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Proteinase 3-processed form of the recombinant IL-32 separate domain

  • Kim, Sun-Jong (Department of Respiratory Medicine, Konkuk University) ;
  • Lee, Si-Young (Department of Immunology, Collage of Medicine, Konkuk University) ;
  • Her, Erk (Department of Immunology, Collage of Medicine, Konkuk University) ;
  • Bae, Su-Young (Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University) ;
  • Choi, Ji-Da (Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University) ;
  • Hong, Jae-Woo (Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University) ;
  • JaeKal, Jun (Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University) ;
  • Yoon, Do-Young (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Azam, Tania (Division of Infectious Diseases, University of Colorado Health Sciences Center) ;
  • Dinarello, Charles A. (Division of Infectious Diseases, University of Colorado Health Sciences Center) ;
  • Kim, Soo-Hyun (Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University)
  • Published : 2008.11.30

Abstract

Interleukin-32 (IL-32) induces a variety of proinflammatory cytokines and chemokines. The IL-32 transcript was reported originally in activated T cells; subsequently, it was demonstrated to be abundantly expressed in epithelial and endothelial cells upon stimulation with inflammatory cytokines. IL-32 is regulated robustly by other major proinflammatory cytokines, thereby suggesting that IL-32 is crucial to inflammation and immune responses. Recently, an IL-32$\alpha$-affinity column was employed in order to isolate an IL-32 binding protein, neutrophil proteinase 3 (PR3). Proteinase 3 processes a variety of inflammatory cytokines, including TNF$\alpha$, IL-$1{\beta}$, IL-8, and IL-32, thereby enhancing their biological activities. In the current study, we designed four PR3-cleaved IL-32 separate domains, identified by potential PR3 cleavage sites in the IL-32$\alpha$ and $\gamma$ polypeptides. The separate domains of the IL-32 isoforms $\alpha$ and $\gamma$ were more active than the intrinsic $\alpha$ and $\gamma$ isoforms. Interestingly, the N-terminal IL-32 isoform $\gamma$ separate domain evidenced the highest levels of biological activity among the IL-32 separate domains.

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