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1 From the Departments of Biomolecular Recognition and Ophthalmology and 2 Ocular Pathophysiology, Yamaguchi University School of Medicine, Ube City, Yamaguchi, Japan.
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-4R
, IL-2R
c,
IL-13R1, and IL-13R2 were detected in human corneal fibroblasts;
IL-4R and IL-2Rc proteins were also expressed on the cell
surface. The maximum number of IL-4 binding sites was 2.3 x
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- was
inhibited by pretreatment of the cells with neutralizing antibodies to
IL-4R.
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 cornea.
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