Open AccessExpression cloning of the murine and human interleukin 9 receptor cDNAs.
Author(s) -
JeanChristophe Renauld,
C Druez,
Abdenaim Kermouni,
Frédéric Houssiau,
Catherine Uyttenhove,
Emiel Van Roost,
Jacques Van Snick
Publication year - 1992
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.12.5690
Subject(s) - complementary dna , microbiology and biotechnology , biology , expression cloning , clone (java method) , signal peptide , lymphokine , cloning (programming) , receptor , cell surface receptor , transfection , transmembrane protein , transmembrane domain , peptide sequence , cell culture , gene , genetics , antigen , computer science , programming language
Interleukin 9 (IL-9) is a T-cell-derived lymphokine that induces the proliferation of various lymphoid and hemopoietic cells. A cDNA clone encoding the murine IL-9 receptor was isolated by expression cloning in COS cells and screening with 125I-labeled IL-9. Transient expression of this cDNA produced high-affinity binding sites for IL-9. The predicted 52-kDa protein contains a putative signal peptide and a typical transmembrane domain. A cDNA for the human homologue was isolated by cross-hybridization. Transfection of this cDNA in a murine T-cell clone conferred responsiveness to human IL-9. Sequence analysis revealed that the IL-9 receptor belongs to the recently described hematopoietin receptor super-family and is expressed in membrane-bound and soluble forms.
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