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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have recently reported that chronic and systemic administration of tumor necrosis factor alpha (TNF) inhibits development of autoimmune diabetes in NOD mice and BB rats, animal models of insulin-dependent diabetes mellitus (IDDM). During these experiments, we unexpectedly found that in vivo production of TNF stimulated by a single injection of lipopolysaccharide was enhanced approximately 10 times in the long-term diabetic BB rats (P less than 0.0001), whose mean duration of diabetes with more than 16.8 mM (300 mg/dl) of nonfasting blood glucose level was 26.2 +/- 2.1 days, as compared to that in the rats of nondiabetes and in the rats at the onset of diabetes, whose mean duration of diabetes was 1.4 +/- 0.6 days. The long-term diabetic, but not short-term-diabetic, rats were also associated with increased levels of serum fructosamine/albumin (P less than 0.01) and triglyceride (P less than 0.01) and with a decreased level of serum albumin (P less than 0.01). The in vivo TNF productivity in the diabetic rats, including the short-term- and long-term-diabetic rats, was correlated positively with the level of fructosamine/albumin (P less than 0.05) and negatively with the level of serum albumin (P less than 0.05), but not with levels of blood glucose. None of these correlations were observed in nondiabetic rats. The increased LPS-induced serum TNF activity in the long-term diabetic state was observed not only in BB rats but also in NOD mice and GK rats, a model of non-IDDM, irrespective of sexes and ages, indicating that the enhancement of in vivo TNF production was a result of long-term diabetes. These findings indicate that some factor(s) associated with the long-term-diabetic state may prime macrophages in vivo to produce TNF. Further study is needed to reveal a mechanism of the enhanced TNF production and its possible relevance to various abnormalities associated with the chronic hyperglycemic state.
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PMID:Increased in vivo production of tumor necrosis factor after development of diabetes in nontreated, long-term diabetic BB rats. 154 Oct 51

Our previous studies have shown that a major protein isolated from purified cell walls of Proteus mirabilis (39-kDa protein) is a strong modulator of the specific immune responses to lipopolysaccharide (LPS) from this bacterium. When the protein is mixed with LPS before immunization of mice, the responses of antibody-producing cells specific for LPS are greatly enhanced and converted predominantly to the immunoglobulin G isotype. In the present study, the immunomodulating effects of the 39-kDa protein were tested at the level of interaction of LPS with macrophages. Activation of macrophages was determined by measuring the production of oxygen radicals in a chemiluminescence assay with lucigenin as the amplifier. LPS from P. mirabilis induced strong oxidative metabolism in both peritoneal and bone marrow-derived murine macrophages. These responses were inhibited in a dose-dependent manner by mixing LPS with increasing amounts of the protein. In contrast, bovine serum albumin and methylated bovine serum albumin enhanced the response of macrophages dramatically when complexed with LPS. The inhibiting activity of the 39-kDa protein was also observed with LPS from Escherichia coli K-12.
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PMID:Modulation of effects of lipopolysaccharide on macrophages by a major outer membrane protein of Proteus mirabilis as measured in a chemiluminescence assay. 154 21

Inflammatory reactions were compared in the air pouch and the CMC pouch. Inflammation was induced by injection of CMC as a non-specific irritant, lipopolysaccharide (LPS) as an activator of macrophages, and methylated bovine serum albumin (m-BSA) as an inducer of delayed type hypersensitivity. There was no prominent difference in the inflammatory reactions following injection of 2% CMC solution into a 4-day-old air pouch and a 3-day-old CMC pouch. On the other hand, injection of 4 ml of 100 ng/ml LPS into each of the pouches enhanced the inflammatory reactions in the CMC pouch several-fold compared with those in the air pouch. A similar tendency was found in the case of an injection of 1 ml of 1 mg/ml m-BSA in rats sensitized with 1 mg of m-BSA. The enhanced inflammatory reactions induced by the injection of LPS or m-BSA were inhibited by dexamethasone, but not by indomethacin. These results indicate that the enhanced inflammatory reactions induced by CMC are related to lining tissue formation, which was a common characteristic in both pouches. Enhanced inflammatory reactions following injection of LPS and m-BSA were related to the activation of macrophages and newly formed blood vessels, which were not characteristic features in the air pouch, but were in the CMC pouch, in addition to the lining tissue. Cyclo-oxygenase products were not associated with the reactions.
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PMID:Comparative studies on inflammatory reactions induced by non-immunological and immunological stimuli in an air pouch and in a carboxymethyl cellulose (CMC)-induced inflammatory pouch. 157 Dec 82

