Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit.
收藏PubMed Central1992-08-01 更新2026-05-16 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC49641/
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资源简介：
By use of a 3' extension PCR strategy, cDNA clones were isolated spanning the transmembrane region and a complete cytoplasmic domain of the human interleukin 5 receptor alpha subunit (hIL5R alpha). These cDNAs differ from previously isolated clones encoding a soluble hIL5R alpha form by a sequence switch at position 1243. When expressed in COS-1 cells, only low-affinity binding of 125I-labeled human interleukin 5 was observed. Coexpression of the hIL5R beta chain led to a 2-fold increase in binding affinity. In addition, this same cloning strategy allowed us to identify a putative second soluble isoform of hIL5R alpha. Genomic data revealed that the two soluble variants arise from either a "normal" splicing event or from the absence of splicing, whereas synthesis of the membrane-anchored form requires alternative splicing. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1992-08-01
