Abstract
cDNA clones encoding two receptor proteins involved in the binding of human interleukin 5 (hIL5) have been isolated. A first class codes for an IL5-specific chain (hIL5R alpha). The major transcript of this receptor gene, as analyzed in both HL-60 eosinophilic cells and eosinophilic myelocytes grown from cord blood, encodes a secreted form of this receptor. This soluble hIL5R alpha has antagonistic properties. A second component of the hIL5R is found to be identical to the beta chain of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) high affinity receptor. The finding that IL5 and GM-CSF share a receptor subunit provides a molecular basis for the observation that these cytokines can partially interfere with each other's binding and have highly overlapping biological activities on eosinophils.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding, Competitive
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Blotting, Northern
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Cell Division
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Cell Line
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Cloning, Molecular
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Cross-Linking Reagents
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DNA / genetics
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Gene Expression
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Granulocyte-Macrophage Colony-Stimulating Factor / metabolism
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Humans
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In Vitro Techniques
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Interleukin-5 / metabolism
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Macromolecular Substances
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Molecular Sequence Data
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Molecular Structure
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Oligonucleotides / chemistry
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RNA, Messenger / genetics
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Receptors, Granulocyte-Macrophage Colony-Stimulating Factor / chemistry*
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Receptors, Immunologic / chemistry*
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Receptors, Immunologic / genetics
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Receptors, Immunologic / metabolism
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Receptors, Interleukin*
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Receptors, Interleukin-5
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Recombinant Proteins
Substances
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Cross-Linking Reagents
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Interleukin-5
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Macromolecular Substances
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Oligonucleotides
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RNA, Messenger
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Receptors, Granulocyte-Macrophage Colony-Stimulating Factor
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Receptors, Immunologic
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Receptors, Interleukin
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Receptors, Interleukin-5
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Recombinant Proteins
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Granulocyte-Macrophage Colony-Stimulating Factor
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DNA