Abstract
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.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
Cell Membrane/immunology
DNA/genetics
Female
Genomic Library
Humans
Interleukin-5/metabolism
Kinetics
Macromolecular Substances
Molecular Sequence Data
Placenta/physiology
Polymerase Chain Reaction/methods
Pregnancy
RNA Splicing
RNA, Messenger/genetics
Receptors, Immunologic/genetics,metabolism
Receptors, Interleukin
Receptors, Interleukin-5
Transfection
Chemicals
Interleukin-5
Macromolecular Substances
RNA, Messenger
Receptors, Immunologic
Receptors, Interleukin
Receptors, Interleukin-5
DNA
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Tavernier J
Roche Research Gent, Belgium.
Tuypens T
Plaetinck G
Verhee A
Fiers W
Devos R
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