Iron in Synovial Fluid

Removal by Lactoferrin and Relationship to Iron Regulatory Protein (IRP) Activity
  • C. Guillen
  • I. B. McInnes
  • J. H. Brock
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 443)


Rheumatoid arthritis (RA) is a common human autoimmune disease with an incidence of about 1%. It is a chronic inflammatory polyarthritis characterised by infiltration of the synovial membrane by macrophages, T cells, B cells and activated fibroblasts1, leading in most cases to progressive destruction of cartilage and bone.


Rheumatoid Arthritis Patient Synovial Fluid Cellular Iron Iron Regulatory Protein Human Lactoferrin 
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  1. 1.
    Cush JJ and Lipsky PE(1988). Phenotypic analysis of synovial tissue and peripheral blood lymphocytes isolated from patients with rheumatoid arthritis. Arthritis Pheum. 31: 1230–1238.Google Scholar
  2. 2.
    Blake DR, Gallagher PJ, Potter AR et al. (1984). The effect of synovial iron on the progression of rheumatoid disease. Arthritis Rheum. 27: 495–501.PubMedCrossRefGoogle Scholar
  3. 3.
    Burkhardt H. Schwingel M (1986). Oxygen radicals as effectors of cartilage destruction. Arthritis Rheum. 29: 379–387.PubMedCrossRefGoogle Scholar
  4. 4.
    Melefors O. Hentze MW (1993). Iron regulatory factor - the conductor of cellular iron regulation. Blood Rev. 7: 251.PubMedCrossRefGoogle Scholar
  5. 5.
    Klausncr RD, Rouault TA, Harford JB (1993). Regulating the fate of mRNA: the control of cellular iron metabolism. Cell. 72: 19.CrossRefGoogle Scholar
  6. 6.
    Pantopoulos K, Weiss G, Hentze MW (1996). Nitric oxide and oxidative stress (H2O,) control mammalian iron metabolism by different pathways. Mol. Cell. Biol. 16: 3781–8.Google Scholar
  7. 7.
    Guttcridge JMC, Rowley DA, Halliwell B (1981). Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Biochem. J. 199: 263–265.Google Scholar
  8. 8.
    Gray NK, Quick S, Goossen B, Constable A, Hirling H, Kühn LC, Hentze MW (1993). Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch. Eur. J. Biochem. 218: 657–667.Google Scholar
  9. 9.
    Etherington DJ, Pugh G, Silver IA (1981). Collagen degradation in an experimental inflammatory lesion: studies on the role of the macrophage. Acta Biol. Med. Ger. 40: 1625–1636.Google Scholar
  10. 10.
    Aisen P. Leibman A (1972). Lactoferrin and transferrin: a comparative study. Biochim. Biophys. Acta. 257: 314–323.Google Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • C. Guillen
    • 1
  • I. B. McInnes
    • 1
  • J. H. Brock
    • 1
  1. 1.Department of ImmunologyWetern InfirmaryGlasgowUK

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