Endogenous metalloprotease solubilizes IL-13 receptor α2 in airway epithelial cells

Mikiko Matsumura, Hiromasa Inoue, Takafumi Matsumoto, Takako Nakano, Satoru Fukuyama, Koichiro Matsumoto, Koichi Takayama, Makoto Saito, Koji Kawakami, Yoichi Nakanishi

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


IL-13 receptor α2 (IL-13Rα2) has been postulated to be a decoy receptor. The precise mechanisms for the generation of soluble IL-13Rα2 and the biological activity of the endogenous soluble form have not been reported. Hypothesizing that the soluble form of IL-13Rα2 is generated by proteolytic cleavage of membrane-bound receptors, we transfected human airway epithelial cells with adenoviral vectors encoding full-length IL-13Rα2. Eotaxin production from IL-13Rα2-transfected cells was suppressed, and soluble IL-13Rα2 in the supernatants was increased time-dependently after the transfection. The transfer of conditioned media from IL-13Rα2-transfected cells inhibited IL-13-induced eotaxin production and STAT6 phosphorylation in non-transfected cells. PMA enhanced the release of soluble IL-13Rα2, and metalloprotease inhibitors inhibited this release. These findings suggest that airway epithelial cells with upregulation of membrane-bound IL-13Rα2 secrete soluble IL-13Rα2 into its supernatant, causing the autocrine and paracrine downregulation of the IL-13/STAT6 signal. Metalloprotease(s) are responsible for the proteolytic cleavage of cell surface IL-13Rα2.

Original languageEnglish
Pages (from-to)464-469
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Aug 24 2007

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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