Human neutrophils and eosinophils have structurally distinct Fc(γ) receptors

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Abstract

Human Fc(γ) receptors were isolated from surface radioiodinated granulocutes and eosinophils by using repetitive affinity chromatography on human IgG-Sepharose columns. Analysis by SDS-polyacrylamide gel electrophoresis demonstrated that cell preparations containing eosinophils possessed a 43,000 M(r) Fc(γ)-binding macromolecule. Nylon wool-filtered cells from patients with eosinophilia and cell cultures derived from normal donors provided highly purified eosinophil preparations that expressed only the 43,000 M(r) Fc(γ) receptor. Granulocyte populations yielded the 52,000 to 68,000 M(r) Fc(γ) receptor characteristic of neutrophils as well as the Fc(γ)-binding macromolecules apparently derived from eosinophils. The 43,000 M(r) Fc(γ) receptor of the eosinophil and the 31,000 and 34,000 M(r) fragments that appear to be derived from it were able to rebind selectively to human IgG1-Sepharose, Fc(γ1)-Sepharose, IgG3-Sepharose, and Fc(γ3)-Sepharose. In contrast, the 52,000 to 68,000 M(r) Fc(γ) receptor from neutrophils could rebind only to IgG1-Sepharose and Fc(γ1)-Sepharose. The results demonstrate that the Fc(γ) receptor of human eosinophils is distinct in structure from the neutrophil Fc(γ) receptor and that these Fc(γ) receptors, at least in their solubilized states, differ in specificity for human IgG3.

Original languageEnglish
Pages (from-to)849-854
Number of pages6
JournalJournal of Immunology
Volume133
Issue number2
StatePublished - 1984

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