Role of Polymorphonuclear Leukocytes in the Pathogenesis of Infective Arthritis

  • I. N. Bird
Part of the New Clinical Applications Rheumatology book series (NCRH, volume 2)

Abstract

Types of arthritis whose onset can be associated with a known infection, diagnosed by the presence of the infective agent or its antigen(s) in the infected joints, are termed infective arthropathies. Infective agents causing such arthropathies are reviewed in the preceding chapters and include bacteria, mycoplasma, fungi and viruses. The arthropathies tend to be acute, with varying patterns of symptoms, and the time taken for resolution is very variable. A major feature of these arthropathies is the increased concentration of polymorphonuclear leukocytes (PMNL) in the synovial fluid.

Keywords

Synovial Fluid Human Neutrophil Polymorphonuclear Leukocyte Chronic Granulomatous Disease Hypochlorous Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Platt, P. N. (1983). Examination of synovial fluid. In Dick, W. C. and Jeffery, M. S. (eds.) Clinics in Rheumatic Diseases, Vol. 9, No. 1, p. 54. (London: WB Saunders Co.)Google Scholar
  2. 2.
    Hurley, J. V. (1983). Acute Inflammation, 2nd Edn. (Edinburgh, London, Melborne and New York: Churchill Livingstone)Google Scholar
  3. 3.
    Ropes, M. W. and Bauer, W. (1953). Synovial Fluid Changes in Joint Diseases. (Cambridge MA: Harvard University Press)Google Scholar
  4. 4.
    Bainton, D. F., Ullyot, J. L. and Farquhar, M. G. (1971). The development of neutrophil polymorphonuclear leukocytes in human bone marrow. J. Exp. Med., 134, 907–934PubMedCrossRefGoogle Scholar
  5. 5.
    Breton-Garius, R. and Reyes, F. (1976). Ultrastructure of human bone marrow maturation Int. Rev. Cytol., 46, 251–321CrossRefGoogle Scholar
  6. 6.
    Lichtman, M. A. and Weed, R. I. (1970). Electrophoretic mobility and N-acetyl neuraminic acid content of human and leukemic lymphocytes and granulocytes. Blood, 35, 12–22PubMedGoogle Scholar
  7. 7.
    Lichtman, M. A. and Weed, R. I. (1972). Alteration of the cell periphery during granulocyte maturation: relationship to cell function. Blood, 39, 301–316PubMedGoogle Scholar
  8. 8.
    Mary, J. Y. (1985). Normal human granulopoiesis revisited. II. Bone marrow data. Biomed. Biopharmacother., 39, 66–77Google Scholar
  9. 9.
    Murphy, P. (1976). The Neutrophil. (New York and London: Plenum Medical Book Company)Google Scholar
  10. 10.
    Marchesi, V. T. (1961). The site of leucocyte emigration during inflammation. Q. J. Exp. Physiol., 46, 115–123Google Scholar
  11. 11.
    Marchesi, V. T. and Florey, H. W. (1960). Electron micrographic observation on the emigration of leucocytes Q. J. Exp. Physiol., 45, 343–348Google Scholar
  12. 12.
    Harlan, J. M. (1985). Leukocyte-endothelial reactions. Blood, 65, 513–525PubMedGoogle Scholar
  13. 13.
    Ramsey, W. S. (1972). Analysis of individual leukocyte behaviour during chemotaxis. Exp. Cell Res., 70, 120–139CrossRefGoogle Scholar
  14. 14.
    Ramsey, W. S. (1972). Locomotion of human polymorphonuclear leukocytes. Exp. Cell Res., 72, 489–500PubMedCrossRefGoogle Scholar
  15. 15.
    Maleh, H. L., Root, R. K. and Gallin, J. I. (1977). Structural analysis of human neutrophil migration (centriole, microtubule and microfilament orientation and function during chemotaxis). J. Cell Biol., 75, 666–693CrossRefGoogle Scholar
  16. 16.
    Chenoweth, D. E. and Hugh, T. E. (1978). Demonstration of a specific C5a receptor on intact human polymorphonuclear leukocytes. Proc. Natl. Acad. Sci. USA, 75, 3943–3947PubMedCrossRefGoogle Scholar
  17. 17.
