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. 1976 Feb 1;143(2):271–289. doi: 10.1084/jem.143.2.271

Binding of components of the properdin system to cultured human lymphoblastoid cells and B lymphocytes

PMCID: PMC2190117  PMID: 1082488

Abstract

Immunofluorescence studies showed that properdin (P) and factor B bind to C3-C3b receptor bearing human lymphoblastoid cells (Raji, Daudi) and B type human peripheral lymphocytes (HPL). P bound to Raji cells first incubated with normal human serum (NHS). EDTA, but not EGTA, halted the binding of P to cells incubated with NHS. However, fixation of P to Raji cells, after incubation with NHS first reacted with inulin, was independent of Ca++ and -g++ ions. Fixation of P to Raji cells depended on the presence of C3 or C3b and occurred in the absence of factor D and factor B. Binding of P to B type HPL was detectable only after incubation of these cells with NHS first reacted with inulin; under these conditions binding of P to Raji cells was also greatly enhanced. With both Raji cells and HPL, factor B was detectable on cell surfaces only after incubation of these cells with NHS first reacted with activators of the P system. Binding of factor B to cells required the presence of C3b and binding or stabilization of cell bound factor B necessitated the presence of activated P. P and factor B were detectable only on cultured cells having C3-C3b receptors. However, incubation of NHS with all lymphoblastoid cell lines studied resulted in activation of P and cleavage of factor B. Binding of P and factor B to cells may follow one of three sequences; (a) activated P in fluid phase combines with C3, factor D, and factor B, and the whole complex fixes to cellular C3-C3b receptors via its C3 moiety; (b) C3b generated in fluid phase combines with P, C3, factor D, and factor B and binds to C3-C3b receptors; or (c) C3 or C3b first binds onto the C3-C3b receptors and thereafter interacts with P, factor D, And factor B. Binding of components of the P system to cells or other particles may relate to such biological phenomena as lysis, phagocytosis, proliferation, attraction of other cell types, and alteration of responsiveness to external stimuli.

