A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF

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阅读量：

127

作者：

J Tavernier，R Devos，S Cornelis，T Tuypens，JVD Heyden，W Fiers，G Plaetinck

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摘要：

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.

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关键词：

EOSINOPHIL DIFFERENTIATION FACTOR , COLONY-STIMULATING FACTOR , MOLECULAR-CLONING , HISTAMINE-RELEASE , SOLUBLE FORM , GENE FAMILY , HUMAN-URINE , EXPRESSION , BINDING , CELLS

DOI：

10.1016/0092-8674(91)90040-6

被引量：

1262

年份：

1991