    Abramson, S. and Weissmann, G. (1981). The release of inflammatory mediators from neutrophils. La Ricerca Clin. Lab., 11, 91–99Google Scholar
  18. 18.
    Weissmann, G., Korchak, H. M., Perez, H. D., Smolen, J. E., Goldstein, I. M. and Hoffstein, S. T. (1979). J. Reticuloendothel Soc., 26, 687–700PubMedGoogle Scholar
  19. 19.
    Baggiolini, M. and Dewald, B. (1985). The neutrophil. Int. Arch. Appl. Immunol., 76 (Suppl. 1), 13–20CrossRefGoogle Scholar
  20. 20.
    Smolen, J. E. and Weissmann, G. (1979). Polymorphonuclear leukocytes. In McCarty, D. J. (ed.) Arthritis and Allied Conditions: A Textbook of Rheumatology, pp. 282–295. (Philadelphia: Lea and Febiger)Google Scholar
  21. 21.
    Baldridge, C. W. and Gerard, R.W. (1933). The extra respiration of phagocytes Am. J. Physiol., 103, 235–236Google Scholar
  22. 22.
    Fantone, J. C. and Ward, P. A. (1982). Role of oxygen derived free radicals and metabolites in leukocyte dependent inflammatory reactions. Am. J. Pathol., 107, 397–418Google Scholar
  23. 23.
    Beaman, L. and Beaman, B. L. (1984). The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu. Rev. Microbiol., 38, 27–48PubMedCrossRefGoogle Scholar
  24. 24.
    Rossi, F., Bellavite, P., Berton, G., Grzeshowiak, M. and Papini, E. (1985). Mechanism of production of toxic oxygen radicals by granulocytes and their function in the inflammatory process. Pathol. Res. Pract., 180, 136–142PubMedGoogle Scholar
  25. 25.
    Fantone, J. C. and Ward, P. A. (1985). Polymorphonuclear leukocyte mediated cell and tissue injury: oxygen metabolites and their relation to human disease. Human Pathol., 16, 973–978CrossRefGoogle Scholar
  26. 26.
    Hattori, H. (1961). Studies on the labile stable NADH oxidase and peroxidase staining reactions in the granulocyte particles of the horse granulocyte. Nagoya J. Med. Sci., 23, 362–378PubMedGoogle Scholar
  27. 27.
    Bellavite, P., Cross, A. R., Serra, M. C., Davoli, A., Jones, O. T. G. and Rossi, F. (1983). The cytochrome B and flavin content and properties of the superoxide forming NADPH oxidase solubilized from activated neutrophils. Biochim. Biophys. Acta, 746, 40–47PubMedCrossRefGoogle Scholar
  28. 28.
    Crawford, D. R. and Schneider, D.L. (1982). Identification of ubiquinone 50 in human neutrophils and its role in microbicidal events. J. Biol. Chem., 257, 6662–6668PubMedGoogle Scholar
  29. 29.
    Allen, R. C. (1982) Biochemiexcitation: chemiluminescence and the study of biological oxygenation reactions. In Deluca, M.A. and McElroy, W. D. (eds.) Chemical and Biological Generation of Excited States, pp. 309–344. (New York: Academic Press)Google Scholar
  30. 30.
    Halliwell, B. and Gutteridge, J. M. C. (1985). The importance of free radicals and the catalytic metal ions in human diseases. Mol. Aspects Med., 8, 89–193PubMedCrossRefGoogle Scholar
  31. 31.
    Halliwell, B. and Gutteridge, J. M. C. (1985). Free Radicals in Biology and Medicine. (Oxford: Clarendon Press)Google Scholar
  32. 32.
    Blum, J. and Fridovich, I. (1985). Inactivation of glutathione peroxidase by superoxide radicals. Arch. Biochem. Biophys., 240, 500–508PubMedCrossRefGoogle Scholar
  33. 33.
    Root, R. K., and Metcalf, J. A. (1977). H2O2 release from human granulocytes during phagocytosis: relationship to superoxide anion formation and cellular catabolism of H2O2: studies with normal and cytochalasin B treated cells. J. Cell Invest., 60, 1266–1276CrossRefGoogle Scholar
  34. 34.
    Halliwell, B. and Gutteridge, J. M. C. (1984). Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J., 219, 1–14PubMedGoogle Scholar
