Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor.

Abstract:

:The recently cloned ligand binding component of the type I human interferon-alpha/beta receptor (IFN-alpha/beta R) 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-alpha/beta R. We find that the 51-kDa IFN-alpha/beta R. Two types of cDNA clones were isolated and sequenced, a 1.5-kb cDNA coding for the transmembrane 51-kDa IFN-alpha/beta R and a 4.5-kb cDNA coding for p40. In addition to ligand binding, IFN-alpha/beta R 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.

journal_name

J Leukoc Biol

authors

Novick D,Cohen B,Tal N,Rubinstein M

doi

10.1002/jlb.57.5.712

subject

Has Abstract

pub_date

1995-05-01 00:00:00

pages

712-8

issue

5

eissn

0741-5400

issn

1938-3673

journal_volume

57

pub_type

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