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)

Cell envelopes prepared from smooth and rough strains of Brucella were characterized on the basis of lipopolysaccharide and protein content. The action of three kinds of detergents on Brucella cell envelopes and Escherichia coli control cell envelopes was examined on the basis of the proteins and lipopolysaccharides that were extracted. As compared with those of E. coli, Brucella cell envelopes were resistant to nonionic detergents. Zwittergents 312 and 316 were most effective in extracting E. coli cell envelopes, and Zwittergent 316 was most effective in extracting Brucella cell envelopes. Sarkosyl extracted proteins but extracted only trace amounts of lipopolysaccharides from cell envelopes of both bacteria. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the Sarkosyl-resistant proteins revealed a composition similar to that of the proteins exposed on the surfaces of viable cells, as determined by the lactoperoxidase-125I radioiodination method. EDTA, with either Tris-HCl or Tris-HCl-Triton X-100, did not have detectable effects on Brucella cell envelopes. Ultracentrifugation of purified lipopolysaccharides in detergents and EDTA demonstrate that, in contrast to that of E. coli, Brucella lipopolysaccharide was not stabilized by divalent cations. Sarkosyl was ineffective in dispersing lipopolysaccharides, whereas the action of Zwittergents was related to the length of their alkyl chains.
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PMID:Effects of nonionic, ionic, and dipolar ionic detergents and EDTA on the Brucella cell envelope. 681 15

The traT protein (TraTp) of the F sex factor is the product of one of the two genes involved in surface exclusion. Several detergents were examined under different conditions in order to determine their ability to solubilize TraTp from membrane vesicles. These experiments showed that TraTp behaved similar to a number of peptidoglycan-associated outer membrane proteins and that it existed in multimeric aggregates within the membrane. However, unlike other major outer membrane proteins, the amount of TraTp incorporated into the membrane was not affected by lipopolysaccharide-deficient mutants, even when mutants totally lacking the neutral sugars in their lipopolysaccharide backbone were used. TraTp wqs also examined by two-dimensional gel electrophoresis, where it ran as a discrete spot with a very basic isoelectric point. By coupling cyanogen bromide-activated dextran onto whole cells and by labeling whole cells with 125I (via lactoperoxidase), it was shown that TraTp was exposed on the cell surface. TraTp in a membrane environment was also insensitive to proteolytic attack by trypsin.
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PMID:Outer membrane of Escherichia coli: properties of the F sex factor traT protein which is involved in surface exclusion. 698 6

Injection of heat killed bacteria into kidney parenchyma results in pathologic lesions similar to chronic pyelonephritis while immunosuppression reverses this phenomenon. These observations and the propensity of lipid A to bind to cell membranes suggest that the lipid component of bacterial lipopolysaccharide antigens may be important in the pathogenesis of kidney tubule cell death. The right kidneys of syngeneic Fischer 344 rats were repeatedly injected with glycolipid prepared from Salmonella minnesota Re 595 cell walls. As a control, the contralateral kidney was injected with normal saline. The inflammatory response observed in the glycolipid injected kidney was significantly greater (p less than 0.005) than the response detected in the contralateral saline injected control kidney. Electron microscopy of kidney tubule cells incubated with peroxidase conjugated glycolipid demonstrated glycolipid bound to the kidney tubule cell plasma membranes. These studies suggest that individual antigenic components can induce kidney lesions and tubule cell death similar to that seen in chronic pyelonephritis.
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PMID:Salmonella Minnesota Re 595 lipid A induced nephritis. 706 6