  35. 35.
    Klebanoff, S. J. (1982). Oxygen dependent cytotoxic mechanisms of phagocytes. In Gallin, J. I. and Fauci, A. S. (eds.) Advances in Host Defence Mechanisms, Vol. I. (New York: Raven Press)Google Scholar
  36. 36.
    Schultz, J. and Kaminker, K. (1962). Myeloperoxidase of the leucocytes of normal human blood. I. Content and localisation. Arch. Biochem., 96, 465–467PubMedCrossRefGoogle Scholar
  37. 37.
    Klebanoff, S. J. (1968). Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J. Bacteriol., 95, 2131–2138PubMedGoogle Scholar
  38. 38.
    Zgliczynski, J. M., Selvaraj, R. J., Paul, B. B., Stelmazynska, T, Poshitt, P. K. F. and Sbarra, A. J. (1977). Chlorination by the myeloperoxidase H2O2-Cl-antimicrobial system at acid and neutral pH. Proc. Soc. Exp. Biol. Med., 154, 418–422PubMedGoogle Scholar
  39. 39.
    Thomas, E. L. and Fishman, M. (1986). Oxidation of chloride and thiocynate by isolated leukocytes. J. Biol. Chem., 261, 9694–9701PubMedGoogle Scholar
  40. 40.
    Babior, B. M. (1978). Oxygen dependent microbial killing by phagocytes. N. Engl. J. Med., 298, 659–668PubMedCrossRefGoogle Scholar
  41. 41.
    Weiss, S. J., Lampert, M. B. and Test, S. T. (1983). Long lived oxidants generated by human neutrophils. Science, 222, 625–628PubMedCrossRefGoogle Scholar
  42. 42.
    Grisham, M. B., Jefferson, M. M., Melton, D. F. and Thomas, E. L. (1984). Chlorination of endogenous amines by isolated neutrophils. J. Biol. Chem., 259, 10404–10413PubMedGoogle Scholar
  43. 43.
    Tauber, A. I. and Babior, B. M. (1985). Neutrophil oxygen reduction: the enzyme and the products. Adv. Free Rad. Biol. Med., 1, 265–307CrossRefGoogle Scholar
  44. 44.
    Greenwald, R. A. and Moy, W. W. (1979). Inhibition of collagen gelatin by the action of superoxide radical. Arthritis Rheum., 22, 251–257PubMedCrossRefGoogle Scholar
  45. 45.
    Carp, H. and Janoff, A. (1983). Modulation of inflammatory cell protease-tissue antiprotease interactions at sites of inflammation by leukocyte derived oxidants. In Weissmann, G. (ed.) Advances in Inflammation Research, Vol. 5, pp. 173–201. (New York: Raven Press)Google Scholar
  46. 46.
    Bates, E. J., Harper, G. S. and Lowther, D. A. (1984). Effect of oxygen derived reactive species on cartilage proteoglycan-hyaluronic aggregates. Biochem. Int., 8, 629–636PubMedGoogle Scholar
  47. 47.
    Greenwald, R. A. and Moy, W. W. (1980). Effect of oxygen derived free radicals on hyaluronic acid. Arthritis Rheum., 23, 455–461PubMedCrossRefGoogle Scholar
  48. 48.
    Strominger, J. L. and Ghuysen, J. M. (1967). Mechanisms of enzymatic bacteriolysis. Science, 156, 213–221PubMedCrossRefGoogle Scholar
  49. 49.
    Root, R. K. and Cohen, M. S. (1981). The microbicidal mechanisms of human neutrophils and eosinophils. Rev. Infect. Dis., 3, 565–598PubMedCrossRefGoogle Scholar
  50. 50.
    Wilson, L. A. and Spitznagel, J. K. (1968). Molecular and structural damage to E. coli produced by antibody, complement and lysozyme systems. J. Bacteriol., 96, 1339–1348PubMedGoogle Scholar
  51. 51.
    Miller, T. E. (1969). Killing and lysis of Gram negative bacteria through the synergistic effect of hydrogen peroxide, ascorbic acid and lysozyme. J. Bacteriol., 98, 949–995PubMedGoogle Scholar
  52. 52.
    Efrati, C., Sachs, T., Ne’eman, N, Lahov, M. and Ginsburg, J. (1976). The effect of leukocyte hydrolyases on bacteria. III. The combined effect of leukocyte lysozyme enzymic cocktails and penicillin on the lysis of Staphylcoccus aureus and group A Streptococci in vitro. Inflammation, 1, 371–407CrossRefGoogle Scholar
