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  • 1
    Electronic Resource
    Electronic Resource
    Detoxification of lipopolysaccharide (LPS) by egg white lysozyme (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 9 (1994), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Recent studies carried out by our group suggest that lysozyme binds to bacterial lipopolysaccharide with a high affinity to produce a complex, and inhibits various biological activities of lipopolysaccharide. Although the basic structure of lipopolysaccharide is independent of the species and strains of Gram-negative bacteria, many structural factors such as O-antigenic polysaccharide, lipid A, substituted groups, and associated molecules, affect the biological activities of lipopolysaccharide. In this study, we prepared lysozyme/lipopolysaccharide complexes using various structures of lipopolysaccharide and compared the activity and physiochemical properties. Native and dansylated lysozyme were found to bind to all tested lipopolysaccharides. The mitogenic activity and TNF production by all tested lipopolysaccharides were significantly reduced by complex formation in vitro. Administration of the complex prepared by various lipopolysaccharides produced significantly less quantities of TNF in the septic shock model. These results suggested that binding of lysozyme to lipopolysaccharide is important for the host both in pathophysiological responses to lipopolysaccharides and in the modification of lipopolysaccharide biological activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1994.tb00360.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of murine lysozyme on lipopolysaccharide-induced biological activities (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 13 (1996), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract 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-α production from RAW264.7 by LPS was inhibited by mixing with MM-LZM and MP-LZM. MP-LZM inhibited TNF-α 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1996.tb00254.x
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  • 3
    Electronic Resource
    Electronic Resource
    Association of immunological disorders in lethal side effect of NSAIDs on β-glucan-administered mice (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 31 (2001), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: (1→3)-β-d-Glucan (β-glucan) is a biological response modifier that regulates host immune response. We have found that the combination of a β-glucan and a non-steroidal anti-inflammatory drug (NSAID), indomethacin (IND), induced lethal toxicity in mice [Yoshioka et al. (1998) FEMS Immunol. Med. Microbiol., 21, 171–179]. This study was undertaken to analyze the mechanism of the lethal side effect. Combination of a β-glucan and IND increased the number of leukocytes, especially macrophages and neutrophils, in various organs and these cells were activated. The activated state of these cells was supported by the enhanced production of interferon-γ in the presence of IND in vitro culture of the peritoneal exudate cells. Intestinal bacterial flora was translocated into the peritoneal cavity in these mice to cause peritonitis. Comparing the toxicity of various NSAIDs, nabumetone, a partially cyclooxygenase-2-selective NSAID with weaker toxicity to the gastrointestinal tract, did not exhibit a lethal side effect. These facts strongly suggested that gastrointestinal damage by NSAIDs was more severe in β-glucan-administered mice, resulting in peritonitis by enteric bacteria and leading to death.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2001.tb01579.x
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of O-antigenic polysaccharide of Escherichia coli on endotoxin neutralizing activity of lysozyme (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 21 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Endotoxemia is considered to be associated with the high mortality of Gram-negative septic patients. Increasing evidence shows that β-lactam antibiotics have a propensity to induce endotoxin release from the bacterial outer membrane while killing bacteria. We have recently found that egg white lysozyme (EW-LZM) shows strong inhibition of β-lactam induced bacteriolysis and lipopolysaccharide (LPS) release from Escherichia coli O111, resulting in reduction of the LPS-initiated inflammatory response. In this study, we compared the effect of EW-LZM on E. coli J5, which possesses rough-type LPS (RaLPS), in order to demonstrate the effect of O-antigenic polysaccharide on endotoxin neutralizing activity of EW-LZM and on inhibition of β-lactam induced lysis by LZM. Both of the β-lactam induced bacterial lysis and subsequent LPS release were almost completely inhibited by EW-LZM. The effect was more potent than that of wild-type LPS as assessed by released LPS concentration and LPS induced cytokine syntheses. In addition, EW-LZM was effective against lethal infection of E. coli J5 in cyclophosphamide induced leukopenic mice. These facts strongly suggested that O-antigenic polysaccharide negatively modulates LPS neutralizing activity of EW-LZM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01152.x
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  • 5
    Electronic Resource
    Electronic Resource
    Immunotoxicity of soluble β-glucans induced by indomethacin treatment (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 21 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: (1→3)-β-d-Glucan (β-glucan) is a biological response modifier that regulates host immune response. However, the side effects of this drug have not been extensively examined. In this study, we found that the combination of a β-glucan and a nonsteroidal anti-inflammatory drug, indomethacin, induced lethal toxicity in mice. Lethal toxicity of orally administered indomethacin (multiple administration to ICR mice; once a day for 2 weeks) was 0/8 (2.5 mg kg−1) and 5/8 (5 mg kg−1) (death/total) over 2 weeks. The toxicity was enhanced to 3/8 and 8/8 in mice treated with a clinical β-glucan preparation, sonifilan (250 μg/mouse, single i.p. administration on day 0). A similar effect was observed for other β-glucans, including SSG, grifolan, zymosan A and zymocel. Enhanced lethal toxicity resulted from a single p.o. administration of indomethacin on day 5 to day 9 after multiple β-glucans administration. Interferon-γ, interleukin-6 and colony stimulating factor concentrations in sera of indomethacin/β-glucan-treated mice were significantly elevated. These results strongly suggest that indomethacin/β-glucan treatment induces lethality in mice by maladjusting the cytokine network.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01163.x
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  • 6
    Electronic Resource
    Electronic Resource
    Chemical and immunochemical characterization of limulus factor G-activating substance of Candida spp. (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 24 (1999), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The limulus test is a well-established method for the diagnosis of both Gram (−) sepsis and invasive fungal infection. To diagnose deep-seated fungal infections, a (1→3)-β-d-glucan-specific chromogenic kit (Fungitec G test MK) has been developed and applied clinically. It is suggested that the limulus reactive substance was released from the fungi to the blood, however, its chemical properties were not precisely examined in detail because of the limited quantity available. In this study, we used chemically defined liquid medium to culture Candida spp. and collected the water soluble fraction, CAWS. The yield of CAWS was circa 100 mg/l, independent of the strain of Candida. CAWS reacted with limulus factor G (Fungitec G test MK) at concentrations as low as 100 ng/ml. Limulus factor G reactivity of CAWS was sensitive to (1→3)-β-glucanase, zymolyase and was, at least in part, bound to ConA-agarose. The ConA-bound fraction also reacted with anti-β-glucan antibody. CAWS is mainly composed of mannan and (1→6)-β-glucan, in addition to protein, assessed by 1H-NMR spectroscopy. CAWS also reacted with typing sera of Candida spp., specific for cell wall mannan. Chemical, immunochemical and biochemical analyses of CAWS strongly suggested that the limulus factor G-activating substance was a mannan-β-glucan complex, present within the architecture of the yeast cell wall.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1999.tb01313.x
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  • 7
    Electronic Resource
    Electronic Resource
    The solubilization and biological activities of Aspergillusβ-(1→3)-d-glucan (2004)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 42 (2004), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have recently demonstrated that the cell wall β-glucan of Candida albicans could be solubilized by sodium hypochlorite, followed by dimethylsulfoxide-extraction (NaClO-DMSO method). In this study, applying this method to Aspergillus spp., we prepared mycelial cell wall β-glucan and examined its physical properties and immunotoxicological activity. The acetone-dried mycelia of Aspergillus spp. were oxidized by the NaClO-DMSO method. An analysis of 13C NMR spectra revealed the preparations to be composed of α-(1→3) and β-(1→3)-d-glucan. Also, the proportion of α-(1→3) and β-(1→3)-d-glucan varied. Futhermore, a solubilized Aspergillusβ-glucan (ASBG) was prepared from OX-Asp by urea-autocalve treatment. ASBG showed limulus activity similar to Candida solubilized β-glucan (CSBG), and there was little difference in the activity of ASBG between various Aspergillus spp. ASBG affected the production of IL-8 by human peripheral blood mononuclear cells (PBMC). ASBG should be useful for analyzing the clinical role of β-glucan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsim.2004.04.004
