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)

Human polymorphonuclear leukocytes (PMN) preincubated overnight with 100 U/mL gamma-interferon (IFN-gamma) had an increased metabolic response, as measured by iodination and/or superoxide production, to stimulation by tumor necrosis factor (TNF), granulocyte-macrophage colony-stimulating factor (GM-CSF), formylmethionyl-leucyl-phenylalanine (FMLP), opsonized zymosan, and lipopolysaccharide (LPS), as compared with cells comparably preincubated in the absence of IFN-gamma. The decline in the staphylocidal activity of the stored PMN was also prevented in part by IFN-gamma, as was the depressed adherence of PMN stimulated with phorbol myristate acetate (PMA), FMLP, TNF, GM-CSF, and LPS. This protective effect of IFN-gamma on PMN function was associated with the prolonged surface expression of the complement receptor three (CR3) alpha-chain (CD11b), CR3 beta-chain (CD18), FcRII (CD32), and FcRIII (CD16), and the appearance of surface FcRI (CD64). The polymerase chain reaction (PCR) was used to amplify neutrophil RNA-derived cDNA recognized by synthetic oliogonucleotides designed from published nucleotide sequences for specific proteins. Using this procedure, mRNA for gp91-phox, p67-phox, p47-phox, CD64, two forms of CD32, CD16, CD11b, CD18, and actin were found to be depressed after overnight storage of neutrophils, and this decrease in steady-state mRNA levels was in part or totally prevented by IFN-gamma. CD64 and gp91-phox mRNA were generally increased by IFN-gamma to a level greater than that of freshly isolated neutrophils. Northern analysis of CD64 and p47 phox mRNAs confirmed the findings with the PCR method. These findings suggest that storage of PMN in a functionally active state is favored by the presence of IFN-gamma.
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PMID:Effects of gamma-interferon on human neutrophils: protection from deterioration on storage. 131 36

It is well known that activated prophenoloxidase (proPO) plays an important role in cuticular melanization and sclerotization. In addition, studies dealing with immune response of insects suggest that phenoloxidase (PO) is also critical in the defense reactions of insects against invaders. proPO is activated by elicitors derived from microbial cell wall components such as peptidoglycan, beta-1,3-glucan, and lipopolysaccharide (LPS). According to our recent studies we proposed a model clarifying the role of PO in both cellular and humoral immune responses. LPS triggers Ceratitis capitata hemocytes via induced protein tyrosine phosphorylation to release biologically active molecules, including p47 and proPO-activators. Furthermore, hemocytes in response to LPS facilitate clearance of LPS from the hemocoel of medfly. The effector molecules involved in the LPS clearance are hemocyte surface-associated p47 (mp47), soluble p47 (sp47), activated proPO, and tyrosine. A similar LPS clearance system in the integument of medfly in vitro was also demonstrated. According to our data, the proposed mechanism for LPS clearance from hemocoel and from integument is the crosslinking of LPS to p47 or certain integumental proteins via the intermediacy of reactive tyrosine derivatives generated by PO activity, as is the case for cuticular protein-chitin crosslinks during sclerotization. We also demonstrated that metabolites of the eumelanin biosynthesis and not melanin itself or N-acetyldopamine (NADA), the key precursor of sclerotizing agent, were necessary for the immune responses by hemocytes and integument.
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PMID:Immune response in insects: the role of phenoloxidase in defense reactions in relation to melanization and sclerotization. 858 Apr 94

