Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1977 May 1;145(5):1368–1381. doi: 10.1084/jem.145.5.1368

Association and dissociation of aggregated IgG from rat peritoneal macrophages

PMCID: PMC2180672  PMID: 859000

Abstract

Stable aggregated IgG (A-IgG) of various sizes, having high biological activity, were incubated at 4 degree C with adhering peritoneal macrophages from normal rats and the kinetics of A-IgG binding to the cell surface were studied. Equilibrium constants were high (2.8-11.7 X 10(8) M-1) and varied as a function of aggregate size. The maximum number of A-IgG bound per cell varied from 230,000 for A-IgG9 to 90,000 for A-IgG74. Binding was 50% inhibited by near physiological concentrations of monomeric IgC. These data suggest that A-IgG are bound at multiple sites by attachment of Fc frgments to Fc receptors present on the macrophage surface with larger A-IgG being more avidly bound. Dissociation was slower for larger A-IgG while no clear trend was seen relating associating rates and aggregate size. Thus, differences in the avidity of binding of A-IgG are due primarily to slower dissociation of larger A-IgG. Dissociationissociation of A-IgG was slower from cells exposed initially to higher doses of A-IgG and dissociation did not follow simple first order kinetics. Thus, the avidity of binding appears to be heterogeneous in a population of similar sized A-IgG. As expected, association was dose-dependent, more rapid than dissociation, and followed pseudo first order kinetics. Based on all of the above data, it is proposed that binding of A-IgG proceeds in two steps. First, A-IgG are loosely bound to perhaps a single Fc receptor. Then, depending upon the availability and mobility of Fc receptors, additional Fc fragments are attached and the A-IgG becomes more firmly attached. Thus binding is slow, but once attached A- IgG are avidly held.

Full Text

The Full Text of this article is available as a PDF (871.5 KB).

