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)

Monoclonal nonspecific suppressor factor (MNSF), a product of a murine T cell hybridoma, suppresses the antibody response to lipopolysaccharide. In an attempt to clarify the N-terminal sequence, MNSF was prepared and purified by affinity chromatography with the use of an anti-MNSF monoclonal antibody (MO6), and reverse-phase high-pressure liquid chromatography. On the SDS-PAGE, the purified MNSF showed a single band with a molecular weight of 12,000. The N-terminal amino acid sequence of the protein was determined and showed no strong homology to any of the sequences of known biologically active proteins. However, the sequence revealed significant (60%) amino acid identity to transforming growth factor beta 2 (TGF beta 2).
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PMID:Characterization of N-terminal amino acid sequence of monoclonal nonspecific suppressor factor. 172 62

B29 is a B-lineage-specific gene predicted from sequence information to be a transmembrane member of the immunoglobulin (Ig) superfamily, with a single extracellular Ig-like domain. Its presumptive cytoplasmic region contains a peptide motif present in CD3 and other molecules involved in lymphocyte activation. Affinity-purified goat antibodies were prepared to a TrpE fusion protein of B29 and used to study B29 expression on lymphoid cells. The antiserum precipitated surface-labeled heterodimers from B lymphoma cells. One was 65-88 kDa (unreduced) or 36-47 plus 32-34 kDa (reduced) by SDS/PAGE analysis, regardless of detergent. A smaller heterodimer was detected only with Triton detergent extraction. IgM molecules were coprecipitated by the B29 antiserum when the weak detergent digitonin was used. In addition, cocapping experiments revealed that most B29 molecules codistribute with Ig on the cell surface. Although early B-lineage cells and plasma cells contain B29 mRNA, surface expression was detectable only on B cells that had significant amounts of surface Ig. The surface expression was B-lineage-specific and included cells from mutant xid mice and B-cell lines representing mu, delta, gamma, and alpha heavy-chain isotypes and both kappa and lambda light-chain types. The density of surface B29 protein correlated directly with surface mu heavy-chain density on subclones of a B-cell lymphoma and lipopolysaccharide-stimulated pre-B cells. These findings show that B29 is covalently linked in a heterodimer and are consistent with a recently proposed model of surface Ig complexes.
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PMID:B29 gene products complex with immunoglobulins on B lymphocytes. 173 34

A comparative study on the endotoxic effects of lipopolysaccharide (LPS) from Veillonella parvula ATCC 10790 and from Bacteroides intermedius BMH was performed using an in vivo approach in the C57BL/6 mouse. Phenol-water extracted LPS of such anaerobes was purified by ultracentrifugation and DNase/RNase digestion, and characterized by a metachromatic assay for endotoxins and by electrophoresis on SDS-polyacrylamide gel and silver staining. Mouse LD50 for V. parvula LPS was 1.479 mg and for B. intermedius greater than 3.160 mg. Sublethal amounts of the LPS from anaerobes as well as from facultative aerobes decreased daily water intake and body weight in the mouse. Endotoxin from Salmonella typhimurium SL1102, Escherichia coli 0128:B12 and V. parvula had a strong effect on water intake and body weight, whereas Bacteroides intermedius LPS activity was very weak. The results of the present report suggest that V. parvula LPS has a toxic in vivo activity on mouse, which is comparable to LPS from classic enteric organisms and stronger than B. intermedius LPS.
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PMID:Biological effects of Veillonella parvula and Bacteroides intermedius lipopolysaccharides. 177 87

The adherence of lipopolysaccharides (LPSs) from periodontal disease-associated bacteria to saliva-coated hydroxyapatite (S-HA) and serum-coated HA beads was examined by chromogenic Limulus activity (toxicolor test). Phenol-water extracted LPS preparations from Bacteroides intermedius, Fusobacterium nucleatum, Actinobacillus actinomycetemcomitans, Eikenella corrodens, and rough-type LPS from Escherichia coli adhered to S-HA and serum-coated beads and agglutinated human erythrocytes. The adhered LPSs to S-HA and serum-coated HA beads were not removed by vigorous washing with distilled water. LPSs from Bacteroides (Porphyromonas) gingivalis strains and wild-type E. coli did not adhere to S-HA, serum-coated HA beads or show hemagglutinating activity. SDS-PAGE patterns stained with silver stain showed that LPSs adhered to S-HA, and serum-coated HA beads and erythrocytes possessed a distinct fast-migrating band similar to rough-type LPS. B. gingivalis LPSs possessed slow-migrating and repeating ladder bands similar to wild-type LPS.
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PMID:Adherence to experimental pellicle of rough-type lipopolysaccharides from subgingival plaque bacteria. 181 66

