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Ken Fukuda, Youichiro Fujitsu, Naoki Kumagai, Teruo Nishida; Characterization of the Interleukin-4 Receptor Complex in Human Corneal Fibroblasts. Invest. Ophthalmol. Vis. Sci. 2002;43(1):183-188.
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purpose. To characterize the interleukin (IL)-4 receptor (IL-4R) complex in
human corneal fibroblasts.
methods. The presence of IL-4R subunit mRNAs and proteins in cultured human
corneal fibroblasts was examined by reverse transcription–polymerase
chain reaction and flow cytometry, respectively. The interaction of 125I-labeled IL-4 with specific cell surface receptors was
characterized by saturation binding and Scatchard analysis. The effects
of IL-4 on the tyrosine phosphorylation and subcellular localization of
signal transducer and activator of transcription 6 (STAT6) were
evaluated by immunoblot and indirect immunofluorescence analyses,
respectively. The concentration of eotaxin in cell culture supernatant
was measured by enzyme-linked immunosorbent assay.
results. Transcripts encoding the IL-4R components IL-4Rα, IL-2Rγc,
IL-13Rα1, and IL-13Rα2 were detected in human corneal fibroblasts;
IL-4Rα and IL-2Rγc proteins were also expressed on the cell
surface. The maximum number of IL-4 binding sites was 2.3 ×
104 per cell, and the dissociation constant for the
interaction of IL-4 with these sites was 10.1 ± 0.3 pM. IL-4
induced tyrosine phosphorylation of STAT6 as well as translocation of
this protein to the nucleus. Eotaxin release from corneal fibroblasts
stimulated by the combination of IL-4 and tumor necrosis factor-α was
inhibited by pretreatment of the cells with neutralizing antibodies to
conclusions. Cultured human corneal fibroblasts express high-affinity functional
IL-4Rs on the cell surface, suggesting that these cells may contribute
to the role of IL-4 as a key mediator of allergic reactions in the
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