Isolation and partial chemical characterization of the IgG Fc receptor of human T lymphocytes and production of an antiserum.
AUTOR(ES)
Cunningham-Rundles, C
RESUMO
We report here the isolation of an IgG Fc receptor from normal human T lymphocytes. The purified receptor has a nonreduced and a reduced component of molecular weights 120,000 and 60,000, respectively, and it was functionally active in the in vitro blocking of rosette formation between T lymphocytes and IgG-coated ox erythrocytes. An antiserum raised to the Fc receptor and an isolated F(ab')2 fragment of this antiserum, also blocked rosette formation between T cells and IgG-coated ox erythrocytes. In contrast, rosette formation between T lymphocytes and IgM-coated ox or sheep erythrocytes was not blocked by the F(ab')2 fragment, demonstrating the marked specificity of this antiserum for the IgG Fc receptor. In addition, this antiserum did not block the Fc receptors of non-T cells, indicating that the T-cell IgG Fc receptor has unique antigenic determinants not shared with B cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=349674Documentos Relacionados
- Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium.
- Production and characterization of monoclonal antibodies anti fragment Fc of bovine IgG
- A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions.
- Studies of lymphocytes in rheumatoid arthritis. I. Uptake of 125I-heat aggregated human IgG by Fc-receptor bearing lymphocytes.
- Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.