A recent report (Cooper et al., Infect. Immun. 28:92-100, 1980) demonstrated that immunization of guinea pigs with ribosomal preparations was protective (approximately 90%) against chamber infections with Neisseria gonorrhoeae. Similar protection has been demonstrated with other cellular immunogens such as outer membranes (OM) (92%) or purified lipopolysaccharide (LPS) (83%). Protection of LPS (5 to 100 micrograms) was dose dependent (83% with 100 micrograms). Treatment of LPS with pronase reduced the protection by 50%. Ribosomal preparations contained LPS contamination (3.9%) based on dry weight determinations by 2-keto-3-deoxyoctonate analysis. Analysis of ribosomal preparations isolated from cells after lactoperoxidase-mediated 125I labeling indicated a major OM contamination (Protein I). The ribosomal preparation also contained low levels of succinic and lactic dehydrogenase. Passive hemagglutination tests revealed that sera from guinea pigs immunized with ribosomal preparations also demonstrated antibody to OM proteins and LPS. LPS was able to absorb one line of precipitation seen in immunodiffusion reactions as well as the bactericidal activity of such sera. OM preparations were unable to absorb the remaining precipitin line or remove the bactericidal activity. It appears that LPS is the major antigen responsible for the bactericidal activity seen in ribosome-immune sera.
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PMID:Role of outer envelope contamination in protection elicited by ribosomal preparations against Neisseria gonorrhoeae infection. 721 84

The surface of dendritic cells (DC) has been analyzed by means of monoclonal antibodies (Ab) and lactoperoxidase (LPO)-mediated radioiodination. Antigens and other exteriorily disposed polypeptides of purified spleen DC were compared with those of tissue macrophages (Mphi), monocytes, and other bone marrow-derived elements. Quantitative binding studies and autoradiography with (125)I-Ab established that DC expressed high levels of I-A and H-2D, 2 x 10(5) and 1 x 10(5) Ab binding sites per cell, respectively. DC from conventional, germ-free, and specific pathogen-free mice were all rich in Ia. Expression of Ia on B cells was 5-10 percent of that on DC and increased fivefold during lipopolysaccharide mitogenesis. More than 70-90 percent of purified Mphi and monocytes from specific pathogen-free mice were Ia negative, but increased levels of Ia were noted on cells from mice reared under conventional conditions. Thus large amounts of Ia on DC is a constitutive trait, whereas the expression of Ia by other cell types may be governed by the environmental and immunological status of the host. The 2.4G2 Fc receptor Ag was not detected on DC. Peritoneal and spleen Mphi had 10(5) 2.4G2 binding sites/cell, whereas monocytes and lymphocytes were less reactive (1 x 10(4)-3 x 10(4) binding sites/cell). Four other Mphi-related antigens were evaluated. Each had a distinctive tissue distribution and none bound exclusively to Mphi and monocytes. Neither 1.21J (Mac-1) nor F4/80 reacted with DC. Immunoprecipitation studies of externally ((125)I) and biosynthetically ([(35)S]methionine)dabeled cells confirmed the binding data. Sensitive binding assays with (125)I-Ab confirmed previous observations that DC lack Ig and Thy-1. Lyt-1 was also not found on DC, but 5-12 percent of the cells in purified DC preparations expressed both Lyt-2 and Ia. All DC expressed the leukocyte common antigens at levels similar to other leukocytes. The spectrum of surface polypeptides labeled by LPO-mediated iodination was different on Mphi, DC, and lymphocytes. Polypeptides migrating at molecular weights of 155,000, 85,000, and 62,000 appeared to be restricted to DC. These observations establish that the cell surface of DC differs considerably from other leukocytes, including the blood monocyte, and suggest that the DC is part of a unique Ia-rich leukocyte differentiation pathway.
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PMID:Studies of the cell surface of mouse dendritic cells and other leukocytes. 725 26

