Abstract
SLPI (secretory leucoprotease inhibitor) and elafin represent the archetypal members of the WFDC [WAP (whey acidic protein) four disulfide core] family of proteins, and were originally characterized as protease inhibitors but have since been shown to possess a wider repertoire of activities. These functions include antimicrobial and immunomodulatory properties, suggesting that these proteins may play key roles in the innate immune response, and indicate the potential to develop some of these proteins as novel therapeutics. Susceptibility to host and bacterial protease cleavage may, however, limit the efficacy of recombinant protein therapies in diseases with a high protease burden such as CF (cystic fibrosis) lung disease. To overcome this problem, further refinement of the native proteins will be required to provide effective treatment strategies.
Original language | English |
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Pages (from-to) | 1437-40 |
Number of pages | 4 |
Journal | Biochemical Society Transactions |
Volume | 39 |
Issue number | 5 |
DOIs | |
Publication status | Published - Oct 2011 |
Keywords
- Anti-Bacterial Agents
- Antiviral Agents
- Elafin
- Humans
- Immunologic Factors
- Protease Inhibitors
- Secretory Leukocyte Peptidase Inhibitor
- Journal Article
- Research Support, Non-U.S. Gov't
- Review