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 Bioljournal_title
Journal of leukocyte biologyauthors
Novick D,Cohen B,Tal N,Rubinstein Mdoi
10.1002/jlb.57.5.712subject
Has Abstractpub_date
1995-05-01 00:00:00pages
712-8issue
5eissn
0741-5400issn
1938-3673journal_volume
57pub_type
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journal_title:Journal of leukocyte biology
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journal_title:Journal of leukocyte biology
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更新日期:2014-08-01 00:00:00
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