The optimal conditions for the detection of outer membrane proteins (OMPs) and lipopolysaccharide (LPS) of Pasteurella haemolytica by immunoblotting were evaluated. The variables examined included the equilibration time of the gels before transfer, composition of the transfer buffer, type of blotting membrane, blocking agent, effect of the zwitterionic detergent Empigen BB on protein renaturation, and the development reagent. The composition of the transfer buffer and time of gel equilibration significantly affected the efficiency of transfer of both OMPs and LPS. However, the optimal conditions for the transfer of OMPs were not the same as those for LPS. Thus, optimal transfer of OMPs occurred in Tris-glycine buffer, with prior equilibration of the gels to allow for expansion, whereas optimal transfer of LPS was achieved in Tris-glycine-methanol buffer with no equilibration of the gels. In Tris-glycine-methanol buffer, gel equilibration resulted in a significantly reduced transfer of both OMPs and LPS, probably due to the removal of SDS from these components. The use of Zeta-Probe blotting membrane which, unlike nitrocellulose, does not require methanol for optimal protein binding, did not result in improved binding of OMPs or LPS in the absence of methanol and, even after prolonged blocking (> 2 h), gave higher background staining than did nitrocellulose. Effective blocking of nitrocellulose was achieved with 3% (w/v) gelatin, 2.5% (w/v) skimmed milk or 0.3% (v/v) Tween 20, whereas increased background staining occurred with 1% (w/v) bovine serum albumin or 1% (w/v) ovalbumin. The incorporation of Empigen BB in the primary antibody buffer did not improve antibody recognition of proteins as a result of their renaturation. For the horseradish-peroxidase enzyme development system, the substrate 3,3'-diaminobenzidine tetrahydrochloride was more sensitive, and developed more quickly, than 4-chloro-1-naphthol, but faded more rapidly after drying of the membrane. 4-chloro-1-naphthol was more suitable for identifying OMPs because less background staining occurred, whereas 3,3'-diaminobenzidine tetrahydrochloride was more suitable for the detection of LPS due to its greater sensitivity.
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PMID:Evaluation of different methods for the detection of outer membrane proteins and lipopolysaccharides of Pasteurella haemolytica by immunoblotting. 750 80

The application of O antigen-specific antisera to the detection of Salmonella lipopolysaccharide (LPS) antigens was examined in an enzyme immunoassay using polymyxin-coated polyester cloth. The LPS antigens were extracted with deoxycholate and captured on polymyxin-cloth. A mixture of rabbit antisera to Salmonella O antigens was allowed to react with the captured antigens, and the reacted antibodies were detected by an anti-rabbit IgG-peroxidase conjugate. The assay gave positive results with 40 different Salmonella serotypes which represented more than 99.9% of the serogroups isolated from over 122,000 food, feed and environmental samples analysed at Laboratory Services Division, Agriculture Canada, from 1975 to 1990. Strong cross-reactivity with Staphylococcus aureus was eliminated by pregrowth of the organisms in the presence of sodium deoxycholate. The O antisera were commercially available and are more economical than monoclonal or affinity purified polyclonal antibodies.
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PMID:Use of inexpensive O antisera as the detecting antibodies for Salmonella antigens in the polymyxin-cloth enzyme immunoassay. 750 35

Nitric oxide (NO) is a messenger molecule that functions as a vasodilator and accounts for the biologic activity of endothelium-derived relaxing factor (EDRF). The enzyme responsible for NO production, NO synthase (NOS), exists in different isoforms. Some are expressed constitutively in various tissues, whereas others require induction by endotoxin and cytokines. There is evidence that NO plays an important role in the regulation of basal renal vascular resistance and in the tubuloglomerular feedback response. Specific antibodies to a constitutive NOS isolated from rat brain (B-NOS) and an inducible NOS isolated from rat aortic smooth muscle (VSM-NOS) were used to establish the cellular and subcellular distribution of NOS in the kidney. Kidneys from normal rats were preserved and processed for light and electron microscopic immunohistochemical studies using both a preembedding and a postembedding horseradish peroxidase technique. By light microscopy, strong immunostaining for B-NOS was observed in the juxtaglomerular apparatus, where it was located in cells of the macula densa. In contrast, immunostaining for VSM-NOS was specifically located in the terminal afferent arteriole and occasionally also in the initial efferent arteriole in the juxtaglomerular apparatus. In addition, faint immunostaining was present in the entire distal tubule. There was no labeling of arcuate or interlobular arteries. The injection of lipopolysaccharide was associated with increased immunostaining for VSM-NOS in the afferent arteriole but had no effect on B-NOS staining. By electron microscopy, B-NOS immunostaining was present throughout the cytoplasm of the macula densa cells, where it appeared to be associated mainly with small vesicles. Immunostaining for VSM-NOS in the afferent arteriole exhibited a patchy distribution in some cells, whereas other cells were stained throughout the cytoplasm. These results indicate that two distinct isoforms of NOS are present in the juxtaglomerular apparatus and support the hypothesis that NOS is involved in the regulation of tubuloglomerular feedback and glomerular capillary pressure.
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PMID:Immunocytochemical localization of distinct isoforms of nitric oxide synthase in the juxtaglomerular apparatus of normal rat kidney. 751 31

