title: Isolation and expression of functional high-affinity Fc receptor complementary DNAs.
abstract: Human and murine mononuclear phagocytes express a high-affinity receptor for immunoglobulin G that plays a central role in macrophage antibody-dependent cellular cytotoxicity and clearance of immune complexes. The receptor (FcRI) may also be involved in CD4-independent infection of human macrophages by human immunodeficiency virus. This report describes the isolation of cDNA clones encoding the human FcRI by a ligand-mediated selection technique. Expression of the cDNAs in COS cells gave rise to immunoglobulin G binding of the expected affinity and subtype specificity. RNA blot analysis revealed expression of a 1.7-kilobase transcript in macrophages and in cells of the promonocytic cell line U937 induced with interferon-gamma. The extracellular region of FcRI consists of three immunoglobulin-like domains, two of which share homology with low-affinity receptor domains.
authors.affiliation: Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.
authors.forename: J M
authors.initials: JM
authors.lastname: Allen
authors.forename: B
authors.initials: B
authors.lastname: Seed
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011110:Polymorphism, Genetic; D011961:Receptors, Fc / Q000235:genetics*; D014162:Transfection
chemical_list: D011961:Receptors, Fc; D004247:DNA