Binding of lysozyme to lipopolysaccharide suppresses tumor necrosis factor production in vivo.
Endotoxin (lipopolysaccharide [LPS]) released during gram-negative bacterial infection induces varieties of cytokines which directly and/or indirectly cause shock, disseminated intravascular coagulation, and death. We previously showed that lysozyme (LZM) was an LPS-binding protein and inhibited various immunomodulating activities of LPS. In this study, we examined the effect of LZM on the LPS-triggered septic shock model induced by carrageenan treatment and assessed by tumor necrosis factor production. The data presented in this report strongly suggest that LZM-LPS complex formation completely abrogates tumor necrosis factor production and the mortality caused by LPS and that LZM may be useful for the treatment of endotoxin shock.
Takada
K
K
Laboratory of Immunopharmacology of Microbial Products, Tokyo College of Pharmacy, Japan.
Ohno
N
N
Yadomae
T
T
D000818:Animals; D004926:Escherichia coli / Q000472:pathogenicity; D008070:Lipopolysaccharides / Q000378:metabolism / Q000494:pharmacology*; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D009113:Muramidase / Q000378:metabolism / Q000494:pharmacology*; D012772:Shock, Septic / Q000401:mortality; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis*
D008070:Lipopolysaccharides; D014409:Tumor Necrosis Factor-alpha; D009113:Muramidase