It is well known that lipopolysaccharide (LPS) of Gram-negative bacteria triggers antibacterial responses to mammalian macrophages [Weinstein, S., Gold, M. R. & DeFranco, A. (1991) Proc. Natl Acad. Sci. USA 88, 4148-4152] and insect hemocytes [Charalambidis, N.D., Zervas, C.G., Lambropoulou, M., Katsoris, P.G. & Marmaras, V.J. (1995) Eur J. Cell Biol. 67, 32-41], via protein-tyrosine phosphorylation. In this study we show that insect hemocytes in response to LPS facilitate internalization of LPS (either cell-associated or cell-free). According to our data, the recognition and covalent association of LPS (either cell-associated or cell-free) to the hemocyte surface are essential initial steps for LPS internalization. LPS (Escherichia coli) recognizes membrane effector 47-kDa protein (p47) and then crosslinks to membrane-associated p47 (mp47) via the intermediacy of tyrosine derivatives generated by the action of phenol oxidase, as is the case for cuticular protein-chitin crosslinks during sclerotization [Shaefer, J., Kramer, K.J., Garbow, J.R., Jacob, G.S., Stejskal, E.O., Hopkins, T.L. & Speirs, R.D. (1987) Science 235, 1200-1204]. The covalent association of LPS to the hemocyte surface appears to be a prerequisite for LPS internalization as judged by the resistance of LPS binding to dissociation by proteinase K. In addition, our results show that the effector molecules participating in LPS covalent association at the cell surface and LPS internalization are not involved in LPS-induced activation of hemocytes. However, the fact that genistein, as well as the inhibitors of LPS-dependent secretion, block LPS covalent association at the cell surface and LPS internalization provides a preliminary characterization of an LPS signal-transduction-dependent process which is apparently involved.
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PMID:Covalent association of lipopolysaccharide at the hemocyte surface of insects is an initial step for its internalization--Protein-tyrosine phosphorylation requirement. 861 65

Bacterial lipopolysaccharide (LPS) attachment at the hemocyte surface is based on the crosslinking of surface associated p47 to LPS, via the intermediacy of tyrosine derivatives generated by the action of phenoloxidase (PO). This attachment is an initial step for LPS internalization from hemocytes (Charalambidis et al., 1996). The results presented clearly show the critical role of hemocyte associated PO activity in the above processes. Biochemical and immunofluorescent analysis demonstrated unambiguously the presence of prophenoloxidase (proPO) on the hemocyte surface. The cell-surface expression of proPO appeared to be LPS-independent, whereas its activation was LPS-dependent. The activation of cell surface proPO involves a limited proteolysis, since upon activation with chymotrypsin proPO is converted to a set of smaller molecular weight proteins with PO activity. The activation appears to be due to enzyme activators, serine proteases, released upon LPS-stimulation. This hypothesis was supported from the activation of membrane proPO by the culture medium of hemocytes which have been triggered with LPS. In addition, proPO, activation was abolished by inhibitors of secretion and PMSF. The release of proPO activators upon LPS-stimulation is mediated via protein tyrosine phosphorylation, as genistein inhibited proPO activation, a situation similar to that reported by us for the release of the effector protein p47 (Charalambidis et al., 1995). The LPS-stimulated activation of cell-surface proPO is a prerequisite for LPS (either cell associated or cell free) internalization, as judged by the resistance of LPS binding to dissociation by proteinase K.
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PMID:Hemocyte surface phenoloxidase (PO) and immune response to lipopolysaccharide (LPS) in Ceratitis capitata. 901 31

Insect hemocytes in response to lipopolysaccharide (LPS) of Gram-negative bacteria facilitate binding and internalization of either cell-associated or cell-free LPS (Charalambidis, N. D., Foukas L. C., and Marmaras V. J. (1996) Eur. J. Biochem. 236, 200-206). An early event in LPS signaling in hemocytes involves protein tyrosine phosphorylation (Charalambidis N. D., Zervas C. G., Lambropoulou M., Katsoris P. G., and Marmaras V. J.(1995) Eur. J. Cell Biol. 67, 32-41). Here we report further data of LPS-mediated signal transduction responsible for Escherichia coli phagocytosis. We demonstrate that both adhesion of hemocytes to substrata and LPS stimulation can cause activation of p44(MAPK) in Ceratitis capitata hemocytes but with distinct kinetics indicating different functions. In addition, we showed that Drk, a homolog protein to the mammalian GRB2, is implicated in the transmission of LPS signaling, indicating that the Ras/mitogen-activated protein kinase pathway is involved. Either the cell-free or the cell-associated LPS appears to attach to the hemocyte surface by the same mechanism that is based on the cross-linking of LPS to membrane-associated p47 via the intermediacy of tyrosine derivatives generated by the action of phenol oxidase. By contrast, the cell-free LPS internalization into the hemocytes differs from the cell-associated LPS internalization. For E. coli internalization integrin receptors as well as cytoskeletal rearrangements are required, as judged by inhibition of E. coli internalization in the presence of the RGD peptide, beta3-integrin antibodies, and cytochalasin D.
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PMID:Phagocytosis of Escherichia coli by insect hemocytes requires both activation of the Ras/mitogen-activated protein kinase signal transduction pathway for attachment and beta3 integrin for internalization. 961 82

Recently, we showed that cultured guinea pig gastric pit cells possess a phagocyte NADPH oxidase-like activity, which was up-regulated by Helicobacter pylori lipopolysaccharide. We demonstrate here that these cells express all of the phagocyte NADPH oxidase components (gp91-, p22-, p67-, p47-, and p40-phoxes). Treatment with lipopolysaccharide increased the expression of gp91-, p22-, and p67-phoxes, but not that of p47- and p40-phoxes. Intriguingly, the p67-phox expression consistently correlated with up-regulation of superoxide anion-producing ability. Thus, the gastric pit cell NADPH oxidase may play an important role in regulation of the inflammatory response associated with H. pylori infection.
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PMID:Helicobacter pylori lipopolysaccharide enhances the expression of NADPH oxidase components in cultured guinea pig gastric mucosal cells. 1038 99

Guinea pig gastric pit cells express an isozyme of gp91-phox, mitogen oxidase 1 (Mox1), and essential components for the phagocyte NADPH oxidase (p67-, p47-, p40-, and p22-phox). Helicobacter pylori lipopolysaccharide (LPS) and Escherichia coli LPS have been shown to function as potent activators for the Mox1 oxidase. These cells spontaneously secreted about 10 nmol of superoxide anion (O(2)(-))/mg of protein/h under LPS-free conditions. They expressed the mRNA and protein of Toll-like receptor 4 (TLR4) but not those of TLR2. LPS from type I H. pylori at 2.1 endotoxin units/ml or higher stimulated TLR4-mediated phosphorylations of transforming growth factor beta-activated kinase 1 and its binding protein 1 induced TLR4 and p67-phox and up-regulated O(2)(-) production 10-fold. In contrast, none of these events occurred with H. pylori LPS from complete or partial deletion mutants of the cag pathogenicity island. Lipid A was confirmed to be a bioactive component for the priming effects, while removal of bisphosphates from lipid A completely eliminated the effects, suggesting the importance of the phosphorylation pattern besides the acylation pattern for the bioactivity. H. pylori LPS is generally accepted as having low toxicity; however, our results suggest that type I H. pylori lipid A may be a potent stimulator for innate immune responses of gastric mucosa by stimulating the TLR4 cascade and Mox1 oxidase in pit cells.
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PMID:Type I Helicobacter pylori lipopolysaccharide stimulates toll-like receptor 4 and activates mitogen oxidase 1 in gastric pit cells. 1140 77

Gastric pit cells express mitogen oxidase1 (Mox1) and essential components for the phagocyte NADPH oxidase (p67-, p47-, p40-, and p22-phoxes). Helicobacter pylori (Hp) lipopolysaccharide (LPS) is a potent up-regulator of the Mox 1 oxidase. In this study, we examined the expression levels of several key members of the Toll-like receptor (TLR) family in primary cultures of guinea pig gastric pit cells. These cells expressed the TLR4 mRNA. Immunoblot analysis and immunofluorescence histochemistry with an anti-TLR4 antibody showed that gastric pit cells possessed significant amounts of TLR4 protein preferentially on the plasma membrane. In contrast, the cells did not express the TLR2 and TLR9 transcripts and did not contain detectable amounts of TLR2 protein. Neither peptidoglycan from Staphylococcus aureus nor Hp DNA with the CpG motif up-regulated Mox1 oxidase activity. Hp LPS activated nuclear factor-kappa B in association with the expression of cyclooxygenase II and tumor necrosis factor alpha transcripts. These findings suggest that TLR4 may play a crucial role in the initiation of inflammatory responses of gastric pit cells against Hp infection.
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PMID:Toll-like receptor 4 regulates gastric pit cell responses to Helicobacter pylori infection. 1169 59

