FcgammaR: The key to optimize therapeutic antibodies?
- PMID: 17240158
- DOI: 10.1016/j.critrevonc.2006.12.003
FcgammaR: The key to optimize therapeutic antibodies?
Abstract
The binding of IgG to receptors for the Fc region of IgG (FcgammaR) is a critical step for the initiation and the control of effector immune functions. Activating FcgammaR induce antibody-dependent cell cytotoxicity (ADCC), endocytosis of immune complexes followed by antigen presentation, phagocytosis, and release of cytokines or pro-inflammatory mediators. By contrast, inhibitory FcgammaR regulate immune responses by inhibiting the activation of B lymphocytes, monocytes, mast cells and basophils, induced through activating receptors. Studies with FcgammaR-deficient mice support the critical role of the different FcgammaR in the in vivo functional effects of therapeutic monoclonal antibodies. Structural studies have provided detailed insights in the molecular mechanisms that govern IgG/FcgammaR interactions. The importance of the sugar components linked to asparagine 297 in the function of IgG has been also highlighted. These data have led to the engineering of a new generation of monoclonal antibodies for therapeutic use with optimized effector functions.
Comment in
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"Antibodies in cancer treatment".Crit Rev Oncol Hematol. 2007 Apr;62(1):23-5. doi: 10.1016/j.critrevonc.2007.02.004. Crit Rev Oncol Hematol. 2007. PMID: 17338979 No abstract available.
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