In order to examine the ability of Limulus antilipopolysaccharide factor (LALF) to bind lipopolysaccharide (LPS), we purified LALF to homogeneity from Limulus amoebocyte lysate and coupled it covalently to agarose beads. LALF-coupled beads captured more tritiated LPS from rough and smooth strains of gram-negative bacteria than did control human serum albumin-coupled beads. Unlabeled homologous and heterologous LPS competed for the binding of 3H-LPS to LALF-coupled beads. LALF bound LPS in a dose-dependent manner as assessed by the precipitation of LPS-LALF complexes with 50% saturated ammonium sulfate. We also studied the ability of LALF to neutralize LPS. LPS preincubated with LALF was less mitogenic for murine splenocytes, was less pyrogenic in the rabbit fever assay, was less lethal in mice which had been sensitized to LPS with actinomycin D, and induced less fever, neutropenia, and pulmonary hypertension when infused into sheep. Our findings extend prior studies which suggested that LALF binds to and neutralizes LPS from multiple strains of gram-negative bacteria.
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PMID:Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor. 158 18

The binding kinetics of radiolabeled Salmonella california 1989/O (mannose-sensitive hemagglutinin-positive [MSHA+]) to immobilized mucus or enterocytes isolated from broiler ceca and inhibition of binding by D-mannose and sodium metaperiodate were characteristic of adherence of mannose-sensitive type 1 fimbriae of bacteria to eukaryotic mannose-containing receptors. Binding by radiolabeled strains 1989/O (in the presence of D-mannose) and S. typhimurium S 7471 N (MSHA-, non-fimbriated) indicated non-specific binding that was characterized by less binding to enterocytes and mucus and lack of inhibition by carbohydrates or prior treatment with sodium metaperiodate. Inhibition of non-specific binding to enterocytes by pretreatment with various enzymes or by the presence of tetramethylurea or p-nitrophenol (known to disrupt hydrophobic interactions) indicate involvement of multiple sites and hydrophobic bonding. Strain-specific outer-membrane preparations inhibited non-specific binding to a greater extent than did lipopolysaccharide, Escherichia coli outer-membrane preparations, or bovine serum albumin.
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PMID:Binding of Salmonella strains to immobilized intestinal mucosal preparations from broiler chickens. 162 2

The passage of different-sized marker molecules over the lower respiratory tract into the blood circulation during pulmonary inflammation induced by dextran, endotoxin [i.e., lipopolysaccharide from Escherichia coli (LPS)], or ferritin was assessed in the rat. Bovine immunoglobulin G (BIgG, mol wt = 150,000 Da), bovine serum albumin (BSA, mol wt = 67,000 Da), and the nonapeptide 1-deaminocysteine-8-D-arginine vasopressin (dDAVP, mol wt = 1,067 Da) were used as permeability markers after intratracheal instillation. The pathophysiological indexes of a proceeding lung inflammation were increased total cell number, changed leukocyte proportions and increased total protein content obtained in bronchoalveolar lavage, and lung edema formation shown as an increased lung wet-dry weight difference. Intratracheal instillation of dextran induced a moderate neutrophil invasion into the lungs but had no effect on the passage of the different markers over the lungs (BIgG 1.8 +/- 0.6%, BSA 3.5 +/- 1.2%, dDAVP 26.1 +/- 20.7%) compared with control rats instilled with the markers alone (1.8 +/- 0.4%, 4.1 +/- 1.3%, 20.0 +/- 3.8%, respectively). Endotoxin administration resulted in markedly higher lavage cell counts and lung edema concomitantly with an increased lung passage of the markers (3.2 +/- 0.9%, 22.0 +/- 6.1%, 33.3 +/- 12.0%, respectively; P less than 0.01-P less than 0.001). The highest marker passage was obtained when the inflammation was most severe, i.e., after ferritin administration (17.6 +/- 2.3%, 60.0 +/- 6.7%, 41.6 +/- 6.9%, respectively; P less than 0.001), which resulted in markedly elevated lavage cell numbers and protein content as well as edema formation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lung to blood passage of different-sized molecules during lung inflammation in the rat. 172 3

Escherichia hermannii (ATCC 33651) LPS O-polysaccharide was covalently linked to a carrier (bovine serum albumin) to form conjugates either directly or with a spacer arm (adipic acid dihydrazide). The immunogenicity of both conjugates at three different doses was tested in mice. Antibodies to the conjugate were produced and were shown to react with free lipopolysaccharide. The directly-coupled conjugate was found to be more immunogenic than the indirect one (i.e. lower dose necessary for a similar response). The antibody response elicited by the directly coupled conjugate (1 microgram/animal) began at 21 days and was sustained for at least 4 months. The mouse model described here may be applicable to the testing of other conjugates composed of bacterial cell wall polysaccharides and LPS O-chains.
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PMID:Escherichia hermannii (ATCC 33651) polysaccharide-protein conjugates: comparison of two conjugation methods for the induction of humoral responses in mice. 177 69

With a 2.9-mM concentration of unlabelled bovine serum albumin (BSA), the FITC-albumin transport (2 mg included) across the omental monolayer (0.48 +/- 0.16 mg/ml/30 min) was found to be significantly reduced as compared with the interstitial BSA concentration (290 microM) as it is the case, e.g., in peritonitis (0.79 +/- 0.09 mg/ml/30 min). Adding 10 micrograms lipopolysaccharide (LPS)/ml from Escherichia coli, serotype 0128:B12, we did not see any differences from the control. Cultured mesothelial cells took up double the amount of FITC-albumin (4.2 +/- 0.13 micrograms/10(5) cells/30 min) and in the presence of LPS the uptake of FITC-albumin was reduced to half the control (2.15 +/- 0.47 micrograms/10(5) cells/30 min). The results reveal the active participation of the mesothelium because high concentrations of BSA reduced exocytosis and stimulated endocytosis. Applying 10 micrograms/ml of LPS turned out to influence endocytosis and to reduce it at a high BSA concentration.
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PMID:Endotoxin effects on transmesothelial transport and intracellular uptake of albumin. 180 34

This project investigated the effects of novel carriers and adjuvants on the isotype of murine immunoglobulin G (IgG) antibody to pneumococcal capsular polysaccharide type 14 (S14PS). S14PS conjugated to bovine serum albumin induced a weak antibody response which was 100% IgG1 following injection without adjuvant. The same polysaccharide conjugated to flagella of Salmonella typhi induced an antibody response which was 88% IgG3. S14PS-bovine serum albumin was injected with block copolymer L121 or Quil A in squalane-in-water emulsions. The copolymer L121 was at least as effective as Quil A or complete Freund adjuvant in inducing IgG antibodies. IgG1 was the dominant subclass for all. Addition of monophosphoryl lipid A, but not the threonyl derivative of muramyl dipeptide or nontoxic Rhodopseudomonas sphaeroides lipopolysaccharide, to copolymer L121 increased production of the IgG2a, IgG2b, and IgG3 subclasses. S14PS-flagella with copolymer L121 induced higher titers with a markedly altered isotype distribution: 13% IgG1, 52% IgG2a, 6% IgG2b, and 29% IgG3. Monophosphoryl lipid A added to L121 reduced IgG1 antibody to 5%, but increased IgG2a antibody to 14%, IgG2b antibody to 3%, and IgG3 antibody to 78%. These studies demonstrate that both the carrier and the adjuvant can influence the titer and isotype distribution of antipolysaccharide antibody responses.
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PMID:Immunogenicity of Streptococcus pneumoniae type 14 capsular polysaccharide: influence of carriers and adjuvants on isotype distribution. 185 91

Injury to the blood brain barrier (BBB) is a fundamental sequela of bacterial meningitis, yet the precise mechanism facilitating exudation of albumin across the endothelium of the cerebral microvasculature remains conjectural. After intracisternal inoculation of Escherichia coli (0111:B4) lipopolysaccharide in rats to elicit a reversible meningitis and BBB injury, we utilized in situ tracer perfusion and immunolabeling procedures to identify by transmission electron microscopy the precise topography and microvascular exit pathway(s) of bovine serum albumin (BSA). Results revealed that during meningitis there was: (a) an inducible increase in immunodetectable monomeric BSA binding to the luminal membrane of all microvascular segments in the pia-arachnoid and superficial brain cortex; (b) similar uptake of both colloidal Au-BSA (as well as monomeric BSA) by plasmalemmal vesicles but no detectable transcytosis to the abluminal side; and (c) predominant exit of both perfused Au-BSA and immunodetectable monomeric BSA through open intercellular junctions of venules in the pia-arachnoid. This was corroborated in separate experiments documenting focal pial venular leaks of in situ perfused 0.01% colloidal carbon black during experimental meningitis. These results provide precise localization of BBB injury in meningitis to meningeal venules, confirm a paracellular exit pathway of albumin via open intercellular junctions, and suggest an injury mechanism amenable to specific therapeutic intervention.
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PMID:Ultrastructural localization of albumin transport across the cerebral microvasculature during experimental meningitis in the rat. 187 66


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