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Characterization of the Interaction Between Recombinant Human lnterferon‐γ and Its Receptor on Human Polymorphonuclear Leukocytes
Author(s) -
Hansen Brian D.,
Finbloom David S.
Publication year - 1990
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.47.1.64
Subject(s) - recombinant dna , biology , lability , receptor , ligand (biochemistry) , tumor necrosis factor alpha , binding site , neutrophile , microbiology and biotechnology , cell culture , in vitro , biochemistry , immunology , gene , genetics
The interaction of human recombinant interferon‐γ (rlFN‐γ) with human polymorphonuclear cells (PMN) was investigated. Bolton‐Hunter radioiodinated rlFN‐γ bound to PMN in a specific and saturable manner. Eleven hundred binding sites were observed with a K a of 0.56 x 10 10 M ‐1 . Binding to PMN was rapid with a K 1 of 9 x 10 5 M ‐1 sec ‐1 at 4°C. At 37°C binding was complete within 6 min. About 50% of bound ligand was internalized within 30 min at 37°C. The receptor demonstrated moderate lability at 37°C in culture. After 1 h at 37°C, PMN lost 80% of their 125 l‐rlFN‐γ binding sites. This loss was reversed in part by the presence of interleukin‐1 in the culture, but not tumor necrosis factor. These studies provide a framework for further investigation into the signalling process of rlFN‐γ on PMN.