ELANE, CTSG or PRTN3 binds bacteria

Stable Identifier
Reaction [binding]
Homo sapiens
Elastase, Proteinase 3, or Cathepsin G binds bacteria
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Polymorphonuclear neutrophils (PMNs) are the most abundant circulating blood leukocytes that are rapidly recruited to sites of infection by host- and/or pathogen-derived components. PMNs provide the first-line defense against infection killing invading pathogens and resolving the inflammation they cause (Kobayashi SD et al. 2005). Activated neutrophils are known to release a variety of molecules, including the neutrophil serine proteases such as neutrophil elastase (ELINE), proteinase 3 (PRTN3) and cathepsin G (CTSG) (Garwicz D et al. 2005). Neutrophil serine proteases contribute to antimicrobial defense by

  • attacking membrane-associated (E. coli) or capsule proteins (S.pneumonia), which leads to loss of membrane integrity (Belaaouaj A et al. 2000; Standish AJ & Weiser JN 2009)
  • processing host immune proteins to generate antimicrobial peptides that can directly kill bacteria (Sorensen OE et al. 2001)
  • targeting and inactivating bacterial virulence factors to attenuate bacteria (Weinrauch Y et al. 2002; Lopez-Boado YS et al. 2004)

Literature References
PubMed ID Title Journal Year
16799473 Neutrophil serine proteases: specific regulators of inflammation

Pham, CT

Nat. Rev. Immunol. 2006
25461571 Neutrophil serine proteases in antibacterial defense

Stapels, DA, Geisbrecht, BV, Rooijakkers, SH

Curr. Opin. Microbiol. 2015
18021746 Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions

Moreau, T, Korkmaz, B, Gauthier, F

Biochimie 2008
Orthologous Events
Cite Us!