  53. 53.
    Garcia, R. C., Peterson, C. G. B., Segal, A. W. and Venge, P. (1985). Elastase in the different primary granules of the human neutrophil. Biochem. Biophys. Res. Commun., 132, 1130–1136PubMedCrossRefGoogle Scholar
  54. 54.
    Klebanoff, S. J. and Clark, R. A. (1978). The Neutrophil: Function and Clinical Perspectives. (Amsterdam, New York and Oxford: North Holland)Google Scholar
  55. 55.
    Travis, J. and Salvesen, G. S. (1983). Human plasma proteinase inhibitors. Annu. Rev. Biochem., 52, 655–709PubMedCrossRefGoogle Scholar
  56. 56.
    Carr, W. P. (1983). Acute phase proteins. In Dick, W. C. and Jeffery, M. S. (eds.) Clinics in Rheumatic Diseases, Vol. 9., pp. 227–239. (London: W. B. Saunders Co.)Google Scholar
  57. 57.
    Smedly, L. A., Tonneson, M. G., Sandhaus, R. A., Haslett, C., Guthrie, L. A., Johnston, R. B., Henson, P. M. and Worthen, G. S. (1986). Neutrophil mediated injury to endothelial cells. Enhancement by endotoxin and essential role of neutrophil elastase. J. Clin. Invest., 77, 1233–1243.PubMedCrossRefGoogle Scholar
  58. 58.
    Janoff, A. (1985). Elastase in tissue injury. Annu. Rev. Med., 36, 207–216PubMedCrossRefGoogle Scholar
  59. 59.
    Baggiolini, M., Bretz, U. and Dewald, B. (1978). Subcellular localization of granulocyte enzymes. In Havemann, K., and Janoff, A. (eds.) Neutral Proteases of Human Polymorphonuclear Leukocytes, pp. 3–17. (Baltimore, Munich: Urban and Schwarzenberg)Google Scholar
  60. 60.
    White, A., Handler, P. and Smith, E. L., (1964). Principles of Biochemistry, 3rd Edn. p. 774. (New York, Toronto, London: McGraw-Hill Book Company)Google Scholar
  61. 61.
    Ohlsson, K., Ohlsson, I. and Spitznagel, J. K. (1977). Localisation of chymotrypsin like cationic protein, collagenase and elastase in azurophilic granules of human neutrophilic polymorphonuclear leukocytes. Hoppe Seylers Z. Physiol. Chem., 358, 361–366PubMedCrossRefGoogle Scholar
  62. 62.
    Selsted, M. E., Brown, D. M., Delange, R. J., Harwig, S. S. L., Ganz, T., Schilling, J. W. and Lehrer, R. I. (1985). Primary structure of six antimicrobial peptides of rabbit peritoneal neutrophils. J. Biol. Chem., 260, 4579–4584PubMedGoogle Scholar
  63. 63.
    Selsted, M. E., Harwig, S. S. L., Ganz, T., Schilling, J. W. and Lehrer, R. I. (1985). Primary structure of three human neutrophil defensins. J. Clin. Invest., 76, 1436–1439PubMedCrossRefGoogle Scholar
  64. 64.
    Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S. L., Daker, K., Bainton, D. F. and Lehrer, R. I. (1985). Defensins: natural peptide antibiotics of human neutrophils. J. Clin. Invest., 76,1427–1435PubMedCrossRefGoogle Scholar
  65. 65.
    Gallin, J. I. (1985). Neutrophil specific granule deficiency. Annu. Rev. Med., 36, 263–274PubMedCrossRefGoogle Scholar
  66. 66.
    Ohlsson, K. (1978). Purification and properties of granulocyte collagenase and elastase. In Havemann, K. and Janoff, A. (eds.) Neutral Proteases of Human Polymorphonuclear Leukocytes, pp. 89–101. (Baltimore and Munich: Urban and Schwarzenberg)Google Scholar
  67. 67.
    Hasty, K. A., Hibbs, M. S., Kang, A. H. and Mainardi, C. L. (1984). Heterogenity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase. J. Exp. Med., 159, 1455–1463PubMedCrossRefGoogle Scholar
  68. 68.
    Weiss, S. J., Peppin, G. J. Ortiz, X., Ragdale, J. and Test, S. T. (1955). Oxidative autoactivation of latent collagenase by human neutrophils. Science, 227, 747–749CrossRefGoogle Scholar
  69. 69.
