelial and erythropoietic systems. A period of adaptation succeeded these events, in which all blood parameters and most tissue values returned to normal, despite the continuing presence of high CO2. The only changes not reversed were the elevations in liver, spleen and bone iron stores. These remained high, with a net accumulation of >2 mg iron, or 3–4 times more than originally present. The results indicate that at least in the guinea-pig, high CO2 exposure results in red cell damage and other events leading to an accumulation of additional iron in the body; also, that iron accumulated as ferritin and hemosiderin in liver and spleen may not be readily available to restore blood hemoglobin concentrations on an acute basis.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Baker, G.T., and Schaefer, K.E., Effect of chronic hypercapnia on blood volume, plasma volume and red cell volume. Naval Submarine Med. Res. Lab. report No. 604, 1969.

  2. Cook, J.D., Hershko, C., and Finch, C.A.: Storage iron kinetics. V. Iron exchange in the rat. Br. J. Haemat.25 (1973) 691–705.

    Article  Google Scholar 

  3. Cook, J.D., Hershko, H., and Finch, C.A., Storage iron kinetics. IV. The effect of inflammation on iron exchange in the rat. Br. J. Haemat.28 (1974) 67–75.

    Article  Google Scholar 

  4. Dacie, J.V., and Lewis, S., Practical hematology, 4th edn. Grune and Stratton, New York 1968.

    Google Scholar 

  5. Davidson, J., and Henry, J.B., eds. Clinical diagnosis through laboratory methods, 15th edn. p. 178. Todd and Stanford, 1974.

  6. Faura, J., and Gurney, C.W., The effect of carbon dioxide on erythropoiesis. Ann. N.Y. Acad. Sci.149 (1968) 456–461.

    Article  CAS  PubMed  Google Scholar 

  7. Giorgio, A.J., Cartwright, G.E., and Wintrobe, M.M. Determination of urinary copper by means of direct extraction with zinc dibenzyldithiocarbamate. Am. J. clin. Path.41 (1964) 22–36.

    Article  CAS  PubMed  Google Scholar 

  8. Haskins, D., Stevens, Jr, A.R., Finch, S., and Finch, C.A., Iron metabolsim. Iron stores in man as measured by phlebotomy. J. clin. Invest.31, (1952), 543–557.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. Hershko, C., Cook, J.D., and Finch, C.A., Storage iron kinetics. VI. The effect of inflammation on iron exchange in the rat. Br. J. Haemat.28 (1974) 67–75.

    Article  CAS  Google Scholar 

  10. Houchin, O.B., A rapid colorimetric method for quantitative determination of copper oxidase activity (ceruloplasmin). Clin. Chem.4 (1958) 519–523.

    Article  CAS  PubMed  Google Scholar 

  11. Levine, W.G., and Peisach, J., Ethylene diamine tetraacetate, iron and ceruloplasmin activity. Biochim. biophys. Acta77 (1963) 602–614.

    Article  CAS  Google Scholar 

  12. Linder, M.C., Hixon, T., and Gonzalez, R., Distribution of copper among components of human serum in normal subjects and patients with cancer. Fedn Proc. Abstr42 (1983) 670.

    Google Scholar 

  13. Linder, M.C., Houle, P.A., Isaacs, E., Moor, J.R., and Scott, L.E., Copper regulation of ceruloplasmin in copper-deficient rats. Enzyme24 (1979) 23–35.

    Article  CAS  PubMed  Google Scholar 

  14. Linder, M.C., and Munro, H.N., Assay of tissue ferritin. Analyt. Biochem.48 (1973) 266–278.

    Article  Google Scholar 

  15. Linder, M.C., and Munro, H.N., Iron and copper metabolism during development. Enzyme15 (1973), 111–138.

    CAS  PubMed  Google Scholar 

  16. Linder, M.C., and Munro, H.N., The mechanism of iron absorption and its regulation. Fedn Proc.36 (1977) 2017–2023.

    CAS  Google Scholar 

  17. Linder-Horowitz, M., Ruettinger, R.T., and Munro, H.N., Iron induction of electrophoretically different ferritins in rat liver, heart and kidney. Biochim. biophys. Acta200 (1970) 442–448.

    Article  CAS  PubMed  Google Scholar 

  18. Matrone, G., Interrelationships of iron and copper in the nutrition and metabolism of animals. Fedn Proc.19 (1960) 659–665.

    CAS  Google Scholar 

  19. Munro, H.N., and Linder, M.C., Ferritin: structure, biosyn-thesis and role in iron metabolism. Physiol. Rev.58 (1978) 317–396.

