Review
Nature Reviews Immunology 6, 541-550 (July 2006) | doi:10.1038/nri1841
Neutrophil serine proteases: specific regulators of inflammation
Christine T. N. Pham1 About the author
Abstract
Neutrophils are essential for host defence against invading pathogens. They engulf and degrade microorganisms using an array of weapons that include reactive oxygen species, antimicrobial peptides, and proteases such as cathepsin G, neutrophil elastase and proteinase 3. As discussed in this Review, the generation of mice deficient in these proteases has established a role for these enzymes as intracellular microbicidal agents. However, I focus mainly on emerging data indicating that, after release, these proteases also contribute to the extracellular killing of microorganisms, and regulate non-infectious inflammatory processes by activating specific receptors and modulating the levels of cytokines.
- View At a Glance
Author affiliations
-
Division of Rheumatology, Department of Internal Medicine, Washington University School of Medicine, Saint Louis, Missouri 63110, USA.
Email: CPHAM@im.wustl.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Angiogenin: an antimicrobial ribonucleaseNature Immunology News and Views (01 Mar 2003)
RESEARCH
Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsisNature Medicine Article (01 May 1998)
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteasesThe EMBO Journal Article (03 Dec 2001)
Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysisThe EMBO Journal Article (06 Feb 2008)
See all 29 matches for Research
