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Journal articles on the topic 'LPS- binding proteins'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Fenton, Matthew J., and Douglas T. Golenbock. "LPS-binding proteins and receptors." Journal of Leukocyte Biology 64, no. 1 (1998): 25–32. http://dx.doi.org/10.1002/jlb.64.1.25.

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2

Hailman, E., H. S. Lichenstein, M. M. Wurfel, et al. "Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14." Journal of Experimental Medicine 179, no. 1 (1994): 269–77. http://dx.doi.org/10.1084/jem.179.1.269.

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CD14 is a 55-kD protein found as a glycosylphosphatidylinositol (GPI)-anchored protein on the surface of monocytes, macrophages, and polymorphonuclear leukocytes, and as a soluble protein in the blood. Both forms of CD14 participate in the serum-dependent responses of cells to bacterial lipopolysaccharide (LPS). While CD14 has been described as a receptor for complexes of LPS with LPS-binding protein (LBP), there has been no direct evidence showing whether a ternary complex of LPS, LBP, and CD14 is formed, or whether CD14 binds LPS directly. Using nondenaturing polyacrylamide gel electrophores

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3

Schumann, R. R., N. Lamping, and A. Hoess. "Interchangeable endotoxin-binding domains in proteins with opposite lipopolysaccharide-dependent activities." Journal of Immunology 159, no. 11 (1997): 5599–605. http://dx.doi.org/10.4049/jimmunol.159.11.5599.

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Abstract Host defense against microorganisms involves proteins that bind specifically to bacterial endotoxins (LPS), causing different cellular effects. Although LPS-binding protein (LBP) can enhance LPS activities, while bactericidal/permeability-increasing protein (BPI) and Limulus anti-LPS factor (LALF) neutralize LPS, it has been proposed that their LPS-binding domains possess a similar structure. Here, we provide evidence that the LBP/LPS-binding domain is, as in the LALF structure, solvent exposed and therefore available for LPS binding. Our investigations into the activity of LPS-bindin

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4

Qureshi, N., P. Y. Perera, J. Shen, et al. "NOVEL LPS-BINDING PROTEINS IN MURINE MACROPHAGES." Shock 17, Supplement (2002): 28. http://dx.doi.org/10.1097/00024382-200206001-00082.

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5

Lei, M. G., and D. C. Morrison. "Specific endotoxic lipopolysaccharide-binding proteins on murine splenocytes. II. Membrane localization and binding characteristics." Journal of Immunology 141, no. 3 (1988): 1006–11. http://dx.doi.org/10.4049/jimmunol.141.3.1006.

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Abstract We have characterized the binding of LPS to an 80-kDa LPS-binding protein detected by an LPS photoaffinity probe to be present on murine splenocytes. Specific binding of LPS to the 80-kDa protein is directly proportional to LPS concentration at low concentrations of LPS and is saturable at high concentrations of LPS. Binding is inhibited by both homologous and heterologous underivatized LPS as well as by polysaccharide-free lipid A, indicating a specificity for the biologically active component of LPS. Analysis of the kinetics of binding indicate a time-dependent increase over the fir

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6

Naberezhnykh, G., V. Davydova, and T. Soloveva. "INTERACTION OF LIPOPOLYSACCHARIDE-BINDING PROTEINS WITH VARIOUS FORMS OF LIPOPOLYSACCHARIDES." Russian Journal of Biological Physics and Chemisrty 8, no. 2 (2024): 178–84. http://dx.doi.org/10.29039/rusjbpc.2023.0606.

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Lipopolysaccharide-binding proteins from two common jellyfish species Aurellia aurita and Ropelema asamushi were isolated and purified, and the interaction of lipopolysaccharides (LPS) of various structural types with LBP was studied. By inhibiting the interaction, it was found that both proteins specifically bind to the lipid and core fragments of the LPS molecule. There are two types of binding sites in LBP with Kd = 3,28 × 10-6 M and Kd = 0,13 × 10-6 M (for the protein from A. aurita) and Kd = 3,66 × 10-6 M and Kd = 0,27 × 10-6 M (for protein from R. asamushi). It has been shown by dynamic

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7

Elass-Rochard, Elisabeth, Dominique Legrand, Valerie Salmon, et al. "Lactoferrin Inhibits the Endotoxin Interaction with CD14 by Competition with the Lipopolysaccharide-Binding Protein." Infection and Immunity 66, no. 2 (1998): 486–91. http://dx.doi.org/10.1128/iai.66.2.486-491.1998.

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ABSTRACT Human lactoferrin (hLf), a glycoprotein released from neutrophil granules during inflammation, and the lipopolysaccharide (LPS)-binding protein (LBP), an acute-phase serum protein, are known to bind to the lipid A of LPS. The LPS-binding sites are located in the N-terminal regions of both proteins, at amino acid residues 28 to 34 of hLf and 91 to 108 of LBP. Both of these proteins modulate endotoxin activities, but they possess biologically antagonistic properties. In this study, we have investigated the competition between hLf and recombinant human LBP (rhLBP) for the binding of Esch

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8

Weersink, A. J., K. P. van Kessel, M. E. van den Tol, et al. "Human granulocytes express a 55-kDa lipopolysaccharide-binding protein on the cell surface that is identical to the bactericidal/permeability-increasing protein." Journal of Immunology 150, no. 1 (1993): 253–63. http://dx.doi.org/10.4049/jimmunol.150.1.253.

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Abstract Several LPS-binding proteins have been identified on the surface of human granulocytes (polymorphonuclear leukocyte (PMN)). We describe a plasma-membrane associated ca. 55-kDa LPS-binding protein of human PMN that is indistinguishable from the bactericidal/permeability-increasing protein (BPI). To detect LPS-binding proteins on the cell surface, PMN were biotinylated before detergent solubilization and incubation with LPS-coated beads. Several biotinylated proteins bound to LPS-coated beads but not to uncoated beads and were characterized after elution with detergent by SDS-PAGE and w

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9

Tobias, P. S., K. Soldau, L. Kline, et al. "Cross-linking of lipopolysaccharide (LPS) to CD14 on THP-1 cells mediated by LPS-binding protein." Journal of Immunology 150, no. 7 (1993): 3011–21. http://dx.doi.org/10.4049/jimmunol.150.7.3011.

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Abstract Recent work has established that bacterial endotoxin (LPS) binds to the plasma protein LPS-binding protein (LBP) forming high affinity complexes (LPS-LBP), that LBP is an opsonin for LPS-bearing particles, and that LPS-LBP complexes are potent agonists for monocytic cells (MO). mAb to the MO plasma membrane protein, CD14, inhibit LBP-dependent binding of LPS to MO, and LPS-LBP-dependent stimulation of cytokine release from MO. These data suggest that CD14 functions as a membrane receptor for LPS but do not demonstrate a direct association of LPS with CD14. Calcitriol was used to induc

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10

Amura, Claudia R., Takayuki Kamei, Noriko Ito, Michael J. Soares, and David C. Morrison. "Differential Regulation of Lipopolysaccharide (LPS) Activation Pathways in Mouse Macrophages by LPS-Binding Proteins." Journal of Immunology 161, no. 5 (1998): 2552–60. http://dx.doi.org/10.4049/jimmunol.161.5.2552.

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Abstract LPS binding to its receptor(s) on macrophages induces the synthesis of inflammatory mediators involved in septic shock. While the signaling mechanism(s) remains to be fully defined, the human LPS-binding protein (LBP) is known to regulate responses to LPS by facilitating its binding to CD14 on human monocytes. The structurally related bactericidal permeability increasing protein (BPI) differs from LBP by inhibiting LPS-induced human monocyte activation. We have demonstrated that, unlike the human monocyte response to LPS, both LBP and BPI inhibited LPS-stimulated TNF-α production in m

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11

Wright, S. D., and M. T. Jong. "Adhesion-promoting receptors on human macrophages recognize Escherichia coli by binding to lipopolysaccharide." Journal of Experimental Medicine 164, no. 6 (1986): 1876–88. http://dx.doi.org/10.1084/jem.164.6.1876.

