Human Fc receptors for IgG.
Human lymphocytes bear at least three different classes of Fc gamma R, which are different in cellular distribution, structure, and function. This review deals with recent advances in understanding the complexity of huFc gamma R. In particular, studies demonstrating the presence of alternate phosphatidyl inositol glycan-anchored and transmembrane-anchored forms of huFc gamma RIII (CD16) are discussed.
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J C
JC
Department of Biochemistry, Mount Sinai School of Medicine, New York, New York, USA.
D002478:Cells, Cultured; D003602:Cytotoxicity, Immunologic; D018076:DNA, Complementary / Q000235:genetics; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D007694:Killer Cells, Natural / Q000378:metabolism; D008264:Macrophages / Q000378:metabolism; D009504:Neutrophils / Q000378:metabolism; D010587:Phagocytosis; D017452:Receptors, IgG / Q000145:classification* / Q000235:genetics / Q000378:metabolism
D018076:DNA, Complementary; D017261:Glycosylphosphatidylinositols; D007074:Immunoglobulin G; D017452:Receptors, IgG