Neutrophil serine proteases: potential key regulators of cell signalling during inflammation.
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.
Wiedow
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Department of Dermatology, University Kiel, Kiel, Germany.
Meyer-Hoffert
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D016207:Cytokines / Q000378:metabolism; D006133:Growth Substances / Q000378:metabolism; D006801:Humans; D007249:Inflammation / Q000188:drug therapy / Q000201:enzymology*; D009504:Neutrophils / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000502:physiology*; D015842:Serine Proteinase Inhibitors / Q000627:therapeutic use; D015398:Signal Transduction / Q000502:physiology
D016207:Cytokines; D006133:Growth Substances; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases