Cell Type-Specific Glycoforms of FcγRIIIa (CD16): Differential Ligand Binding

Journal of Immunology

Volumn 159, Issue 8, 1997, Pages 3849-3857

  Edberg, Jeffrey C ^a   Kimberly, Robert P ^a  

^a The University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; LIGAND; MANNOSIDE; OLIGOSACCHARIDE;

ARTICLE; BLOOD; CHEMISTRY; COMPARATIVE STUDY; GLYCOSYLATION; HUMAN; IMMUNOLOGY; ISOMERISM; METABOLISM; MONOCYTE; NATURAL KILLER CELL; PROTEIN BINDING; STRUCTURE ACTIVITY RELATION;

GLYCOSYLATION; HUMANS; ISOMERISM; KILLER CELLS, NATURAL; LIGANDS; MANNOSIDES; MONOCYTES; OLIGOSACCHARIDES; PROTEIN BINDING; RECEPTORS, IGG; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031572518     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (46)

1. Kimberly, R. P., J. E. Salmon, and J. C. Edberg. 1995. Receptors for immunoglobulin G: molecular diversity and implications for disease. Arthritis Rheum. 38:306.
2. Hulett, M. D., and P. M. Hogarth. 1994. Molecular basis of Fc receptor function. Adv. Immunol. 56:1.
3. Ravetch, J. V. 1994. Fc receptors: rubor redux. Cell 78:553.
4. Ravetch, J. V., and B. Perussia. 1989. Alternative membrane forms of FcγRIII (CD16) on human natural killer cells and neutrophils: cell type-specific expression of two genes that differ in single nucleotide substitutions. J. Exp. Med. 170:481.
5. Scallon, B. J., E. Scigliano, V. H. Freedman, M. C. Miedel, Y.-C. E. Pan, J. C. Unkeless, and J. P. Kochan. 1989. A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-anchored forms. Proc. Natl. Acad. Sci. USA 86:5079.
6. Anderson, C. L., R. J. Looney, D. J. Culp, D. H. Ryan, H. B. Fleit, M. J. Utell, M. W. Frampton, P. D. Morganelli, and P. M. Guyre. 1990. Alveolar and peritoneal macrophages bear three distinct classes of Fc receptors for IgG. J. Immunol. 145:196.
7. Vance, B. A., T. W. J. Huizinga, K. Wardwell, and P. M. Guyre. 1993. Binding of monomeric human IgG defines an expression polymorphism of FcγRIII on large granular lymphocyte/natural killer cells. J. Immunol. 151:6429.
8. Kimberly, R. P., N. J. Tappe, L. T. Merriam, P. B. Redecha, J. C. Edberg, S. Schwartzman, and J. E. Valinsky. 1989. Carbohydrates on human Fcγ receptors: interdependence of the classical IgG and nonclassical lectin-binding sites on human FcγRIII expressed on neutrophils. J. Immunol. 142:3923.
9. Uggla, C. K., M. Jondal, D. Kaplan, N. Flomenberg, and R. W. Knowles. 1987. Enhancement of natural killer cell activity by unique antibodies within the CD2 (sheep-RBC receptor) and CD16 (Fc receptor) cluster. In Leukocyte Typing III. A. J. McMichael, ed. Oxford University Press, Oxford, p. 134.
10. Ravetch, J. V., and B. Perussia. 1991. FcγRIII (CD16) on human macrophages is a functional product of the FcγRIII-2 gene. Eur. J. Immunol. 21:425.
11. Edberg, J. C., M. Barinsky, P. B. Redecha, J. E. Salmon, and R. P. Kimberly. 1990. FcγRIII expressed on cultured monocytes is a N-glycosylated transmembrane protein distinct from FcγRIII expressed on natural killer cells. J. Immunol. 144:4729.
12. De Haas, M., M. Kleijer, R. M. Minchinton, D. Roos, and A. E. G. von dem Borne. 1994. Soluble FcγRIIIa is present in plasma and is derived from natural killer cells. J. Immunol. 152:900.
13. Fleit, H. B., C. D. Kobasiuk, N. S. Peress, and S. A. Fleit. 1992. A common epitope is recognized by monoclonal antibodies prepared against purified human neutrophil FcγRIII (CD16). Clin. Immunol. Immunopathol. 62:16.
14. Edberg, J. C., and R. P. Kimberly. 1992. Receptor specific probes for the study of individual Fcγ receptor function. J. Immunol Methods 148:179.
15. Fleit, H. B., S. D. Wright, and J. C. Unkeless. 1982. Human neutrophil Fcγ receptor distribution and structure. Proc. Natl. Acad. Sci. USA 79:3275.
16. Cummings, R. D., and S. Kornfeld. 1982. Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography: a rapid, sensitive, and specific technique. J. Biol. Chem. 257:11235.
17. Osawa, T., and T. Tsuji. 1987. Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins. Annu. Rev. Biochem. 56:21.
18. Wu, J., J. C. Edberg, P. B. Redecha, V. Bansal, P. M. Guyre, K. Coleman, J. E. Salmon, and R. P. Kimberly. 1997. A novel polymorphism of FcγRIIIa (CD16) alters receptor function and predisposes to autoimmune disease. J. Clin. Invest. 100:1059.
19. De Haas, M., H. R. Koene, M. Kleijer, E. de Vries, S. Simsek, M. J. D. van Tol, D. Roos, and A. E. G. K. von dem Borne. 1996. A triallelic Fcγ receptor type IIIA polymorphism influences the binding of human IgG by NK cell FcγRIIIA. J. Immunol. 156:2948.
20. Hibbs, M. L., M. Tolvanen, and O. Carpen. 1994. Membrane-proximal Ig-like domain of FcγRIII (CD16) contains residues critical for ligand binding. J. Immunol. 152:4466.
21. Warmerdam, P. A. M., J. G. J. van de Winkel, A. Vlug, N. A. C. Westerdal, and P. J. A. Capel. 1991. A single amino acid in the second Ig-like domain of the human Fcγ receptor II is critical for human IgG2 binding. J. Immunol. 147:1338.
22. Salmon, J. E., J. C. Edberg, N. Brogle, and R. P. Kimberly. 1992. Allelic polymorphisms of human Fcγ receptor IIA and Fcγ receptor IIIB: independent mechanisms for differences in human phagocyte function. J. Clin. Invest. 89:1274.
23. + blood monocytes exhibits features of tissue macrophages. Eur. J. Immunol. 23: 2053.
24. Edberg, J. C., P. B. Redecha, J. E. Salmon, and R. P. Kimberly. 1989. Human FcγRIII (CD16): isoforms with distinct allelic expression, extracellular domains, and membrane linkages on polymorphonuclear and natural killer cells. J. Immunol. 143:1642.
25. Huizinga, T. W. J., M. de Haas, M. Kleijer, J. H. Nuijens, D. Roos, and A. E. G. von dem Borne. 1990. Soluble Fcγ receptor III in human plasma originates from release by neutrophils. J. Clin. Invest. 86:416.
26. Clarkson, S. B., J. B. Bussel, R. P. Kimberly, J. E. Valinsky, R. L. Nachman, and J. C. Unkeless. 1986. Treatment of refractory immune thrombocytopenic purpura with an anti-Fcγ-receptor antibody. N. Engl. J. Med. 314:1236.
27. Clarkson, S. B., R. P. Kimberly, J. E. Valinsky, M. D. Witmer, J. B. Bussel, R. L. Nachman, and J. C. Unkeless. 1986. Blockade of clearance of immune complexes by an anti-Fcγ receptor monoclonal antibody. J. Exp. Med. 164:474.
28. Kimberly, R. P., J. C. Edberg, L. T. Merriam, S. B. Clarkson, J. C. Unkeless, and R. P. Taylor. 1989. The in vivo handling of soluble complement fixing Ab/ dsDNA immune complexes in chimpanzees. J. Clin. Invest. 84:962.
29. Taylor, R. P., J. Burge, C. Horgan, and D. M. Shasby. 1983. The complement-mediated binding of soluble antibody/dsDNA immune complexes to human neutrophils. J. Immunol. 130:2656.
