Isolation and expression of functional high-affinity Fc receptor complementary DNAs.
Science
; 243(4889): 378-81, 1989 Jan 20.
Article
em En
| MEDLINE
| ID: mdl-2911749
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.
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Base de dados:
MEDLINE
Assunto principal:
Receptores Fc
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1989
Tipo de documento:
Article