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Selected References

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  1. Auderset M. J., Lambert P. H., Miescher P. A. Purification of human C3 proactivator by affinity chromatography. Immunochemistry. 1974 Apr;11(4):207–211. doi: 10.1016/0019-2791(74)90330-9. [DOI] [PubMed] [Google Scholar]
  2. Bokisch V. A., Müller-Eberhard H. J., Cochrane C. G. Isolation of a fragment (C3a) of the third component of human complement containing anaphylatoxin and chemotactic activity and description of an anaphylatoxin inactivator of human serum. J Exp Med. 1969 May 1;129(5):1109–1130. doi: 10.1084/jem.129.5.1109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brade V., Lee G. D., Nicholson A., Shin H. S., Mayer M. M. The reaction of zymosan with the properdin system in normal and C4-deficienct guinea pig serum. Demonstration of C3- and C5-cleaving multi-unit enzymes, both containing factor B, and acceleration of their formation by the classical complement pathway. J Immunol. 1973 Nov;111(5):1389–1400. [PubMed] [Google Scholar]
  4. Brade V., Nicholson A., Bitter-Suermann D., Hadding U. Formation of the C3-cleaving properdin enzyme on zymosan. Demonstration that factor D is replaceable by proteolytic enzymes. J Immunol. 1974 Dec;113(6):1735–1743. [PubMed] [Google Scholar]
  5. Brade V., Nicholson A., Lee G. D., Mayer M. M. The reaction of zymosan with the properdin system: isolation of purified factor D from guinea pig serum and study of its reaction characteristics. J Immunol. 1974 May;112(5):1845–1854. [PubMed] [Google Scholar]
  6. CLARK H. F., SHEPARD C. C. A DIALYSIS TECHNIQUE FOR PREPARING FLUORESCENT ANTIBODY. Virology. 1963 Aug;20:642–644. doi: 10.1016/0042-6822(63)90292-7. [DOI] [PubMed] [Google Scholar]
  7. Cuatrecasas P. Affinity chromatography. Annu Rev Biochem. 1971;40:259–278. doi: 10.1146/annurev.bi.40.070171.001355. [DOI] [PubMed] [Google Scholar]
  8. Dukor P., Schumann G., Gisler R. H., Dierich M., König W., Hadding U., Bitter-Suermann D. Complement-dependent B-cell activation by cobra venom factor and other mitogens? J Exp Med. 1974 Feb 1;139(2):337–354. doi: 10.1084/jem.139.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ensky J., Hinz C. F., Jr, Todd E. W., Wedgwood R. J., Boyer J. T., Lepow I. H. Properties of highly purified human properdin. J Immunol. 1968 Jan;100(1):142–158. [PubMed] [Google Scholar]
  10. Fearon D. T., Austen K. F. Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase. J Exp Med. 1975 Oct 1;142(4):856–863. doi: 10.1084/jem.142.4.856. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fearon D. T., Austen K. F., Ruddy S. Formation of a hemolytically active cellular intermediate by the interaction between properdin factors B and D and the activated third component of complement. J Exp Med. 1973 Dec 1;138(6):1305–1313. doi: 10.1084/jem.138.6.1305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gewurz H., Pickering R. J., Snyderman R., Lichtenstein L. M., Good R. A., Mergenhagen S. E. Interactions of the complement system with endotoxic lipopolysaccharides in immunoglobulin-deficient sera. J Exp Med. 1970 Apr 1;131(4):817–831. doi: 10.1084/jem.131.4.817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Glaser R., O'Neill F. J. Hybridization of Burkitt lymphoblastoid cells. Science. 1972 Jun 16;176(4040):1245–1247. doi: 10.1126/science.176.4040.1245. [DOI] [PubMed] [Google Scholar]
  14. Götze O., Müller-Eberhard H. J. The C3-activator system: an alternate pathway of complement activation. J Exp Med. 1971 Sep 1;134(3 Pt 2):90s–108s. [PubMed] [Google Scholar]
  15. Götze O., Müller-Eberhard H. J. The role of properdin in the alternate pathway of complement activation. J Exp Med. 1974 Jan 1;139(1):44–57. doi: 10.1084/jem.139.1.44. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Joseph B. S., Cooper N. R., Oldstone M. B. Immunologic injury of cultured cells infected with measles virus. I. role of IfG antibody and the alternative complement pathway. J Exp Med. 1975 Apr 1;141(4):761–774. [PMC free article] [PubMed] [Google Scholar]
  17. Kassel R. L., Old L. J., Carswell E. A., Fiore N. C., Hardy W. D., Jr Serum-mediated leukemia cell destruction in AKR mice. J Exp Med. 1973 Oct 1;138(4):925–938. doi: 10.1084/jem.138.4.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lachmann P. J., Nicol P. Reaction mechanism of the alternative pathway of complement fixation. Lancet. 1973 Mar 3;1(7801):465–467. doi: 10.1016/s0140-6736(73)91886-2. [DOI] [PubMed] [Google Scholar]
  19. Lachmann P. J. The purification of specific antibody as F(ab')2 by the pepsin digestion of antigen-antibody precipitates, and its application to immunoglobulin and complement antigens. Immunochemistry. 1971 Jan;8(1):81–88. doi: 10.1016/0019-2791(71)90423-x. [DOI] [PubMed] [Google Scholar]
  20. Lay W. H., Nussenzweig V. Receptors for complement of leukocytes. J Exp Med. 1968 Nov 1;128(5):991–1009. doi: 10.1084/jem.128.5.991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lerner R. A., Oldstone M. B., Cooper N. R. Cell cycle-dependent immune lysis of Moloney virus-transformed lymphocytes: presence of viral antigen, accessibility to antibody, and complement activation. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2584–2588. doi: 10.1073/pnas.68.10.2584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Levy N. L., Scott D. W., Snyderman R. Bone marrow-derived lymphoid cells (B cells): functional depletion with cobra factor and fresh serum. Science. 1972 Nov 24;178(4063):866–867. doi: 10.1126/science.178.4063.866. [DOI] [PubMed] [Google Scholar]