    Burkhardt, H., Schwingel, M., Menninger, H., MaCartney, H. W. and Tschesche, T. (1986). Oxygen radicals as effectors of cartilage destruction. Direct degradative effect on matrix components and indirect action via activation of latent collagenase from polymorphonuclear leukocytes. Arthritis Rheum., 29, 379–387PubMedCrossRefGoogle Scholar
  70. 70.
    Ambrusco, D. R. and Johnston, R. B., (1981). Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions and an enzymatic generating system. J. Clin. Invest., 67, 352–360CrossRefGoogle Scholar
  71. 71.
    Boxer, L., Bjorksten, B., Bjork, J., Yang, H., Allen, J. M. and Baehner, R. M. (1982). Neutropenia induced by systemic infusion of lactoferrin. J. Lab. Clin. Med., 99, 866–872PubMedGoogle Scholar
  72. 72.
    O’Shea, J., Seligmann, B., Gallin, J. I., Chused, T., Berger, M., Frank, M. and Brown, E. (1984). Distinct modulation of complement receptors on human neutrophils. Fed. Proc., 43, 1505Google Scholar
  73. 73.
    Arnaout, M. A., Spits, H., Terhorst, C., Pitt, J. and Todel, R. F. (1984). Deficiency of a leukocyte glycoprotein (LFA-1) in two patients with MO 1 deficiency: effects of cell activation on MO 1/LFA 1 surface expression on normal and deficient leukocytes. J. Clin. Invest., 74, 1291–1300PubMedCrossRefGoogle Scholar
  74. 74.
    Fletcher, M. and Gallin, J. I. (1983). Human neutrophils contain an intracellular pool of putative receptors for the chemoattractant N-formylmethionylleucylphenylalanine. Blood, 62, 792–799PubMedGoogle Scholar
  75. 75.
    Borregaard, N., Heiple, J. M., Simons, E. and Clark, R. A., (1983). Subcellular localization of the b cytochrome component of the human neutrophil microbicidal oxidase: translocation during activation. J. Cell Biol., 97, 52–61PubMedCrossRefGoogle Scholar
  76. 76.
    Wright, D. G. and Gallin, J. I. (1977). A functional separation of human neutrophil granules: generation of C5a by a specific granule product and inactivation of C5a by azurophil granule products. J. Immunol., 119, 1068–1076PubMedGoogle Scholar
  77. 77.
    Wright, D. G. and Greenwald, D. (1979). Increased motility and maturation of human blood monocytes stimulated by products released from neutrophil secondary granules. Blood, 54, (Suppl 1.), 95aGoogle Scholar
  78. 78.
    Murphy, G., Bretz, U., Baggiolini, M. and Reynolds, J. J., (1980). The latent collagenase and gelatinase of human polymorphonuclear leukocytes. Biochem. J., 192, 517–525PubMedGoogle Scholar
  79. 79.
    Dewald, B., Bretz, U. and Baggiolini, M. (1982). Release of gelatinase from a novel secretory component of human neutrophils. J. Clin. Invest., 70, 518–525PubMedCrossRefGoogle Scholar
  80. 80.
    Peppin, G. J. and Weiss, S. J. (1986). Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils. Proc. Natl. Acad. Sci. USA, 83, 4322–4326PubMedCrossRefGoogle Scholar
  81. 81.
    Davies, P., Bailey, P. J. and Goldenberg, M. M. (1984). The role of arachidonic acid oxygenation products in pain and inflammation. Annu. Rev. Immunol., 2, 335–357PubMedCrossRefGoogle Scholar
  82. 82.
    Granstrom, E. (1984). The arachidonic acid cascade. The prostaglandins, thromboxanes and leukotrienes. Inflammation, 8, S15–S25PubMedCrossRefGoogle Scholar
  83. 83.
    Abramson, S., Edelson, H., Kaplan, H., Ludewig, R. and Weissmann, G. (1984). Inhibition of neutrophil activation by non-steroidal anti-inflammatory drugs. Am. J. Med., 77, 3–6PubMedCrossRefGoogle Scholar
  84. 84.
    Piper, P. (1984). Formation and action of leukotrienes. Physiol. Rev., 64, 744–761PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1989

Authors and Affiliations

  • I. N. Bird

There are no affiliations available

Personalised recommendations