Abstract
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.
MeSH Terms
Amidohydrolases
Amino Acid Sequence
Binding, Competitive
Cells, Cultured
Chromatography
Chromatography, High Pressure Liquid
Dinoprostone/biosynthesis
Electrophoresis, Polyacrylamide Gel
Fibroblasts/metabolism
Glycosylation
Humans
Interleukin 1 Receptor Antagonist Protein
Interleukin-1/antagonists & inhibitors
Molecular Sequence Data
Monocytes/metabolism
Peptide Fragments
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Proteins/isolation & purification,metabolism,pharmacology
Receptors, Immunologic/antagonists & inhibitors,metabolism
Receptors, Interleukin-1
Recombinant Proteins/metabolism,pharmacology
Sialoglycoproteins
Chemicals
IL1RN protein, human
Interleukin 1 Receptor Antagonist Protein
Interleukin-1
Peptide Fragments
Proteins
Receptors, Immunologic
Receptors, Interleukin-1
Recombinant Proteins
Sialoglycoproteins
Amidohydrolases
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Dinoprostone
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Hannum C H
Synergen Inc., Boulder, Colorado 80301.
Wilcox C J
Arend W P
Joslin F G
Dripps D J
Heimdal P L
Armes L G
Sommer A
Eisenberg S P
Thompson R C