NDT Advance Access originally published online on February 13, 2007
Nephrology Dialysis Transplantation 2007 22(5):1301-1304; doi:10.1093/ndt/gfl847
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© The Author [2007]. Published by Oxford University Press on behalf of ERA-EDTA. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Sialylated therapeutic IgG: a sweet remedy for inflammatory diseases?*


INSERM UMRS 872 Equipe 16- Immunopathology and therapeutic immunointervention and Université Pierre et Marie Curie (UPMC-Paris-6), Centre de Recherche des Cordeliers, 15, rue de lEcole de Médecine, Paris 75006, France
Correspondence and offprint requests to: Dr Srini V. Kaveri, INSERM UMRS 872 Equipe 16, Centre de Recherche des Cordeliers, 15, rue de lEcole de Médecine, Paris 75006, France. Email: srini.kaveri@umrs681.jussieu.fr
Keywords: Fc gamma receptor; intravenous immunoglobulin; therapeutic IgG
| The first 10% of the full text of this article appears below. |
| Introduction |
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Immunoglobulin G (IgG) is the main serum glycoprotein responsible for detection and destruction of pathogens or their noxious products. IgG consists of Fab (fragment antigen binding) regions, that recognize antigenic targets and provide diversity to antibodies, and Fc (fragment crystallizable) regions, that allow antibodies to interact with Fc gamma receptors (Fc
R) on phagocytes (Fig. 1). Currently, four classes of Fc
R are identified: Fc
RI, Fc
RII, Fc
RIII and Fc
RIV [1]. For the initiation of a biological response against the bound antigen, IgGs rely on their constant Fc portion. CH2 domains of the Fc fragment contain complex oligosaccharide structures covalently attached to asparagine 297 of the heavy chain of the IgG [2,3]. The presence of a complex oligosaccharide structure modulates the functions of IgG, especially the | Overview of the study by Kaneko et al. [5] |
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| Discussion |
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| Perspective |
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