Binding of lysozyme to lipopolysaccharide suppresses tumor necrosis factor production in vivo.

Abstract

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.

• Authors: K Takada, N Ohno, T Yadomae
• Journal: Infection and immunity (Infect Immun) Vol. 62 Issue 4 Pg. 1171-5 (Apr 1994) ISSN: 0019-9567 [Print] United States
• PMID: 8132323 (Publication Type: Journal Article)

Chemical References

• Lipopolysaccharides
• Tumor Necrosis Factor-alpha
• Muramidase

Topics

• Animals
• Escherichia coli (pathogenicity)
• Lipopolysaccharides (metabolism, pharmacology)
• Male
• Mice
• Mice, Inbred ICR
• Muramidase (metabolism, pharmacology)
• Shock, Septic (mortality)
• Tumor Necrosis Factor-alpha (biosynthesis)