Structure and function of immunoglobulin domains. VIII. An analysis of the structural requirements in human IgG1 for binding to the Fc receptor of human monocytes.

A human mononuclear cell population, enriched with monocytes by adhering them to microexudate on Petri dishes previously used for fibroblast cultures was used in a homologous human system to form EA rosettes. IgG1, Fc, and subfragments of Fc representing the C gamma 2 and C gamma 3 domains were tested for their ability to inhibit rosette formation. Although Fc and IgG were equally effective in inhibiting rosette formation over the concentration range 10(-6) to 10(-5) M, all subfragments were inactive at these concentrations. At 10-fold higher concentrations the C gamma 2 fragment was still inactive; however, both the C gamma 3 fragments, pFc' and at C gamma 3, did show significant activity at this higher level. Reduction and alkylation diminished the inhibitory capacity of IgG 10-fold but had a lesser effect on Fc. In a parallel series of experiments the ability of IgG and Fc to inhibit granulocyte rosettes was found to be markedly diminished by reduction and alkylation in both cases. These experiments reveal differences between Fc receptors in different cells, confirm a role for the C gamma 3 homology region in monocyte Fc receptor recognition, but do suggest a requirement, either direct or indirect, for the C gamma 2 domain.

• Publication year

  1980

• Venue

  Journal of Immunology

• Publication date

  1980-05-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.4049/jimmunol.124.5.2186PMID 7365252
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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