Journal
BMB REPORTS
Volume 41, Issue 11, Pages 814-819Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2008.41.11.814
Keywords
Cytokine; Human lung epithelial cell; Inflammation; Interleukin-32; Proteinase 3
Categories
Funding
- Korea Science and Engineering Foundation (KOSEF)
- Korean government (MOST) [R01-2006-000-10837]
- Korea Research Foundation [2006-E00119]
- NIH [Al-15614, HL-68743, CA-04 6934]
- Amgen, Inc
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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. [BMB reports 2008; 41(11): 814-819]
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