Soluble and membrane-anchored forms of the human IFN-α/β receptor
Copyright policy )Soluble and membrane-anchored forms of the human IFN-α/β receptor
Abstract The recently cloned ligand binding component of the type I human interferon-α/β receptor (IFN-α/βR) and its soluble analogue (p40) were characterized. p40 is a potent inhibitor of type I IFNs and antibodies directed against p40 completely block the activity of type I IFNs in human cells. These antibodies immunoprecipitate cellular 102-kDa (major) and 51-kDa (minor) forms of IFN-α/βR. We find that the 51-kDa IFN-α/βR is a disulfide-linked subunit of the 102-kDa IFN-α/βR. Two types of cDNA clones were isolated and sequenced, a 1.5-kb cDNA coding for the transmembrane 51-kDa IFN-α/βR and a 4.5-kb cDNA coding for p40. In addition to ligand binding, IFN-α/βR is directly involved in signaling, because it becomes phosphorylated at Tyr residues on ligand binding and it is physically associated with the cytoplasmic tyrosine kinase JAK1. J. Leukoc. Biol. 57: 712–718; 1995.
Binding Sites, DNA, Complementary, Base Sequence, Blotting, Western, Molecular Sequence Data, Gene Expression, Membrane Proteins, Receptors, Cell Surface, Receptor, Interferon alpha-beta, Ligands, Peptide Fragments, Solubility, Humans, Amino Acid Sequence, RNA, Messenger, Receptors, Interferon
Binding Sites, DNA, Complementary, Base Sequence, Blotting, Western, Molecular Sequence Data, Gene Expression, Membrane Proteins, Receptors, Cell Surface, Receptor, Interferon alpha-beta, Ligands, Peptide Fragments, Solubility, Humans, Amino Acid Sequence, RNA, Messenger, Receptors, Interferon
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