- Top of page
- Conversion of cytokines and growth factors
- Proteinase 3 converts TNF-α
- Proteinase 3 activates IL-1β
- Proteinase 3 activates IL-18
- HLE activates EGFR
- HLE may activate toll-like receptor-4
- Cathepsin G activates protease-activated receptor-4
- Caspase-like activity
- Shedding of receptors and cytokines
- Therapeutic approaches
- Conflict of interest statement
Abstract. Wiedow O, Meyer-Hoffert U (University Kiel, Kiel, Germany; and Karolinska Institute, Stockholm, Sweden). Neutrophil serine proteases: potential key regulators of cell signalling during inflammation (Review). J Intern Med 2005; 257: 319–328.
The serine proteases cathepsin G, human leucocyte elastase and proteinase 3 are major contents of neutrophils and are released at sites of inflammation. The common picture of their function was that they do not degrade extracellular proteins specifically. Recent studies provided evidence that these proteases are able to activate specifically pro-inflammatory cytokines and lead to the activation of different receptors. Neutrophil serine proteases might therefore be important regulators of inflammatory processes and are interesting targets for new therapeutic approaches against inflammatory disorders. This review summarizes the current knowledge on the regulation of cell signalling by neutrophil serine proteases.