Abstract
Receptors for the Fc region of immunoglobulins (FcRs) have been identified on a variety of cell types and have been shown to promote multiple cellular functions.1,2 They are differentially expressed on different types of leucocyte and show slightly different subclass specificity.3 Only FcγRI binds to monomeric IgG with sufficient affinity that binding is likely to occur at physiological concentrations. Efficient binding of IgG to FcγRII and FcγRIII only occurs when the IgG is aggregated. Binding of aggregated IgG causes clustering of Fc receptors which triggers a biological response by the cell.
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© 1995 Springer Science+Business Media New York
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Stewart, W.W., Kerr, M.A. (1995). The Binding of Monomeric IgA to Myeloid FcαR: Evidence for Receptor Re-Cycling and Determination of its Affinity. In: Mestecky, J., Russell, M.W., Jackson, S., Michalek, S.M., Tlaskalová-Hogenová, H., Šterzl, J. (eds) Advances in Mucosal Immunology. Advances in Experimental Medicine and Biology, vol 371. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1941-6_138
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DOI: https://doi.org/10.1007/978-1-4615-1941-6_138
Publisher Name: Springer, Boston, MA
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