Selected References

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

  1. Abramson N., Lo Buglio A. F., Jandl J. H., Cotran R. S. The interaction between human monocytes and red cells. Binding characteristics. J Exp Med. 1970 Dec 1;132(6):1191–1206. doi: 10.1084/jem.132.6.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arend W. P., Mannik M. In vitro adherence of soluble immune complexes to macrophages. J Exp Med. 1972 Sep 1;136(3):514–531. doi: 10.1084/jem.136.3.514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Arend W. P., Mannik M. The macrophage receptor for IgG: number and affinity of binding sites. J Immunol. 1973 Jun;110(6):1455–1463. [PubMed] [Google Scholar]
  4. BENACERRAF B., SEBESTYEN M., COOPER N. S. The clearance of antigen antibody complexes from the blood by the reticuloendothelial system. J Immunol. 1959 Feb;82(2):131–137. [PubMed] [Google Scholar]
  5. Brown J. C., Harris G., Papamichail M., Sljivić V. S., Holborow E. J. The localization of aggregated human -globulin in the spleens of normal mice. Immunology. 1973 Jun;24(6):955–968. [PMC free article] [PubMed] [Google Scholar]
  6. CHRISTIAN C. L. Studies of aggregated gamma-globulin. I. Sedimentation, electrophoretic and anticomplementary properties. J Immunol. 1960 Jan;84:112–116. [PubMed] [Google Scholar]
  7. Cochrane C. G., Koffler D. Immune complex disease in experimental animals and man. Adv Immunol. 1973;16(0):185–264. doi: 10.1016/s0065-2776(08)60298-9. [DOI] [PubMed] [Google Scholar]
  8. Cowdery J. S., Jr, Treadwell P. E., Fritz R. B. A radioimmunoassay for human antigen-antibody complexes in clinical material. J Immunol. 1975 Jan;114(1 Pt 1):5–9. [PubMed] [Google Scholar]
  9. Dandliker W. B., Levison S. A. Investigation of antigen-antibody kinetics by fluorescence polarization. Immunochemistry. 1968 Mar;5(2):171–183. doi: 10.1016/0019-2791(68)90101-8. [DOI] [PubMed] [Google Scholar]
  10. Deutsch H. F., Fudenberg H. H. Immunoglobulin structure and function. Adv Intern Med. 1969;15:377–396. [PubMed] [Google Scholar]
  11. Haakenstad A. O., Mannik M. The disappearance kinetics of soluble immune complexes prepared with reduced and alkylated antibodies and with intact antibodies in mice. Lab Invest. 1976 Sep;35(3):283–292. [PubMed] [Google Scholar]
  12. Huber H., Polley M. J., Linscott W. D., Fudenberg H. H., Müller-Eberhard H. J. Human monocytes: distinct receptor sites for the third component of complement and for immunoglobulin G. Science. 1968 Dec 13;162(3859):1281–1283. doi: 10.1126/science.162.3859.1281. [DOI] [PubMed] [Google Scholar]
  13. ISHIZAKA K. Gamma globulin and molecular mechanisms in hypersensitivity reactions. Prog Allergy. 1963;7:32–106. [PubMed] [Google Scholar]
  14. Leslie R. G., Cohen S. Cytophilic activity of IgG2 from sera of guinea-pigs immunized with bovine gamma-globulin. Immunology. 1974 Oct;27(4):589–599. [PMC free article] [PubMed] [Google Scholar]
  15. Leslie R. G., Cohen S. Cytophilic activity of IgG2 from sera of unimmunized guinea-pigs. Immunology. 1974 Oct;27(4):577–587. [PMC free article] [PubMed] [Google Scholar]
  16. Mannik M., Arend M. P., Hall A. P., Gilliland B. C. Studies on antigen-antibody complexes. I. Elimination of soluble complexes from rabbit circulation. J Exp Med. 1971 Apr 1;133(4):713–739. doi: 10.1084/jem.133.4.713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mauer S. M., Fish A. J., Blau E. B., Michael A. F. The glomerular mesangium. I. Kinetic studies of macromolecular uptake in normal and nephrotic rats. J Clin Invest. 1972 May;51(5):1092–1101. doi: 10.1172/JCI106901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
  19. Phillips-Quagliata J. M., Levine B. B., Quagliata F., Uhr J. W. Mechanisms underlying binding of immune complexes to macrophages. J Exp Med. 1971 Mar 1;133(3):589–601. doi: 10.1084/jem.133.3.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Shinomiya T., Koyama J. In vitro uptake and digestion of immune complexes containing guinea-pig IgG1 and IgG2 antibodies by macrophages. Immunology. 1976 Feb;30(2):267–275. [PMC free article] [PubMed] [Google Scholar]
  21. Steensgaard J., Funding L. On the formulation of a reaction scheme for the interaction between an antigen and its antibody. Immunology. 1974 Feb;26(2):299–302. [PMC free article] [PubMed] [Google Scholar]
  22. TALMAGE D. W. The kinetics of the reaction between antibody and bovine serum albumin using the Farr method. J Infect Dis. 1960 Jul-Aug;107:115–132. doi: 10.1093/infdis/107.1.115. [DOI] [PubMed] [Google Scholar]
  23. Unkeless J. C., Eisen H. N. Binding of monomeric immunoglobulins to Fc receptors of mouse macrophages. J Exp Med. 1975 Dec 1;142(6):1520–1533. doi: 10.1084/jem.142.6.1520. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Van Oss C. J., Gillman C. F., Neumann A. W. Phagocytosis as a surface phenomenon. IV. The minimum size and composition of antigen-antibody complexes that can become phagocytized. Immunol Commun. 1974;3(1):77–84. doi: 10.3109/08820137409055746. [DOI] [PubMed] [Google Scholar]
  25. Van Oss C. J., Gillman C. F. Phagocytosis as a surface phenomenon. II. Contact angles and phagocytosis of encapsulated bacteria before and after opsonization by specific antiserum and complement. J Reticuloendothel Soc. 1972 Nov;12(5):497–502. [PubMed] [Google Scholar]
  26. Wellek B., Hahn H. H., Opferkuch W. Evidence for macrophage C3d-receptor active in phagocytosis. J Immunol. 1975 May;114(5):1643–1645. [PubMed] [Google Scholar]
  27. van Furth R. An approach to the characterization of mononuclear phagocytes involved in pathological processes. Agents Actions. 1976 Feb;6(1-3):91–98. doi: 10.1007/BF01972190. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES