Abstract
Since the elucidation of the structure of antibodies, it has been recognized that immunoglobulins (Ig) are bifunctional molecules which assemble the products of several genes, allowing the almost infinite diversity of antigen recognition and a large array of effector and regulatory functions. Families of V genes encode the variable regions of Ig heavy (H) and light (L) chains whereas a set of C genes encodes the H and L constant regions which define Ig isotypes. Associations of the variable regions form the antigen-binding site while the C terminal constant regions form the Fc part of the Ig molecule and bear the sites for functional activities. The use of proteolytic enzymes has allowed separation of the Fc region from the rest of the molecule. An Fc-less Ig is a pure antigen-binding unit (and has therefore be called F(ab) when monovalent and F(ab)′ 2 when divalent) whereas intact molecules, after binding to antigen, exert multiple effector and regulatory functions [1,2].
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Nezlin R. Immunoglobulin Structure and Function. In: Van Oss CJ, Van Regenmortel MHV, eds, Immunochemistry. New York: Marcel Dekker Inc; 1994: 3–45.
Fridman WH. Structure and function of immunoglobulins. In: Fridman WH, Sautès C, eds. Cell Mediated Effects of Immunoglobulins. Heidelberg: RG Landes Company, Springer; 1997: 128.
Paraskevas F, Lee ST, Orr KB, Israels G. A Receptor for Fc on Mouse B-Lymphocytes. J Immunol. 1972; 108: 1319–27.
Fridman WH, Sautès C. Cell Mediated Effects of Immunoglobulins. Heidelberg: RG Landes Company, Springer; 1997: 1–201.
Hulett MD, Hogarth MP. Molecular basis of the Fc receptor function. Adv Immunol. 1994; 57: 1–127.
Metzger H, Alcaraz G, Hohman R, Kinet JP, Pribluda V, Quarto R. The receptor with high affinity for immunoglobulin E. Annu Rev Immunol. 1986; 4: 419–70.
Capron M, Grangette C, Torpier G, Capron A. The second receptor for IgE in eosinophil effector function. Chem Immunol. 1989; 47: 128–78.
Coico RF, Siskind GW, Thorbecke J. Role of IgD and T cells in the regulation of humoral immune response. Immunol Rev. 1988; 105: 45–68.
Fridman WH. Fc Receptors and immunoglobulin-binding factors. FASEB J. 1991; 5: 2684–90.
Ravetch JV, Kinet JP. Fc receptors. Annu Rev Immunol. 1991; 9: 457–92.
Ran M, Katz B, Kimchi N. et al. In vivo acquisition of FcγRII expression on polyoma virus transformed cells derived from tumors of long latency. Cancer Res. 1991; 51: 612–8.
Daëron M. Fc receptor biology. Annu Rev Immunol. 1997; 15: 203–34.
Bonnerot C, Amigorena S, Choquet D, Pavlovich R, Choukroun V, Fridman WH. Role of associated γchain in tyrosine kinase activation via murine FcγRIII. EMBO J. 1992; 11: 2747–57.
Amigorena S, Salamero J, Davoust J, Fridman WH, Bonnerot C. Tyrosine-containing motif that transduces cell activation signals also determines internalization and antigen presentation via type III receptors for IgG. Nature. 1992; 358: 337–41.
Zhou MJ, Poo H, Todd III RF, Petty HR. Surface-bound immune complexes trigger transmembrane proximity between complement receptor type 3 and the neutrophil’s cortical microfilaments. J Immunol. 1992; 148: 3550–3.
Amigorena S, Bonnerot C, Drake J. et al. Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes. Science. 1992; 256: 1808–12.
Muta T, Kurosaki T, Misulovin Z, Sanchez M, Mussenzweig MC, Ravetch JV. A13-aminoacid motif in the cytoplasmic domain of FcγRIIB modulates B cell receptor signalling. Nature. 1994; 368: 70–3.
Daëron M, Latour S, Malbec O. et al. The same tyrosine-based inhibition motif in the intracytoplasmic domain of FcγRIIB, regulates negatively BCR-, TCR-and FcR-dependent cell activation. Immunity. 1995; 3: 635–46.
D’Ambrosio D, Hippen KH, Minskor T. SA. et al. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by FcγRIIBl. Science. 1995; 268: 293–6.
Ono M, Bolland S, Tempst P, Ravetch JV. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature. 1996; 383: 263–6.
Scharenberg AM, Kinet JP. The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? Cell. 1996; 87: 961–4.
Fridman WH, Rabourdin-Combe C, Neauport-Sautès C, Gisler RH. Characterization and function of T cell Fcγreceptor. Immunological Rev. 1981; 56: 51–88.
Sautès C. Soluble Fc receptor. In: Fridman WH, Sautès C, eds, Cell Mediated Effects of Immunoglobulins. Heidelberg: RG Landes Company, Springer; 1997: 139–63.
Lecoanet-Henchoz S, Gauchat J, Aubry J. et al. CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD 11 b-CD 18 and CD 11 c-CD 18. Immunity. 1995; 3: 119–25.
Galon J, Gauchat JF, Mazières N. et al. Soluble Fcγreceptor type III (FcγRIII, CD16) triggers cell activation through interaction with complement receptors. J Immunol. 1996; 157: 1184–92.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Fridman, W.H. (1998). Introduction to the field. In: van de Winkel, J.G.J., Hogarth, P.M. (eds) The Immunoglobulin Receptors and their Physiological and Pathological Roles in Immunity. Immunology and Medicine Series, vol 26. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5018-7_1
Download citation
DOI: https://doi.org/10.1007/978-94-011-5018-7_1
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6106-3
Online ISBN: 978-94-011-5018-7
eBook Packages: Springer Book Archive