30. Wilson, A. B., and R. R. Coombs. 1985. Fcγ-receptor-bearing, non-B lymphocytes in human peripheral blood: cytophilic immunoglobulin binds almost exclusively to large granular lymphocytes. Cell. Immunol. 90:196.
31. Sulica, A., C. Galatiuc, M. Manciulea, A. C. Bancu, A. DeLeo, T. L. Whiteside, and R. B. Herberman. 1993. Regulation of human natural cytotoxicity by IgG. IV. Association between binding of monomeric IgG to the Fc receptors on large granular lymphocytes and inhibition of natural killer (NK) cell activity. Cell. Immunol. 147:397.
32. Anasetti, C., P. J. Martin, Y. Morishita, C. C. Badger, I. D. Bernstein, and J. A. Hensen. 1987. Human large granular lymphocytes express high affinity receptors for murine monoclonal antibodies of the IgG3 subclass. J. Immunol. 138:2979.
33. PMN (CD16) in paroxysmal nocturnal hemoglobinuria: discordant expression of glycosyl phosphatidylinositol-linked proteins. J. Clin. Invest. 87:58.
34. Miller, K. L., A. M. Duchemin, and C. L. Anderson. 1996. A novel role for the Fc receptor γ-subunit: enhancement of FcγR ligand affinity. J. Exp. Med. 183: 2227.
35. Hibb, M. L., P. Selvaraj, O. Carpen, T. A. Springer, H. Kuster, M. Jouvin, and J.-P. Kinet. 1989. Mechanisms for regulating expression of membrane isoforms of FcγRIII (CD16). Science 246:1608.
36. Kinet, J.-P. 1992. The γ-ζ dimers of Fc receptors as connectors to signal transduction. Curr. Opin. Immunol. 4:43.
37. Blank, U., C. S. Ra, and J.-P. Kinet. 1991. Characterization of truncated alpha chain products from human, rat, and mouse high affinity receptor for immunoglobulin E. J. Biol. Chem. 266:2639.
38. Opdenakker, G., P. M. Rudd, C. P. Ponting, and R. A. Dwek. 1993. Concepts and principles of glycobiology. FASEB J. 7:1330.
39. Baenziger, J. U. 1994. Protein-specific glycosyltransferases: how and why they do it. FASEB J. 8:1019.
40. Hoover, R. G., C. Lary, R. Page, P. Travis, R. Owens, J. Flick, J. Kornbluth, and B. Barlogie. 1995. Autoregulatory circuits in myeloma: tumor cell cytotoxicity mediated by soluble CD16. J. Clin. Invest. 95:241.
41. Zhou, M., R. F. Todd, J. G. J. van de Winkel, and H. R. Petty. 1993. Co-capping of the leukoadhesin molecules complement receptor type 3 and lymphocyte function-associated antigen-1 with Fcγ receptor III on human neutrophils: possible role of lectin-like interactions. J. Immunol. 150:3030.
42. Jones, D. H., R. J. Looney, and C. L. Anderson. 1985. Two distinct classes of IgG Fc receptors on a human monocyte line (U937) defined by differences in binding of murine IgG subclasses at low ionic strength. J. Immunol. 135:3348.
43. Kimberly, R. P., J. E. Salmon, J. B. Bussel, M. K. Crow, and M. W. Hilgartner. 1984. Modulation of mononuclear phagocyte function by intravenous γ-globulin. J. Immunol. 132:745.
44. Bussel, J. B., R. P. Kimberly, R. D. Inman, I. Schulman, C. Cunningham-Ruddles, N. Cheung, E. M. Smithwick, J. O'Malley, S. Barandum, and M. W. Hilgartner. 1983. Intravenous gammaglobulin treatment of chronic idiopathic thrombocytopenic purpura. Blood 62:480.
45. 123I-labeled aggregates of IgG in patients with systemic lupus erythematosus: effect of serum IgG and numbers of erythrocyte complement receptor type 1. Arthritis Rheum. 34:442.
46. Kelton, J. G., J. Singer, C. Rodger, J. Gauldie, P. Horsewood, and P. Dent. 1985. The concentration of IgG in the serum is a major determinant of Fc-dependent reticuloendothelial function. Blood 66:490.