There will be a maintenance on OICR IT systems starting Friday Dec 15 at 6PM EST until midnight Sunday Dec 17; Reactome will be affected by this downtime

Service under maintenance from Friday Dec 15 at 6PM EST until midnight Sunday Dec 17

BPI binds LPS on the bacterial surface

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

Bactericidal permeability-increasing protein (BPI) is a 57-kDa cationic antimicrobial protein that is present principally in the azurophilic granules of polymorphonuclear leukocytes (Elsbach P 1998). BPI has both heparin- and LPS-binding capacity and displays anti-inflammatory activity and direct bactericidal action toward Gram-negative bacteria (Ooi CE et al. 1991; Weiss J et al. 1992; Levy O et al. 2000). Direct bactericidal activity and lipopolysaccharide neutralization are mediated by the N-terminal part of the protein, whereas the C-terminal region has been shown to opsonize bacteria (Iovine NM et al. 1997; Elsbach P & Weiss J 1998).

Antineutrophil cytoplasmic autoantibodies against BPI (BPI-ANCA) have been found in diseases of different etiologies, such as cystic fibrosis, TAP deficiency or inflammatory bowel diseases (Walmsley RS et al. 1997; Schultz H et al. 2004; Schinke S et al. 2004; Aichele D et al. 2006). The presence of BPI-ANCA has been shown to correlate with the chronic or profuse exposure of the host to Gram-negative bacteria and their endotoxin (Aebi C et al. 2000; Carlsson M et al. 2003; Schultz H et al. 2003; Schultz H 2007).

Entity On Other Cell
Participant Of
Orthologous Events