Alleles of the Ly-17 alloantigen define polymorphisms of the murine IgG Fc receptor.

AUTOR(ES)

Holmes, K L

RESUMO

Antibodies specific for allelic determinants of the cell membrane alloantigen Ly-17 were found to react with genetically determined polymorphic sites on the murine IgG Fc receptor (Fc gamma R). Monoclonal antibodies specific for Ly-17.2 and the Fc gamma R detected identical populations of cells in thymus, spleen, lymph node, and bone marrow and had nearly identical reactivity with a large number of hematopoietic neoplasms. Antibodies to the Fc gamma R and either allele of Ly-17 blocked binding of rabbit IgG dimers to the Fc gamma R on spleen and bone marrow cells. Antibodies to the Fc gamma R also blocked binding of antibodies to either allele of Ly-17, whereas anti-Ly-17 antibodies only partially blocked the binding of antibodies to the Fc gamma R. Biochemical studies showed that antibodies to Ly-17 and the Fc gamma R precipitated proteins of Mr 55,000-60,000. The identity of the proteins recognized by these antibodies was confirmed by sequential immunoprecipitation.

Documentos Relacionados

• Association of the high-affinity receptor for IgG (Fc gamma RI) with the gamma subunit of the IgE receptor.
• 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.
• Physical association between the high-affinity IgG receptor (Fc gamma RI) and the gamma subunit of the high-affinity IgE receptor (Fc epsilon RI gamma).
• Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium.
• Human immunoglobulin G (IgG) Fc receptor IIA (CD32) polymorphism and IgG2-mediated bacterial phagocytosis by neutrophils.