Novick D, Cohen B, Tal N, Rubinstein M
Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel.
J Leukoc Biol. 1995 May;57(5):712-8. doi: 10.1002/jlb.57.5.712.
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.
对最近克隆的I型人干扰素α/β受体（IFN-α/βR）的配体结合成分及其可溶性类似物（p40）进行了表征。p40是I型干扰素的有效抑制剂，针对p40的抗体可完全阻断I型干扰素在人细胞中的活性。这些抗体免疫沉淀细胞中102 kDa（主要）和51 kDa（次要）形式的IFN-α/βR。我们发现51 kDa的IFN-α/βR。分离并测序了两种类型的cDNA克隆，一种是编码跨膜51 kDa IFN-α/βR的1.5 kb cDNA，另一种是编码p40的4.5 kb cDNA。除了配体结合外，IFN-α/βR还直接参与信号传导，因为它在配体结合时在酪氨酸残基处发生磷酸化，并且与细胞质酪氨酸激酶JAK1存在物理关联。
