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. 1990 Feb 15;266(1):213–219. doi: 10.1042/bj2660213

Expression of extracellular superoxide dismutase by human cell lines.

S L Marklund 1
PMCID: PMC1131117  PMID: 2106874

Abstract

Extracellular superoxide dismutase (EC-SOD) is the major SOD isoenzyme in extracellular fluids, but occurs also in tissues. The sites and characteristics of the synthesis of the enzyme are unknown. The occurrence of EC-SOD in cultures of a large panel of human cell lines was assayed by means of an e.l.i.s.a. Unlike the situation for the intracellular isoenzymes CuZn-SOD and Mn-SOD, expression of EC-SOD occurs in only a few cell types. None of the ten investigated suspension-growing cell lines produced EC-SOD. Among normal diploid anchorage-dependent cell lines, expression was found in all 25 investigated fibroblast cell lines, in the two glia-cell lines, but not in six endothelial-cell lines, two epithelial-cell lines or in two amnion-derived lines. Among neoplastic anchorage-dependent cell lines expression was found in 13 out of 29. EC-SOD was secreted into the culture medium by cell lines expressing the enzyme. The rate of EC-SOD synthesis varied by nearly 100-fold among the fibroblast lines and remained essentially constant in the individual lines during long-term culture. In the nine investigated cases, the secreted EC-SOD was of the high-heparin-affinity C type. It is suggested that tissue EC-SOD is secreted by a few well-dispersed cell types, such as fibroblasts and glia cells, to diffuse subsequently around and reversibly bind to heparan sulphate proteoglycan ligands in the glycocalyx of the surface of most tissue cell types and in the interstitial matrix.

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Selected References

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

  1. Adachi T., Marklund S. L. Interactions between human extracellular superoxide dismutase C and sulfated polysaccharides. J Biol Chem. 1989 May 25;264(15):8537–8541. [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Hjalmarsson K., Marklund S. L., Engström A., Edlund T. Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6340–6344. doi: 10.1073/pnas.84.18.6340. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Karlsson K., Lindahl U., Marklund S. L. Binding of human extracellular superoxide dismutase C to sulphated glycosaminoglycans. Biochem J. 1988 Nov 15;256(1):29–33. doi: 10.1042/bj2560029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Karlsson K., Marklund S. L. Binding of human extracellular-superoxide dismutase C to cultured cell lines and to blood cells. Lab Invest. 1989 May;60(5):659–666. [PubMed] [Google Scholar]
  6. Karlsson K., Marklund S. L. Extracellular superoxide dismutase in the vascular system of mammals. Biochem J. 1988 Oct 1;255(1):223–228. [PMC free article] [PubMed] [Google Scholar]
  7. Karlsson K., Marklund S. L. Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem J. 1987 Feb 15;242(1):55–59. doi: 10.1042/bj2420055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Karlsson K., Marklund S. L. Plasma clearance of human extracellular-superoxide dismutase C in rabbits. J Clin Invest. 1988 Sep;82(3):762–766. doi: 10.1172/JCI113676. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Marklund S. L., Bjelle A., Elmqvist L. G. Superoxide dismutase isoenzymes of the synovial fluid in rheumatoid arthritis and in reactive arthritides. Ann Rheum Dis. 1986 Oct;45(10):847–851. doi: 10.1136/ard.45.10.847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Marklund S. L. Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem J. 1984 Sep 15;222(3):649–655. doi: 10.1042/bj2220649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Marklund S. L. Extracellular superoxide dismutase in human tissues and human cell lines. J Clin Invest. 1984 Oct;74(4):1398–1403. doi: 10.1172/JCI111550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Marklund S. L., Holme E., Hellner L. Superoxide dismutase in extracellular fluids. Clin Chim Acta. 1982 Nov 24;126(1):41–51. doi: 10.1016/0009-8981(82)90360-6. [DOI] [PubMed] [Google Scholar]
  13. Marklund S. L. Human copper-containing superoxide dismutase of high molecular weight. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7634–7638. doi: 10.1073/pnas.79.24.7634. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Marklund S. L. Properties of extracellular superoxide dismutase from human lung. Biochem J. 1984 May 15;220(1):269–272. doi: 10.1042/bj2200269. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Marklund S. L., Westman N. G., Lundgren E., Roos G. Copper- and zinc-containing superoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues. Cancer Res. 1982 May;42(5):1955–1961. [PubMed] [Google Scholar]
  16. Marklund S. Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase. J Biol Chem. 1976 Dec 10;251(23):7504–7507. [PubMed] [Google Scholar]
  17. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  18. Tibell L., Hjalmarsson K., Edlund T., Skogman G., Engström A., Marklund S. L. Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6634–6638. doi: 10.1073/pnas.84.19.6634. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Weisiger R. A., Fridovich I. Mitochondrial superoxide simutase. Site of synthesis and intramitochondrial localization. J Biol Chem. 1973 Jul 10;248(13):4793–4796. [PubMed] [Google Scholar]

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