Laminin receptor was isolated from gastric epithelial cell membrane by the procedure involving membrane solubilization with octylglucoside followed by affinity chromatography on laminin-coupled Sepharose. The receptor protein, eluted from the matrix with cation-free EDTA buffer, yielded on SDS-PAGE a single 67kDa band. After radioiodination, the protein was incorporated into liposomes which displayed specific affinity toward the laminin-coated surface. The binding of liposomal receptor to the laminin-coated surface was inhibited by lipopolysaccharide from H.pylori. The inhibitory effect was proportional to the concentration of lipopolysaccharide up to 50 micrograms/ml at which point a 96% decrease in the receptor binding occurred. It is suggested that a similar process may account for the loss of mucosal integrity in the pathogenesis of H. pylori associated gastric disease.
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PMID:Inhibition of gastric mucosal laminin receptor by Helicobacter pylori lipopolysaccharide. 182 58

The maintenance of gastric mucosal integrity depends upon the interaction involving specific cell surface receptors with distinct proteins of extracellular matrix, one of which is laminin. We present here evidence that lipopolysaccharide from Helicobacter pylori interferes with laminin binding on the receptor. The laminin receptor was isolated from gastric epithelial cell membrane by the procedure involving membrane solubilization with octylglucoside followed by affinity chromatography on laminin-coupled Sepharose. The receptor protein yielded on SDS-PAGE a single 67 kDa band. After radioiodination, the protein was incorporated into liposomes which displayed specific affinity toward laminin-coated surface. The binding of liposomal receptor to the laminin-coated surface was inhibited by lipopolysaccharide from H. pylori. The inhibitory effect was proportional to the concentration of lipopolysaccharide up to 50 micrograms/ml, at which a 96% decrease in binding occurred. Introduction of sucralfate to the assay system led to the prevention of the inhibitory effect of lipopolysaccharide on the receptor-laminin binding. The effect was dose dependent and, at sucralfate concentration of 45 micrograms/ml, nearly complete restoration in binding was achieved. The results suggest that H. pylori also may be capable of disrupting the gastric mucosal integrity through a similar mechanism in vivo, and that anti-ulcer drug sucralfate counteracts this effect.
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PMID:Inhibition of gastric mucosal laminin receptor by Helicobacter pylori lipopolysaccharide: effect of sucralfate. 183 19

A laminin receptor was isolated from bovine gingival epithelial-cell membrane. After solubilization with octylglucoside, the receptor was subjected to affinity chromatography on laminin-coupled Sepharose and eluted with cation-free EDTA buffer yielding on SDS-PAGE a 67 kDa protein band. After radioiodination, the protein was incorporated into liposomes which displayed specific affinity towards laminin-coated surfaces, as well as to tooth cementum. The binding of receptor protein to cementum was inhibited by lipopolysaccharide from Bacteroides gingivalis. Preincubation of cementum with the lipopolysaccharide decreased the binding of the liposomal laminin-receptor preparation by 35.8%, while a 59.2% decrease in binding occurred when the lipopolysaccharide was preincubated with the receptor, suggesting that the lipopolysaccharide interfered with the laminin binding site on the receptor. The results demonstrate the existence of a specific gingival cell-surface laminin receptor, show that it is capable of binding to cementum, and provide evidence for the disruption of this process by bacterial lipopolysaccharide. This mechanism may account for the loss of gingival attachment in the pathogenesis of periodontal disease.
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PMID:Inhibition of bovine gingival laminin receptor by bacterial lipopolysaccharide. 187 30

