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The Homologous Species Restriction of the Complement Attack: Structure and Function of the C8 Binding Protein

  • G. M. Hänsch
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 140)

Abstract

The homologous restriction of the complement attack, i.e., the inability of complement to lyse erythrocytes of the same species, has long been known (Bordet 1900), but only in the last decade has progress been made in understanding the nature of this phenomenon. It has become evident that the complement sequence is inhibited species-specifically on the membrane at two steps at least (Shin et al. 1986), thus protecting the erythrocytes against the complement attack. Inhibition is accomplished by two membrane proteins: one, the so-called decay accelerating factor (DAF) which inhibits the complement activation phase (Nicholson-Weller et al. 1982), and the other, the C8 binding protein (C8bp) which interferes with the action of the late complement components (Schönermark et al. 1984, 1986). Since the late complement components C5b-9 represent the cytolytic effector phase of complement, the following discussion will be restricted to the function and characterization of the C8bp.

Keywords

Paroxysmal Nocturnal Hemoglobinuria Decay Accelerate Factor Erythrocyte Membrane Protein Paroxysmal Nocturnal Hemoglobinuria Patient Complement Attack 
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.

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References

  1. Betz M, Hänsch GM (1984) Release of arachidonic acid: a new function of the late complement components. Immunobiology 166:473–483PubMedCrossRefGoogle Scholar
  2. Betz M, Seitz M, Hänsch GM (1987) Thromboxane B2 synthesis in human platelets induced by the late complement components C5b-9. Int Arch Allergy Appl Immunol 82:313–316PubMedCrossRefGoogle Scholar
  3. Blaas P, Berger B, Weber S, Peter HH, Hänsch GM (1988) Paroxysmal nocturnal hemoglobinuria (PNH) type III: enhanced stimulation of platelets by the terminal complement components is related to the lack of C8bp in the membrane. J Immunol 140:3045–3051PubMedGoogle Scholar
  4. Bordet J (1900) Les serums hemolytique, les antitoxines et les theories des serum cytolytiques. Ann Inst Pasteur 14:257–271Google Scholar
  5. Davitz MA, Low MG, Nussenzweig V (1986) Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C. J Exp Med 163:1150–1161PubMedCrossRefGoogle Scholar
  6. Devine DV, Siegel RS, Rosse WF (1987) Interaction of the platelets in paroxysmal nocturnal hemoglobinuria with complement. J Clin Invest 79:131–137PubMedCrossRefGoogle Scholar
  7. Götze O, Müller-Eberhard HJ (1970) Lysis of erythrocytes by complement in the absence of antibody. J exp Med 132:898–903PubMedCrossRefGoogle Scholar
  8. Hänsch GM, Hammer C, Vanguri P, Shin ML (1981) Self versus nonself restriction in the lysis of erythrocytes by the terminal complement proteins. Proc Natl Acad Sci USA 78:5118–5122PubMedCrossRefGoogle Scholar
  9. Hänsch GM, Seitz M, Martinotti G, Betz M, Rauterberg EW, Gemsa D (1984) Macrophages release arachidonic acid, prostaglandin E2 and thromboxane in response to the late complement components. J Immunol 133:2145–2150PubMedGoogle Scholar
  10. Hänsch GM, Gemsa D, Resch K (1985) Induction of prostanoid synthesis in human platelets by the late complement components C5b-9 and channel forming antibiotic nystatin: inhibition of reacylation of liberated arachidonic acid. J Immunol 135:1320–1324PubMedGoogle Scholar
  11. Hänsch GM, Schönermark S, Roelcke D (1987) Paroxysmal nocturnal hemoglobinuria type III: lack of an erythrocyte membrane protein restricting the lysis by C5b-9. J Clin Invest 80:7–12PubMedCrossRefGoogle Scholar
  12. Hänsch GM, Weller P, Nicholson-Weller A (1988) Release of C8bp from the cell membrane by phosphatidylinositol-specific phospholipase C. Blood (in press)Google Scholar
  13. Hu V, Nicholson-Weiler A (1985) Enhanced complement-mediated lysis of type III paroxysmal nocturnal hemoglobinuria erythrocytes involves increased C9 binding and polymerisation. Proc Natl Acad Sci USA 82:5520–5524PubMedCrossRefGoogle Scholar
  14. Hu V, Shin ML (1984) Species-restricted target cell lysis by human complement. Complement-lysed erythrocytes from different species differ in the ratio of bound and inserted C9. J Immunol 133:2133–2137PubMedGoogle Scholar
  15. Imagawa DK, Osifchin NE, Paznekas WA, Shin ML, Mayer MM (1983) Consequences of cell membrane attack by complement: release of arachidonate and formation of inflammatory mediators. Proc Natl Acad Sci USA 80:6647–6651PubMedCrossRefGoogle Scholar
  16. Lachmann PJ, Thompson RA (1970) Reactive lysis: the complement-mediated lysis of unsensitized cells. II. The characterization of activated reactor as C5b6 and the participation of C8 and C9. J Exp Med 131:643–657PubMedCrossRefGoogle Scholar
