Isolation and expression of functional high-affinity Fc receptor complementary DNAs.

Article Details

Citation

Allen JM, Seed B

Isolation and expression of functional high-affinity Fc receptor complementary DNAs.

Science. 1989 Jan 20;243(4889):378-81.

PubMed ID
2911749 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
High affinity immunoglobulin gamma Fc receptor IP12314Details