Effects of murine lysozyme on lipopolysaccharide-induced biological activities.
We have demonstrated that egg-white lysozyme (EW-LZM) bound to lipopolysaccharide (LPS), reduced the lethal toxicity and the biological activity of LPS. In this study, the interaction of LPS with murine lysozyme (M-LZM) and the modulation of biological activities were investigated. M-LZM was prepared from the culture supernatant of the murine macrophage cell line RAW264.7 by ion-exchange and gel filtration chromatographies and dialysis. Two types of M-LZM, murine M lysozyme (MM-LZM) and murine P lysozyme (MP-LZM), were purified from the supernatant. The enzymatic activities of both MM-LZM and MP-LZM were inhibited by LPS and their effects were affected by the temperature and the ionic strength. TNF-alpha production from RAW264.7 by LPS was inhibited by mixing with MM-LZM and MP-LZM. MP-LZM inhibited TNF-alpha production stronger than MM-LZM. Considering these facts, we suggested that M-LZM, like EW-LZM, make a complex with LPS to reduce the toxicity of LPS together with inhibiting the enzymatic activity.
Kurasawa
T
T
Laboratory for Immunopharmacology of Microbial Products, Tokyo University of Pharmacy and Life Science, Japan.
Takada
K
K
Ohno
N
N
Yadomae
T
T
D000595:Amino Acid Sequence; D000818:Animals; D004347:Drug Interactions; D007527:Isoenzymes / Q000494:pharmacology*; D008033:Limulus Test; D008070:Lipopolysaccharides / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D009113:Muramidase / Q000494:pharmacology*; D017421:Sequence Analysis; D013045:Species Specificity
D007527:Isoenzymes; D008070:Lipopolysaccharides; D009113:Muramidase