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  • 8
    Electronic Resource
    Electronic Resource
    Protective effect of β-glucan against systemic Streptococcus pneumoniae infection in mice (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 27 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The antimicrobial effect of soluble β-1,3-d-glucan from Sclerotinia sclerotiorum (SSG) was examined in mice experimentally infected intraperitoneally (i.p.) with Streptococcus pneumoniae serotypes 4 and 6B. SSG was administered i.p. either 3 days before challenge or 3–48 h after challenge. The number of bacteria in blood samples and the mouse survival rates were recorded. Pre-challenge SSG administration protected dose-dependently against both S. pneumoniae type 4 and 6B infections. SSG injected 24 h post-challenge had a curative effect against type 6B but not type 4 pneumococcal infection. The data demonstrate that SSG administered systemically protects against pneumococcal infection in mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01420.x
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  • 9
    Electronic Resource
    Electronic Resource
    Soluble mannan and β-glucan inhibit the uptake of Malassezia furfur by human monocytic cell line, THP-1 (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 21 (1998), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The uptake of live and heat-killed Malassezia furfur HIC 3321, HIC 3343 and Candida albicans ATCC 10231 by human monocytic cell line, THP-1, was examined. THP-1 was differentiated by PMA for 7 days before use. The uptake of these yeasts by THP-1 was increased in a concentration-dependent manner of yeasts, and the uptake reached plateau level at the E/T (yeast/THP-1) ratio 5. In addition, a higher percentage of heat-killed cells than live cells was taken in THP-1. Yeast mannan and β-1,3-glucan, random coiled conformer, inhibited the uptake of live and heat-killed M. furfur by THP-1, though dextran T-250, that is α-glucan, and schizophyllan (SPG), triple helix conformer of β-glucan, did not. Interestingly, mannan inhibited the uptake of both types, live and heat-killed, of C. albicans, however, laminaran inhibited the uptake of heat-killed C. albicans alone. Opsonization of these yeasts with normal human serum enhanced the uptake of yeasts, although opsonization with heat-inactivated serum, the treatment at 56°C for 30 min, did not enhance. These results suggested that live and heat-killed M. furfur was recognized by THP-1 through mannose receptor, β-glucan receptor and complement receptor type 3 via the activation of alternative pathway of complement.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1998.tb01169.x
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  • 10
    Electronic Resource
    Electronic Resource
    Enhancement of IL-8 production from human monocytic and granulocytic cell lines, THP-1 and HL-60, stimulated with Malassezia furfur (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 28 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Previously, we reported that Malassezia furfur, causing systemic fungal infection, was taken up into human monocytic cell line, THP-1, in a concentration-dependent manner. This fact suggested that M. furfur could activate phagocytes, such as monocyte and polymorphonuclear leukocyte. Thus we examined cytokine mRNA expression from human monocytic and granulocytic cell line, THP-1 and HL-60, stimulated with M. furfur by using reverse transcriptase-polymerase chain reaction (RT-PCR) and ELISA. We chose IL-1α, IL-6, IL-8, IL-12 and TNF-α as primers for THP-1, and IL-1α, IL-6 and IL-8 for HL-60. M. furfur induced the expression of IL-8 mRNA from THP-1 and HL-60 following incubation for 3 h, and also induced IL-1α mRNA from HL-60, although this induction was weaker than that of IL-8 mRNA. Furthermore, opsonized M. furfur induced stronger expression of IL-8 mRNA in comparison with intact M. furfur. IL-8 production from THP-1 and HL-60 was enhanced in a concentration- and incubation time-dependent manner. These facts strongly suggested that M. furfur could activate phagocytes, and could induce inflammatory responses in systemic infection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01471.x
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