Published April 30, 1996
by Springer .
Written in English
|Contributions||Jan G.J. van de Winkel (Editor), Peter J.A. Capel (Editor)|
|The Physical Object|
|Number of Pages||241|
CLINICAL IMMUNOLOGY AND IMMUNOPATHOL SS71 () Human IgG Fc Receptors' CLARK L. ANDERSON Department of Medicine, The Ohio State University College of Medicine, Columbus, Ohio Considerable recent progress has been made in our understanding of how IgG immune complexes interact with plasma membrane Fc receptors Cited by: Human IgG Fc receptor heterogeneity: molecular aspects and clinical implications. Receptors for the Fc domain of IgG (Fc gamma R) provide a critical link between specific humoral responses and the cellular branch of the immune system. When hFc gamma R interact with immunoglobulin, a variety of biological responses are triggered. These Cited by: IgG antibodies can act as opsonins, which in the context of this study, bind to general Aβ or pGlu-3 Aβ, to tag them for phagocytosis through recognition of the Fc portion of the antibody by the. A major difference between the complex of Fc with hFcγRI and that with other human Fcγ receptors is reflected in the relative orientation Cited by:
The Ig domain of FcμR is similar but distantly related to that of pIgR and Fcα/µR. FCMR is a single copy gene located on chromosome 1q, adjacent to two other IgM-binding receptor genes, PIGR and FCAMR. The Ig-like domain of FAIM3/TOSO/FcμR is thought to be involved in the binding of agonistic IgM anti-Fas mAb (Hitoshi et al., ).A comparison of the Cited by: Human and mouse Fc receptors for IgG (FcγRs) can be distinguished by their affinity for the antibody Fc-fragment and by the signalling pathways they induce. Mice and humans have one high-affinity receptor, FcγRI; all other FcRs have low to medium affinity for the antibody Fc fragment. With respect to. The unique features of the four human IgG subclasses are exam - ined by Theo Rispens and Gestur Vidarsson. Differences in the IgG isotype structures (e.g., variation in the hinge region, disulfide bonds, susceptibility to proteolysis) and their binding to effector molecules (e.g., C1q, Fc γRs) are detailed. The authors. MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price. Fc Receptors and Phagocytosis, p In Russell D, Gordon S (ed) The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J. by: 1.
Since the description of the first mouse knockout for an IgG Fc receptor seven years ago, considerable progress has been made in defining the in vivo functions of these receptors in diverse biological systems. The role of activating FcγRs in providing a critical link between ligands and effector cells in type II and type III inflammation is now well established and has led to a . IgG immune complexes are of central importance in the humoral immune system and strongly implicated in the pathogenesis of hematologic and rheumatic autoimmune disorders. Cross-linking of receptors for the Fc domain of IgG antibodies (FcγRs) triggers a wide variety of effector functions including phagocytosis, antibody-dependent cellular cytotoxicity, and release Cited by: Background Current anti-cancer therapeutic antibodies that are used in the clinic are predominantly humanized or fully human immunoglobulin G1 (IgG1). These antibodies bind with high affinity to the target antigen and are efficient in activating the immune system via IgG Fc receptors and/or complement. In addition to IgG1, three more isotypes are present in humans, Cited by: 3. Abstract. Glycosylation of IgG Fc domains is a central mechanism in the diversification of antibody function. Modifications to the core Fc glycan impact antibody function by shifting the balance of Type I and Type II Fc gamma receptors (FcγR) that will be engaged by immune by: 1.