Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated the in vivo and in vitro cytokine inducing effects of Deodan, an oral preparation from Lactobacillus bulgaricus "LB-51", using the rabbit pyrogen test. In the first experimental approach we administered Deodan, or its chromatographically purified fraction, via the i.m. or i.v. routes. Low doses of Deodan i.m. caused the formation of a single temperature peak, whereas large doses produced a biphasic temperature curve. Intravenous injection of Deodan produced a monophasic fever in all tested doses. Chromatographically purified Deodan injected i.v. to rabbits caused a febrile response with a dose-dependent pattern, strikingly similar to that of lipopolysaccharide. LAL-testing of Deodan, however, showed that the preparation does not contain endotoxin. In in vivo neutralization studies we demonstrated that IL-1, TNF alpha, and IL-6 mediate the rabbit febrile response to Deodan. Interestingly, the effects of Deodan on the production of TNF alpha and IL-6 were more pronounced than its IL-1 inducing activity. In the second approach, we injected supernatants from mononuclear cells incubated with nonpyrogenic doses of Deodan, intravenously to rabbits ("monocyte type" of pyrogen test). Rapid-onset monophasic fevers were observed, typical for the rabbit pyrogen reaction to i.v. administration of exogenous IL-1 and TNF. Finally, we demonstrated the presence of pyrogenic cytokines in the supernatants from macrophages of Deodan-treated mice. Together, these results indicate that Deodan induces the production of cytokines with endogenous pyrogenic activity.
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PMID:Determination of cytokine release after in vivo and in vitro administration of Deodan (a preparation from Lactobacillus bulgaricus "LB51") by the rabbit pyrogen test. 146 75

Sodium nucleinate (NN) as well as bacterial lipopolysaccharide (LPS) can be detected by epinephrine-skin, dactinomycin and LAL tests. In the quantitative determination of two pyrogen standards for rabbit tests, consisting of NN, a smaller value was found by LAL test for the standard of greatest pyrogenic effect than for that less pyrogenically effective in rabbits. A standard consisting of NN can be used for the pyrogen test in rabbits. But in the future, if necessary a standard consisting of endotoxin will be used, due to its better comparability of results obtained by LAL and rabbit tests.
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PMID:[The effects and properties of sodium nucleinate as a pyrogen working-standard. 9. Pyrogen detection with epinephrine-skin-, dactinomycin- and LAL-tests. The suitability of sodium nucleinate as a pyrogen standard]. 180 86

In this study we compared the interleukin 1 (IL 1)-inducing capacity and the reactivity in the Limulus amoebocyte assay (LAL) of purified lipopolysaccharides (LPSs) from various bacterial strains. LPSs differed greatly in their capacities (on a weight basis) to induce IL 1 release from serum-free cultured human monocytes. LPS species that induced high levels of IL 1 release from human monocytes exhibited a high thiobarbiturate-reactive 2-keto-3-deoxy-octonic acid (KDO) content. No relationship was found between the IL 1-inducing activity and the LAL reactivity of purified LPSs. Filtration experiments in which membranes of decreasing size-exclusion limits were used demonstrated that molecular species of LPS with an apparent Mr below 3,000 may induce IL 1, whereas only species with an apparent Mr above 8,000 are recognized in the LAL assay. The latter observation suggests that the reaction with LAL requires an aggregated form of LPS. These results indicate that biologically active LPS species can cross dialysis membranes in vivo although no LAL reactive material is detected in the blood compartment. The Limulus assay is an insufficient criterion for the absence of LPS in biological fluids.
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PMID:Dissociation between the interleukin 1-inducing capacity and Limulus reactivity of lipopolysaccharides from gram-negative bacteria. 212 2

Carcinoscorpius amoebocyte lysate (CAL) was prepared from C. rotunda cauda by a modification of the method described by Mahalanabis et al. [Indian J Med Res, 70 (1979) 35]. Seasonal variation as well as batch variation was observed in the yield of haemolymph and the total lysate protein. In the presence of E. coli lipopolysaccharide (pure, free endotoxin) and E. coli and Salmonella cell suspensions (bound endotoxin), the CAL formed a gel after incubation at 37 degrees C. The gelling time varied from 10-90 min depending on the concentration of endotoxin used; higher concentrations formed gel more rapidly. The endotoxin detection capacity (sensitivity) of the lysate preparations was influenced by the season in which prepared, but not by the total protein content. Ten fold increase in the sensitivity was achieved by a purification step using chloroform. Although subsequent frozen storage with or without lyophilization did not alter the initial sensitivity, it was either decreased considerably or lost totally when the lysate was stored for 4 months at 4 degrees C or for 2 months at 30 degrees C. Under the same conditions, Limulus lysate was more stable. The lost sensitivity could not be regained by the incorporation of divalent cations (Ca2+ and Mg2+). The CAL preparations in general were able to detect as little as 10-100 pg of endotoxin or as few as 10(3) cells of E. coli or 10(4) cells of Salmonella and were comparable to LAL. CAL could be used successfully in lieu of Limulus amoebocyte lysate in the detection and assay of endotoxins.
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PMID:Carcinoscorpius rotunda cauda amoebocyte lysate for detection of endotoxins--its preparation, stability, sensitivity and comparison with Limulus amoebocyte lysate. 260 19