    Article  CAS  PubMed  Google Scholar 

  20. Noyes, W.D., Bothwell, T.H., and Finch, C.A., The role of the reticuloendothelial cell in iron metabolism. Br. J. Haemat.6 (1960) 43–55.

    Article  CAS  Google Scholar 

  21. Osaki, S., and Johnson, D.A., Mobilization of liver iron by ferroxidase (ceruloplasmin). J. biol. Chem.241 (1969) 5053–5059.

    Article  Google Scholar 

  22. Owen, Jr, C.A., Effects of iron on copper metabolism and copper on iron metabolism. Am. J. Physiol.224 (1973) 514–518.

    Article  CAS  PubMed  Google Scholar 

  23. Ragan, H.A., Nacht, S., Lee, G.R., Bishop, C.R., and Cartwright, G.E., Effect of ceruloplasmin on plasma iron in copper deficient swine. Am. J. Physiol.217 (1969) 1320–1323.

    Article  CAS  PubMed  Google Scholar 

  24. Ravin, H.A., An improved colorimetric enzymatic assay of ceruloplasmin. J. Lab. clin. Med.58 (1961) 161–168.

    CAS  PubMed  Google Scholar 

  25. Rice, E.W., Standardization of ceruloplasmin activity in terms of International Units. Oxidative formation of Bandrowski's base from p-phenylenediamine by ceruloplasmin. Analyt. Biochem.3 (1962) 452–456.

    Article  CAS  PubMed  Google Scholar 

  26. Roeser, H.P., Nikles, A., and Cham, B.E., Effects of ascorbic acid deficiency on ferritin turnover; in The biochemistry and physiology of iron, pp. 385–393. Eds P. Saltman and J. Hegenaur. Elsevier North-Holland, New York 1982.

    Google Scholar 

  27. Schaefer, K.E., Metabolic aspects of adaptation to carbon dioxide; in: Carbon dioxide and metabolic regulation, pp. 253–265. Eds H. Nahas and K.E. Schaefer. Springer Verlag, New York 1974.

    Chapter  Google Scholar 

  28. Schaefer, K.E., and Baker, G.T., Effects of chronic hypercapnia on blood distribution in organs. Naval Submarine Med. Res. Lab. Report No. 603, 1969.

  29. Schaefer, K.E., Messier, A.A., and Morgan, C.C., Displacement of oxygen dissociation curves and red cell cation exchange in chronic hypercapnia. Respir. Physiol.10, (1970) 299–312.

    Article  CAS  PubMed  Google Scholar 

  30. Siimes, M.A., and Dallman, P.R., New kinetic role for serum ferritin in iron metabolism. Br. J. Haemat.28 (1974) 7–18.

    Article  CAS  Google Scholar 

  31. Van Wyk, C.P., Linder-Horowitz, M., and Munro, H.N., The effect of iron loading on non-heme iron compounds in different liver cell populations. J. biol. Chem.246 (1970) 1025–1031.

    Google Scholar 

  32. Wixon, R.L., Prutkin, L., and Munro, H.N., Hemosiderin: Nature, formation and sign, Int. Rev. exp. Path.22 (1980) 193–225.

    Google Scholar 

  33. Zähringer, J., Baliga, B.S., and Munro, H.N., Novel mechanism for translational control in regulation of ferritin synthesis by iron. Proc. natl Acad. Sci. USA73 (1976) 857–861.

    Article  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Author notes

  1. Maria C. Linder

    Present address: Department of Chemistry, California State University, 92634, Fullerton, California, USA

Authors and Affiliations

  1. Naval Submarine Medical Research Laboratory, Naval Submarine Base, 06340, Groton, Connecticut, USA

    Karl E. Schaefer & Maria C. Linder

  2. Department of Nutrition and Food Science, Massachusetts Institute of Technology, 02139, Cambridge, Massachusetts, USA

    Karl E. Schaefer & Maria C. Linder

Authors
  1. Karl E. Schaefer
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Maria C. Linder
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Acknowledgments. We gratefully acknowledge the technical assistance of Joan R. Moor and Lakshmi Vulimiri with these studies, and the support of Grants No. 17249 and HL22410 from the U.S. Public Health Service.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schaefer, K.E., Linder, M.C. Effects of CO2 exposure on distribution of various forms of iron and copper in guinea-pig tissues. Experientia 39, 850–855 (1983). https://doi.org/10.1007/BF01990402

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01990402

Keywords

Search

Navigation