SLPI and elafin: multifunctional antiproteases of the WFDC family

Aaron Scott, Sinéad Weldon, Clifford C Taggart

Research output: Contribution to journalReview articlepeer-review

73 Citations (Scopus)

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 languageEnglish
Pages (from-to)1437-40
Number of pages4
JournalBiochemical Society Transactions
Volume39
Issue number5
DOIs
Publication statusPublished - 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

Fingerprint

Dive into the research topics of 'SLPI and elafin: multifunctional antiproteases of the WFDC family'. Together they form a unique fingerprint.

Cite this