An inhibition enzyme-linked immunosorbent assay (ELISA) was developed for the specific quantitation of rough (R) mutant E. coli K12 lipopolysaccharide (LPS). Since R-LPS binds poorly to polystyrene microplates, an LPS-BSA covalent complex was prepared following glutaraldehyde activation and used as a coating surface antigen. A 100-fold higher signal was observed using the LPS-BSA complex as solid-phase antigen instead of free LPS. The LPS detection limit obtained was 0.5 ng/ml. This test was applied to hGH extracts produced genetically engineered E. coli K12 and a good correlation was found with the LAL test. This new LPS titration technique will be useful for detecting LPS in complex mixtures and the antigen-antibody reaction will ensure the specificity of the detection.
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PMID:An inhibition enzyme-linked immunosorbent assay technique for the detection of endotoxins in proteins extracted from Escherichia coli K12 recombinant DNA. 266 93

Proteose-peptone-induced macrophages (pM phi) from C57BL/6 (B6) mice were treated in vitro with lymphokine, and 2 functions were evaluated: the ability to suppress lymphokine production and the cytotoxic capacity against tumor target cells. When 10% to 20% pM phi treated with lymphokine were added to a lymphokine-producing system, strong inhibition of MIF and MAF production occurred. The suppression was not specific, since pM phi inhibited the production of lymphokine obtained by either mitogenic stimulation of normal spleen cells (NSC) or alloantigen stimulation of immune spleen cells (ISC). The suppressor cells were adherent, phagocytic, Thy 1.2 negative, with monocyte-macrophage-like morphology. Lymphokine-treated pM phi were also tumoricidal when tested in 18 hr microcytotoxicity assay against RL male 1 lymphoma target cells. However, using endotoxin-free reagents (less than or equal to 0.01 ng/ml of endotoxin by the LAL assay), we found that small amounts of lipopolysaccharide (LPS) were required, in addition to lymphokine, to induce tumoricidal activity in pM phi. In contrast, noncytotoxic pM phi stimulated with lymphokine alone were also able to inhibit lymphokine production, although not as effectively as pM phi stimulated by lymphokine plus LPS. Therefore, we concluded that lymphokine treatment itself is sufficient to induce M phi to become suppressor cells, whereas an additional signal is necessary to induce cytolytic activity. We suggest that there is a negative feedback mechanism of control on the lymphokine-producing cells through the activation of suppressor M phi by lymphokine.
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PMID:In vitro induction of tumoricidal and suppressor macrophages by lymphokines: possible feedback regulation. 645 55

The ability of poly I:C to activate mouse macrophages (M phi) to become tumoricidal was evaluated and compared with the ability of 2 other agents, lipopolysaccharide (LPS) and M phi-activating factor (MAF), to induce a tumoricidal state. All these agents were able to stimulate proteose-peptone-elicited M phi to kill RL male 1 tumor cells in an 18-hr 51Cr release cytotoxicity assay. High levels of cytotoxicity were obtained with concentrations as low as 1 microgram/ml of LPS or poly I:C and with 1/81 dilution of MAF. However, in the presence of reagents shown to contain less than 0.01 ng/ml of LPS by the LAL assay (LPS free), we found that poly I:C induced strong reactivity, whereas MAF was ineffective. The addition of 10 ng/ml of LPS during the stimulation period did not enhance the cytotoxicity induced by poly I:C, but it did restore MAF-induced, M phi-mediated cytotoxicity. In addition, poly I:C induced strong tumoricidal activity in resident M phi and in peritoneal exudate cells from the genetically defective C3H/HeJ mice that normally do not respond to LPS and MAF treatment. Therefore, it seems that although LPS is required as a second signal for MAF-induced cytotoxicity, such a second signal is not required for poly I:C-induced cytotoxicity. From the above results, it appears that poly I:C is a more powerful activating agent than LPS and MAF and either activates M phi via a different pathway or is effective on subpopulations of M phi that are not activated by the other agents.
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PMID:Activation of murine macrophages. I. Different pattern of activation by poly I:C than by lymphokine or LPS. 678 32