  23. May J. E., Kane M. A., Frank M. M. Immune adherence by the alternate complement pathway. Proc Soc Exp Biol Med. 1972 Oct;141(1):287–290. doi: 10.3181/00379727-141-36760. [DOI] [PubMed] [Google Scholar]
  24. McLean R. H., Michael A. F. The immunoelectrophoretic pattern of properdin in fresh and aged human serum. Proc Soc Exp Biol Med. 1972 Nov;141(2):403–407. doi: 10.3181/00379727-141-36786. [DOI] [PubMed] [Google Scholar]
  25. McLean R. H., Townsend K., Michael A. F. The effect of anticomplementary substances on properdin in normal and C2-deficient sera. Clin Exp Immunol. 1975 Mar;19(3):435–444. [PMC free article] [PubMed] [Google Scholar]
  26. Mendes N. F., Miki S. S., Peixinho Z. F. Combined detection of human T and B lymphocytes by rosette formation with sheep erythrocytes and zymosan-C3 complexes. J Immunol. 1974 Aug;113(2):531–536. [PubMed] [Google Scholar]
  27. Minowada J., Onuma T., Moore G. E. Rosette-forming human lymphoid cell lines. I. Establishment and evidence for origin of thymus-derived lymphocytes. J Natl Cancer Inst. 1972 Sep;49(3):891–895. [PubMed] [Google Scholar]
  28. Müller-Eberhard H. J., Götze O. C3 proactivator convertase and its mode of action. J Exp Med. 1972 Apr 1;135(4):1003–1008. doi: 10.1084/jem.135.4.1003. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. NILSSON U. R., MUELLER-EBERHARD H. J. ISOLATION OF BETA IF-GLOBULIN FROM HUMAN SERUM AND ITS CHARACTERIZATION AS THE FIFTH COMPONENT OF COMPLEMENT. J Exp Med. 1965 Aug 1;122:277–298. doi: 10.1084/jem.122.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Nicholson A., Brade V., Lee G. D., Shin H. S., Mayer M. M. Kinetic studies of the formation of the properdin system enzymes on zymosan: evidence that nascent C3b controls the rate of assembly. J Immunol. 1974 Mar;112(3):1115–1123. [PubMed] [Google Scholar]
  31. Nicol P. A., Lachmann P. J. The alternate pathway of complement activation. The role of C3 and its inactivator (KAF). Immunology. 1973 Feb;24(2):259–275. [PMC free article] [PubMed] [Google Scholar]
  32. Nilsson U. R., Müller-Eberhard H. J. Deficiency of the fifth component of complement in mice with an inherited complement defect. J Exp Med. 1967 Jan 1;125(1):1–16. doi: 10.1084/jem.125.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Oldstone M. B. Virus neutralization and virus-induced immune complex disease. Virus-antibody union resulting in immunoprotection or immunologic injury--two sides of the same coin. Prog Med Virol. 1975;19:84–119. [PubMed] [Google Scholar]
  34. PILLEMER L., BLUM L., LEPOW I. H., ROSS O. A., TODD E. W., WARDLAW A. C. The properdin system and immunity. I. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena. Science. 1954 Aug 20;120(3112):279–285. doi: 10.1126/science.120.3112.279. [DOI] [PubMed] [Google Scholar]
  35. Perrin L. H., Lambert P. H., Miescher P. A. Complement breakdown products in plasma from patients with systemic lupus erythematosus and patients with membranoproliferative or other glomerulonephritis. J Clin Invest. 1975 Jul;56(1):165–176. doi: 10.1172/JCI108065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Rother K., Rother U., Müller-Eberhard H. J., Nilsson J. R. Deficiency of the sixth component of complement in rabbits with an inherited complement defect. J Exp Med. 1966 Oct 1;124(4):773–785. doi: 10.1084/jem.124.4.773. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Ruddy S., Austen K. F. C3b inactivator of man. II. Fragments produced by C3b inactivator cleavage of cell-bound or fluid phase C3b. J Immunol. 1971 Sep;107(3):742–750. [PubMed] [Google Scholar]
  38. Ruddy S., Austen K. F., Goetzl E. J. Chemotactic activity derived from interaction of factors D and B of the properdin pathway with cobra venom factor or C3B. J Clin Invest. 1975 Mar;55(3):587–592. doi: 10.1172/JCI107966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Schreiber R. D., Medicus R. G., Gïtze O., Müller-Eberhard H. J. Properdin- and nephritic factor-dependent C3 convertases: requirement of native C3 for enzyme formation and the function of bound C3b as properdin receptor. J Exp Med. 1975 Sep 1;142(3):760–772. doi: 10.1084/jem.142.3.760. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Stossel T. P., Alper C. A., Rosen F. S. Serum-dependent phagocytosis of paraffin oil emulsified with bacterial lipopolysaccharide. J Exp Med. 1973 Mar 1;137(3):690–705. doi: 10.1084/jem.137.3.690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Theofilopoulos A. N., Bokisch V. A., Dixon F. J. Receptor for soluble C3 and C3b on human lymphoblastoid (RAJI) cells. Properties and biologocal significance. J Exp Med. 1974 Mar 1;139(3):696–711. doi: 10.1084/jem.139.3.696. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Theofilopoulos A. N., Dixon F. J., Bokisch V. A. Binding of soluble immune complexes to human lymphoblastoid cells. I. Characterization of receptors for IgG Fc and complement and description of the binding mechanism. J Exp Med. 1974 Oct 1;140(4):877–894. doi: 10.1084/jem.140.4.877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. West C., Davis N. C., Forristal J., Herbst J., Spitzer R. Antigenic determinants of human beta-1c and beta-1g-globulins. J Immunol. 1966 Apr;96(4):650–658. [PubMed] [Google Scholar]
  44. Zucker-Franklin D. The percentage of monocytes among "mononuclear" cell fractions obtained from normal human blood. J Immunol. 1974 Jan;112(1):234–240. [PubMed] [Google Scholar]

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