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Neutrophil serine proteases: potential key regulators of cell signalling during inflammation
Author(s) -
WIEDOW O.,
MEYERHOFFERT U.
Publication year - 2005
Publication title -
journal of internal medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.625
H-Index - 160
eISSN - 1365-2796
pISSN - 0954-6820
DOI - 10.1111/j.1365-2796.2005.01476.x
Subject(s) - proteases , cathepsin g , serine , elastase , inflammation , neutrophil elastase , microbiology and biotechnology , cathepsin , extracellular , proteinase 3 , biology , immunology , biochemistry , enzyme , phosphorylation , myeloperoxidase
. 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.