Interferon-gamma (IFN-gamma) is known to prime macrophages for tumor cell lysis and nitric oxide (NO) production as measured by enhanced sensitivity to lipopolysaccharide (LPS). In the present study, the ability of IFN-gamma to directly activate peritoneal macrophages from C57BL/6 and Balb/c mice for tumor cytotoxicity and NO production was evaluated. Macrophage-mediated tumor cell killing was measured by an 18 h 51Cr release assay using P815 mastocytoma cells as targets. Concurrent NO production was measured as nitrite in the supernatants of macrophage cultures. Incubation of macrophages with IFN-gamma resulted in activation of macrophages for tumor cell lysis. IFN-gamma alone also activated macrophages for NO production under identical conditions. Addition of LPS along with IFN-gamma resulted in synergism in the activation of macrophages for both cytolysis and NO production. LPS contamination of the IFN-gamma preparation was absent as evidenced by the following criteria: (1) the IFN-gamma preparation as well as the reagents used were shown to be free of LPS contamination based on LAL endotoxin tests (sensitivity 25 pg/ml), (2) the ability of IFN-gamma to activated macrophages was not abrogated by prior treatment of the cytokine with polymyxin B, whereas the effect of LPS was inhibited (70-100%) under similar conditions, (3) pretreatment of the IFN-gamma preparation with a specific endotoxin neutralizing protein did not abrogate the ability of IFN-gamma to induce macrophage activation, and (4) heat treatment of solutions containing IFN-gamma alone or IFN-gamma+LPS abolished only the effect of IFN-gamma, not that of LPS.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Direct activation of murine peritoneal macrophages for nitric oxide production and tumor cell killing by interferon-gamma. 764 40

Human neutrophil azurophilic granules contain an approximately 55-kDa protein, known as bactericidal/permeability-increasing protein (BPI), which possesses a high-affinity binding domain for the lipid A component of lipopolysaccharide (LPS). The in vivo LPS neutralizing activity of exogenous BPI was studied in a model of lethal Escherichia coli bacteremia. Five baboons were treated with BPI (5 mg/kg bolus injection followed by a 95 micrograms/kg/min BPI infusion over 4 hr), while four additional animals received a genetically engineered variant of BPI (NCY103). Five animals received a placebo treatment and served as controls. Both wild-type rhBPI and NCY103 significantly (P < 0.05) decreased blood levels of LPS throughout an 8-hr evaluation period following live bacterial challenge. Two hours following E. coli administration, LPS levels peaked in the controls, at 6.86 +/- 3.22 ng/ml, whereas LPS levels were 3.39 +/- 2.1 ng/ml in the BPI group and 2.04 +/- 1.18 ng/ml in the NCY103 group. Tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 levels likewise were attenuated in the treatment groups, whereas circulating sTNFR I was significantly (P < 0.05) reduced only in the BPI group. Leukocytopenia and granulocytopenia were significantly (P < 0.02) lessened in the BPI group, by an average of 59% leukocytopenia and 65% granulocytopenia, respectively. This study supports the concept of E. coli LPS neutralization by BPI in vivo and demonstrates that a moderate (70%) reduction in peak LPS-LAL activity is sufficient to alter some hematologic and cytokine manifestations of bacteremia.
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PMID:The role of bactericidal/permeability-increasing protein in the treatment of primate bacteremia and septic shock. 819 14

Bordetella pertussis is composed of a series of active components: (1) a heat-labile or dermonecrotic toxin (HLT); (2) a lipopolysaccharide endotoxin (LPS); (3) pertussis toxin; (4) filamentous hemagglutinin (FHA); (5) agglutinogens; (6) outer membrane proteins; (7) adenylate cyclase; and (8) tracheal cytotoxin. Pertussis toxin (PT), also called lymphocytosis-promoting factor (LPF), encompasses a series of biological activities including: (1) histamine-sensitization (HSF); (2) leukocytosis-promoting activity (LPF); (3) LPF-hemagglutinin (LPF-HA); and (4) pancreatic islet-activating protein (IAP). The heat-labile toxin is inactivated during vaccine production. Pertussis toxin is inactivated when heated to 80 degrees C for 30 min and endotoxin at a temperature greater than 120 degrees C for 30 min. The effect of pre- and post-heat treatment on DTP vaccine, Bordetella pertussis endotoxin, pertussis toxin and a pertussis toxin/endotoxin combination, was determined as related to: (1) paw swelling response; (2) LAL activity (endotoxin); and (3) HSF activity. With the exception of DTP and B. pertussis endotoxin, the average paw swelling response after injection of non-treated and heat-treated test samples was similar to the saline control at all measured time intervals. Contrary to anticipated results, heat treatment enhanced the paw-swelling response of DTP vaccine and B. pertussis endotoxin. Endotoxin levels, as measured by LAL, were significantly lower after heat-treatment, with the exception of B. pertussis endotoxin and the E-1 control. The addition of pertussis toxin, B. pertussis endotoxin or pertussis toxin/endotoxin did not restore LAL values to the levels seen for non-treated DTP vaccine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Assay of pertussis vaccine reactivity factors by measurement of the paw swelling response, endotoxin and histamine-sensitizing factor. 821 17


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