The molecular sources of reactive oxygen species (ROS) in skeletal muscles are not well understood. We hypothesized that nonphagocyte NAD(P)H oxidase could be a source of ROS in muscle fibers. We thus investigated the existence, structure, and contribution of nonphagocyte NAD(P)H oxidase to ROS production in rat skeletal muscles. ROS production and NAD(P)H oxidase activity were evaluated by lucigenin-enhanced chemiluminescence and NADH consumption rate, whereas enzyme composition was monitored by reverse transcription-polymerase chain reaction and immunoblotting. Basal O(-)(2) production in muscle strips from normal rats averaged 1.4 nmol/mg per 10 min and increased to approximately 18 nmol/mg per 10 min in the presence of NADH. Muscle O(-)(2) production and NADH consumption were inhibited by Tiron, superoxide dismutase, apocynin, and diphenyleneiodonium but not by inhibitors of cyclo-oxygenases, xanthine oxidase, nitric oxide synthases (NOS), and mitochondrial enzymes. We detected mRNA and proteins of p22(phox), gp91(phox), p47(phox), and p67(phox) subunits in normal rat muscles. These subunits were localized in close proximity to the sarcolemma. Induction of sepsis in rats doubled muscle O(-)(2) production with no major changes in muscle NADPH oxide subunit expression. In lipopolysaccharide-treated but not in control muscles, O(-)(2) production was increased significantly by NOS inhibition. We conclude that a constitutively active NAD(P)H oxidase enzyme complex exists in normal skeletal muscle fibers and contributes to ROS production. In septic rats, this production is increased but measurable O(-)(2) is reduced by enhanced NO production.
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PMID:Molecular characterization of a superoxide-generating NAD(P)H oxidase in the ventilatory muscles. 1255 34

Sepsis is associated with increased production of reactive oxygen species (ROS); however, the metabolic sources of increased ROS are not well understood. We hypothesized that the recently described nonphagocytic NAD(P)H oxidase system could be an important source of the ROS superoxide anion (O2-) during sepsis, and the interaction of O2- with nitric oxide (NO) may contribute to sepsis-induced vascular Injury. To evaluate this issue, we measured O2- production before and after treatment with lipopolysaccharide (LPS) in rats, who are Inducible NO synthase producers (NOSII) and in pigs, who do not produce NOSII. LPS increased O2- production in aorta from rats from 0.38 +/- 0.07 nmol/mg/10 min to 1.18 +/- 0.23 nmol/mg/10 min, (P = 0.001) in rats, and 0.63 +/- 0.05 nmol/mg/10 min to 1.5 +/- 1.6 nmol/mg/10 min (P = 0.001) in carotid arteries from pigs. Components of NAD(P)H oxidase, including p22(phox), gp91(phox), p47(phox), p67(phox), mRNA and p22(phox), and gp91(phox) proteins were present in rat aorta and aorta and carotid arteries from pigs. Expression mildly increased in rats, but not in pigs. In rats, NADH and NADPH greatly increased O2- production with no difference in untreated versus LPS-treated rats. The addition of L-NAME increased NADH-dependant O2- production from 75 +/- 3 nmol/O2-/mg/10 min to 113 +/- 7 nmoVO2-/mg/10 min in LPS-treated rats, but had no effect in untreated rats. In pigs, the NADH-stimulated O2- production was 43 +/- 8 nmol/mg/10 min before and 63 +/- 4.3 nmol/mg/10 min after LPS even without L-NAME (P < 0.05). In contrast to LPS-treated rats, L-NAME markedly decreased NADH-stimulated O2- production (63 +/- 4 nmol/mg/10 min to 33 +/- 5.6 nmol/mg/10 min, P < 0.01). Luminol-enhanced chemiluminescence was also Increased in porcine carotid arteries after LPS treatment, which is consistent with peroxynitrite formation. Our results indicate that components of NAD(P)H oxidase are present in vessels of pigs and rats and there is substantial NADH-dependent O2- production that is increased after LPS. However, the behavior of NAD(P)H oxidase in NOSII-producing and nonproducing species differs with a reduction of O2- by NO in rats and NO-dependent production in pigs.
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PMID:Superoxide production in the vasculature of lipopolysaccharide-treated rats and pigs. 1274 95


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