Monoclonal antibodies (MAbs) were raised against the major, 46-48-Kda outer-membrane proteins of Vibrio cholerae O1. The hybridoma clones were screened by enzyme-linked immunosorbent assay (ELISA) with cell-surface proteins of V. cholerae O1 as the coating antigen. Four hybridomas, which secreted anti-V. cholerae cell-surface-protein antibodies, were subcloned by limiting dilution and obtained as ascites in vivo. A MAb of the IgG1 subclass was isolated in good yield from the murine ascites by affinity chromatography with recombinant protein G-Sepharose 4B. It gave positive reactions, as determined by ELISA, against cell-surface proteins prepared from both biotypes (classical and El Tor) and both serotypes (Ogawa and Inaba) of V. cholerae O1. The MAb did not have any reactivity towards V. cholerae lipopolysaccharide preparations. Immunoblotting studies were performed on cell-surface proteins separated by one-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (1D SDS-PAGE) and also by two-dimensional (2D) electrophoresis with iso-electric focusing in the first dimension followed by SDS-PAGE in the second dimension. When proteins were separated by 1D SDS-PAGE, only one band at 46-48 Kda reacted with the MAb. This protein appeared to consist of two narrowly-spaced and cross-reactive bands when a nitrocellulose blot, obtained by 2D SDS-PAGE, was exposed to the MAb.
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PMID:Production and characterisation of monoclonal antibodies to outer-membrane-protein antigens of Vibrio cholerae O1. 190 61

A rifampin-resistant mutant of Brucella abortus, designated RB51, was derived by repeated passage of strain 2308 on Trypticase soy supplemented with 1.5% agar and varying concentrations rifampin or penicillin. The RB51 colonies absorbed crystal violet and RB51 cell suspensions autoagglutinated, indicating a rough type colonial morphology for this strain. No O-chain component was detected in lipopolysaccharide (LPS) extracted from RB51 on SDS-PAGE gels stained with silver. Western blot analysis with the monoclonal antibody BRU 38, which is specific for the perosamine homopolymer O-chain of smooth Brucella LPS, indicated that the LPS of RB51 is highly deficient in O-chain when compared with the parenteral smooth strain 2308 or rough strain 45/20. Biochemically, RB51 resembles parental strain 2308 in its ability to utilize erythritol. Intraperitoneal inoculation of RB51 into mice results in a splenic colonization which is cleared within four weeks post infection. RB51 does not revert to smooth colony morphology upon passage in vivo (mice) or in vitro. Mice infected with RB51 produce antibodies against B. abortus antigens including class 2 and 3 outer membrane proteins but not against the O-chain. Furthermore, rabbits, goats and cattle hyperimmunized with sonicates of RB51 develop antibodies to B. abortus cellular antigens but do not develop antibodies specific for the O-chain. Immunization of mice with 1 x 10(8) viable RB51 organisms confers significant protection against challenge with virulent B. abortus strain 2308.
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PMID:Biological properties of RB51; a stable rough strain of Brucella abortus. 190 58

Lipase was isolated from P. aeruginosa by ultrafiltration of sterile-filtered culture supernatant. Gel filtration on Sepharose 4B yielded a broad peak corresponding to a molecular mass range of 100 to 1000 kDa. Electron microscopy of a negatively stained lipase preparation after Sepharose 4B chromatography revealed spherical particles with diameters ranging from 5 to 20 nm. Biochemical characterization and SDS polyacrylamide gel electrophoresis suggested that these particles consisted of protein and carbohydrate including lipopolysaccharide with the major enzyme activity being lipase. Various concentrations of this lipase preparation were preincubated with human peripheral blood neutrophils and monocytes. The chemotaxis and chemiluminescence of these cells were then determined. It was shown that lipase inhibited the monocyte chemotaxis and chemiluminescence, whereas it had no or very little effect on neutrophils. The inhibitory effect was concentration dependent and was abolished by heat treatment of the enzyme at 100 degrees C. Since monocytes are one of the important cells of the host defence system the inhibition of the function of these cells may contribute to the pathogenesis of infections caused by P. aeruginosa.
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PMID:Extracellular lipase of Pseudomonas aeruginosa: biochemical characterization and effect on human neutrophil and monocyte function in vitro. 191 Jan 41


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