TY - JOUR
T1 - FcR γ chain deletion results in pleiotrophic effector cell defects
AU - Takai, Toshiyuki
AU - Li, Min
AU - Sylvestre, Diana
AU - Clynes, Raphael
AU - Ravetch, Jeffrey V.
N1 - Funding Information:
nique Flamand for generously providing reagents and helpful discussions; Annemarie Walsh, Michelle Inserra, Vera Soares, and Elizabeth H. Lacy for helpful instructions in ES cell culturing, microinjection, and mouse breeding; J. Carter Ralphe for technical assistance; Cynthia Ritter for secretarial assistance; and our colleagues for helpful criticisms. T. T. is supported by Yamada Science Foundation, Mochida Memorial Medical and Pharmaceutical Research Foundation, and Shi-mazu Science and Technology Foundation. This work was supported by grants from the National Institutes of Health to J. V. Ft.
PY - 1994/2/11
Y1 - 1994/2/11
N2 - The γ subunit of immunoglobulin Fc receptors is an essential component of the high-affinity receptor for IgE (FcεRI) and the low-affinity receptor for IgG (FcγRIII) and is associated with the high-affinity receptor for IgG (FcγRI) and the T cell receptor-CD3 complex. It is required for both receptor assembly and signal transduction. Targeted disruption of this subunit results in immunocompromised mice. Activated macrophages from γ chain-deficient mice unexpectedly lack the ability to phagocytose antibody-coated particles, despite normal binding. Defects in NK cell-mediated antibody-dependent cytotoxicity and mast cell-mediated allergic responses are evident in these animals, establishing the indispensable role of FcRs in these responses. However, loss of γ chain does not appear to perturb T cell development, since both thymic and peripheral T cell populations appear normal. These mice thus represent an important tool for evaluating the role of these receptors in humoral and cellular immune responses.
AB - The γ subunit of immunoglobulin Fc receptors is an essential component of the high-affinity receptor for IgE (FcεRI) and the low-affinity receptor for IgG (FcγRIII) and is associated with the high-affinity receptor for IgG (FcγRI) and the T cell receptor-CD3 complex. It is required for both receptor assembly and signal transduction. Targeted disruption of this subunit results in immunocompromised mice. Activated macrophages from γ chain-deficient mice unexpectedly lack the ability to phagocytose antibody-coated particles, despite normal binding. Defects in NK cell-mediated antibody-dependent cytotoxicity and mast cell-mediated allergic responses are evident in these animals, establishing the indispensable role of FcRs in these responses. However, loss of γ chain does not appear to perturb T cell development, since both thymic and peripheral T cell populations appear normal. These mice thus represent an important tool for evaluating the role of these receptors in humoral and cellular immune responses.
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U2 - 10.1016/0092-8674(94)90115-5
DO - 10.1016/0092-8674(94)90115-5
M3 - Article
C2 - 8313472
AN - SCOPUS:0028042424
SN - 0092-8674
VL - 76
SP - 519
EP - 529
JO - Cell
JF - Cell
IS - 3
ER -