Small numbers of CD34+ primitive hematopoietic progenitors are found in normal human peripheral blood. These cells differentiate to myeloid or lymphoid lineage under the influence of different growth factors. We investigated the effects of IL5 and other growth factors on the production of eosinophils from peripheral blood CD34+ cells. CD34+ cells were enriched from normal donors by apheresis and positive selection using an affinity column and plated in agarose with different combinations of cytokines. At 14 days of growth a triple stain technique was used to identify eosinophil, monocyte, and neutrophil colonies. IL5 alone did not support colony growth from CD34+ cells. In contrast, GM-CSF and IL3 alone or together without added IL5 supported the generation of more than 50% pure eosinophil colonies. Addition of IL5 did not change the total number of colonies, but increased the fraction of pure eosinophil colonies to over 70%. Addition of G-CSF reduced the percentage of eosinophil colonies and increased the percentage of neutrophil colonies. Under the best conditions for eosinophil colony growth (IL3+GM-CSF+IL5), the addition of interferon-alpha or bacterial lipopolysaccharide inhibited colony growth by 51 and 58%, respectively. Addition of interferon-gamma, tumor necrosis factor-alpha, or dexamethasone had no effect on eosinophil colonies. Since IL5 alone did not support colony growth from CD34+ cells, we determined when IL5-responsive cells appeared in culture. Cells were grown initially with IL3 + GM-CSF in suspension, washed, and plated in agarose with IL5 alone. Only when progenitors were grown at least 3 days could IL5 serve as the single growth factor supporting pure eosinophil colony growth (47 colonies/10(4) cells plated at Day 3 and 134 colonies/10(4) cells at Day 7). We used neutralizing anti-IL5 antibodies to demonstrate that this late acting IL5 growth effect was specific, and that differentiation of eosinophils in the presence of IL3 + GM-CSF was IL5 independent. Using reverse-transcriptase polymerase chain reaction, the mRNA encoding the eosinophil-specific protein eosinophil peroxidase (EPO) was not detected in Day 0 CD34+ cells, but was demonstrated by Day 3 of culture. We conclude that within 3 days of culture, peripheral blood CD34+ cells can become committed to the eosinophil lineage as demonstrated by responsiveness to IL5 and production of EPO transcripts.
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PMID:Modulation of growth and differentiation of eosinophils from human peripheral blood CD34+ cells by IL5 and other growth factors. 753 Nov 18

Interstitial pneumonia has been reported to be a side effect of treatment with interferon, and Sho-saiko-to (Xiao-Chai-Hu-Tang) may enhance this side effect. It is well known that activated neutrophils are important mediators of pulmonary fibrosis, so we studied the effects of interferon and Sho-saiko-to on neutrophil activation. Homogenized lung myeloperoxidase (MPO) activity was assayed after intraperitoneal injection of interferon with or without pretreatment with Sho-saiko-to. Although Sho-saiko-to alone did not change the lung MPO content, MPO in the lung was significantly increased by interferon administration. The increase was enhanced further by pretreatment with Sho-saiko-to. When the accumulated neutrophils are activated by some cytokines, such as TNF alpha or IL-1 beta from monocytes/macrophages, they may damage lung tissue. We therefore studied the effects of Sho-saiko-to and interferon on TNF alpha production in freshly isolated human monocytes. Sho-saiko-to increased the production of TNF alpha, but interferon did not. In addition, Sho-saiko-to significantly increased the production of TNF alpha by monocytes stimulated by lipopolysaccharide. Taken together, these data indicate that interferon causes neutrophils to accumulate in the lung. Sho-saiko-to alone may not injure lung tissue, but it increases the effect of interferon. When stimulated by some antigen, Sho-saiko-to may overstimulate the neutrophils. Granulocytes elastase and oxygen radicals released from activated neutrophils may damage lung tissue. The fibroblasts that repair the damaged tissue may increase the risk of pulmonary fibrosis.
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PMID:[A possible mechanism of interstitial pneumonia during interferon therapy with sho-saiko-to]. 754 Jun 98


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