  17. Lachmann PJ, Bowyer DE, Nicol P, Dawson RMC, Munn EA (1973) Studies on the terminal stages of complement lysis. Immunology 24:135–145PubMedGoogle Scholar
  18. Lint TF, Behrends CL, Gewurz H (1977) Serum lipoproteins and C567-INH activity. J Immunol 119:883–888PubMedGoogle Scholar
  19. Low MG, Finean JB (1977) Non-lytic release of acetylcholinesterase from erythrocytes by a phospha-tidylinositol-specific phospholipase C. FEBS Lett 82:143–146PubMedCrossRefGoogle Scholar
  20. Nicholson-Weiler A, Burger J, Fearon DT, Weller PF, Austen KF (1982) Isolation of human erythrocyte membrane glycoprotein with decay-accelerating activity for C3-convertases of the complement system. J Immunol 129:184–189Google Scholar
  21. Packman CH, Rosenfeld SI, Jenkins DE, Thiem PA, Leddy JP (1979) Complement lysis of human erythrocytes. Differing susceptibility of two types of paroxysmal nocturnal hemoglobinuria cells to C5b-9. J Clin Invest 64:428–433PubMedCrossRefGoogle Scholar
  22. Parker CJ, Wiedmer T, Sims PJ, Rosse WF (1985) Characterization of the complement sensitivity of paroxysmal nocturnal hemoglobinuria erythrocytes. J Clin Invest 75:2074–2084PubMedCrossRefGoogle Scholar
  23. Podack ER, Kolb WP, Müller-Eberhard HJ (1977) The SC5b-7 complex: formation, isolation, properties and subunit composition. J Immunol 119:2024–2029PubMedGoogle Scholar
  24. Podack ER, Kolb WP, Müller-Eberhard HJ (1978) The C5b6 complex: formation, isolation and inhibition of its activity by lipoprotein and the S-protein of human serum. J Immunol 120:1841–1848PubMedGoogle Scholar
  25. Podack ER, Preissner KT, Müller-Eberhard HJ (1984) Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein. Acta Pathol Microbiol Immunol Scand [Suppl] [C] 284:89–96Google Scholar
  26. Polley MJ, Nachman RL, Weksler BB (1981) Human complement in the arachidonic acid transformation pathway in platelets. J Exp Med 153:257–268PubMedCrossRefGoogle Scholar
  27. Rosenfeld SI, Jenkins DE, Leddy JP (1985) Enhanced reactive lysis of paroxysmal nocturnal hemoglobinuria cells does not involve increased C7 binding or cell bound C3b. J Immunol 134:506–510PubMedGoogle Scholar
  28. Rosse WF (1973) Variations in the complement-sensitive cells in paroxysmal nocturnal hemoglobinuria. Br J Haematol 24:327–342PubMedCrossRefGoogle Scholar
  29. Rosse WF (1986) The control of complement activation by the blood cells ion paroxysmal nocturnal hemoglobinuria. Blood 67:268–269PubMedGoogle Scholar
  30. Rother U, Hänsch GM, Menzel J, Rother K (1974) Deviated lysis: transfer of complement lytic activity to unsensitized cells. Generation of a transferable activity on the surface of complement-resistent bacteria. Z Immunitaetsforsch 148:172–178Google Scholar
  31. Schönermark S, Rauterberg EW, Roelcke D, Löke S, Hänsch GM (1984) A C8-binding protein on the surface of human erythrocytes: the inhibition of lysis in a homologous system (abstract). Immunobiology 168:109Google Scholar
  32. Schönermark S, Rauterberg EW, Shin ML, Löke S, Roelcke D, Hänsch GM (1986) Homologous species restriction in lysis of human erythrocytes. A membrane-derived protein with C8-binding capacity functions as an inhibitor. J Immunol 136:1772–1776PubMedGoogle Scholar
  33. Schönermark S, Filsinger S, Berger B, Hänsch GM (1988) The C8 binding protein of the human erythrocyte: interaction with the components of the complement attack phase. Immunology 63:585–590PubMedGoogle Scholar
  34. Shin ML, Hänsch GM, Hu V, Nicholson-Weller A (1986) Membrane factor(s) responsible for homologous species restriction of complement-mediated lysis: evidence for a factor other than DAF operating at the stage of C8 and C9. Immunology 136:1777–1782Google Scholar
  35. Tschopp J, Podack ER, Müller-Eberhard HJ (1985) The membrane attack complex of complement: C5b-8 complex as accelerator of C9 polymerization. J Immunol 134:495–499PubMedGoogle Scholar
  36. Yamamoto K (1977) Lytic activity of C5–9 complexes for erythrocytes from species other than sheep: C9 rather than C8-dependent lytic activity. J Immunol 119:1482–1487PubMedGoogle Scholar
  37. Zalman LS, Wood LM, Müller-Eberhard HJ (1986) Isolation of a human erythrocyte membrane protein capable of inhibiting expression of homologous complement channels. Proc Natl Acad Sci USA 83:6975–6979PubMedCrossRefGoogle Scholar
  38. Zalman LS, Wood LM, Frank MM, Müller-Eberhard HJ (1987) Deficiency of the homologous restriction factor in paroxysmal nocturnal hemoglobinuria. J Exp Med 165:572–577PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin · Heidelberg 1988

Authors and Affiliations

  • G. M. Hänsch
    • 1
  1. 1.Institut für ImmunologieUniversität HeidelbergHeidelbergFederal Republic of Germany

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