Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor

Three interleukin-1 inhibitors have been purified to homogeneity from medium conditioned by human monocytes. Partial sequence analysis and digestion with N-glycanase indicate that these are glycosylation forms of a single protein. The protein binds to the interleukin-1 receptor but has no interleuki...

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Bibliographic Details
Published in:Nature (London) 1990-01, Vol.343 (6256), p.336-340
Main Authors: Hannum, Charles H, Wilcox, Carol J, Arend, William P, Joslin, Fenneke G, Dripps, David J, Heimdal, Patricia L, Armes, Lyman G, Sommer, Andreas, Eisenberg, Stephen P, Thompson, Robert C
Format: Article
Language:English
Subjects:
Amidohydrolases
Amino Acid Sequence
Anion exchange
Anion exchanging
Beta protein
Binding
Binding, Competitive
Biological activity
Cells, Cultured
Chromatofocusing
Chromatography
Chromatography, High Pressure Liquid
Conditioning
Cytokines
Dinoprostone - biosynthesis
Electrophoresis, Polyacrylamide Gel
Fibroblasts - metabolism
Glycosylation
Humanities and Social Sciences
Humans
Immunity (Disease)
Inhibitors
Interleukin 1
Interleukin 1 receptor antagonist
Interleukin 1 Receptor Antagonist Protein
interleukin 1 receptors
Interleukin-1 - antagonists & inhibitors
man
Medical research
Molecular Sequence Data
Monocytes
Monocytes - metabolism
multidisciplinary
Peptide Fragments
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Physiology
Prostaglandin E2
Proteins
Proteins - isolation & purification
Proteins - metabolism
Proteins - pharmacology
Receptors, Immunologic - antagonists & inhibitors
Receptors, Immunologic - metabolism
Receptors, Interleukin-1
Recombinant Proteins - metabolism
Recombinant Proteins - pharmacology
Science
Science (multidisciplinary)
Sialoglycoproteins
Sugar
Urine
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Description
Summary:Three interleukin-1 inhibitors have been purified to homogeneity from medium conditioned by human monocytes. Partial sequence analysis and digestion with N-glycanase indicate that these are glycosylation forms of a single protein. The protein binds to the interleukin-1 receptor but has no interleukin-1-like activity, even at very high concentrations, and is therefore a pure receptor antagonist.
ISSN:0028-0836
1476-4687
DOI:10.1038/343336a0