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We report here that human macrophages bind Escherichia coli by recognizing bacterial lipopolysaccharide (LPS). Purified LPS was inserted into erythrocyte membranes, and the resulting LPS-coated red cells were bound by macrophages with the same temperature and cation dependence as observed for E. coli. When receptors for LPS were withdrawn from the plasma membrane by spreading the macrophages on LPS-coated surfaces, the binding of E. coli was blocked. We have also identified the receptors on macrophages that recognize LPS. Macrophages express three structurally homologous cell surface proteins,

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12

Hoess, A., Ch Ried, C. Wahl, R. Liddington, H. Wagner, and L. Schneider-Mergener. "110 THE LPS-BINDING DOMAIN OF ENDOTOXIN NEUTRALISING PROTEINS." Shock 3, no. 5 (1995): 34. http://dx.doi.org/10.1097/00024382-199505000-00111.

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13

Gravallese, E. M., J. M. Darling, L. H. Glimcher, and M. Boothby. "Role of lipopolysaccharide and IL-4 in control of transcription of the class II A alpha gene." Journal of Immunology 147, no. 7 (1991): 2377–83. http://dx.doi.org/10.4049/jimmunol.147.7.2377.

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Abstract The class II (Ia) MHC molecules are cell surface proteins that regulate the activation of T cells. B lymphocyte expression of class II molecules has been shown to be influenced by a number of external stimuli. It has been previously demonstrated that treatment of these cells with IL-4 leads to an increase in class II gene transcription at 18 h as well as to an increase in steady state class II mRNA. It has also been previously demonstrated that LPS treatment of splenic B cells from athymic mice results in a decrease in steady state mRNA encoding the A alpha class II protein. This decr

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14

Pulido, David, Rocío Rebollido-Rios, Javier Valle, David Andreu, Ester Boix, and Marc Torrent. "Structural similarities in the CPC clip motif explain peptide-binding promiscuity between glycosaminoglycans and lipopolysaccharides." Journal of The Royal Society Interface 14, no. 136 (2017): 20170423. http://dx.doi.org/10.1098/rsif.2017.0423.

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Lipopolysaccharides (LPSs) and glycosaminoglycans (GAGs) are polymeric structures containing negatively charged disaccharide units that bind to specialized proteins and peptides in the human body and control fundamental processes such as inflammation and coagulation. Surprisingly, some proteins can bind both LPSs and GAGs with high affinity, suggesting that a cross-communication between these two pathways can occur. Here, we explore whether GAGs and LPSs can share common binding sites in proteins and what are the structural determinants of this binding. We found that the LPS-binding peptide YI

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15

Gravallese, E. M., M. R. Boothby, C. M. Smas, and L. H. Glimcher. "A lipopolysaccharide-induced DNA-binding protein for a class II gene in B cells is distinct from NF-kappa B." Molecular and Cellular Biology 9, no. 8 (1989): 3184–92. http://dx.doi.org/10.1128/mcb.9.8.3184-3192.1989.

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Class II (Ia) major histocompatibility complex molecules are cell surface proteins normally expressed by a limited subset of cells of the immune system. These molecules regulate the activation of T cells and are required for the presentation of antigens and the initiation of immune responses. The expression of Ia in B cells is determined by both the developmental stage of the B cell and by certain external stimuli. It has been demonstrated previously that treatment of B cells with lipopolysaccharide (LPS) results in increased surface expression of Ia protein. However, we have confirmed that LP

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16

Gravallese, E. M., M. R. Boothby, C. M. Smas, and L. H. Glimcher. "A lipopolysaccharide-induced DNA-binding protein for a class II gene in B cells is distinct from NF-kappa B." Molecular and Cellular Biology 9, no. 8 (1989): 3184–92. http://dx.doi.org/10.1128/mcb.9.8.3184.

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Class II (Ia) major histocompatibility complex molecules are cell surface proteins normally expressed by a limited subset of cells of the immune system. These molecules regulate the activation of T cells and are required for the presentation of antigens and the initiation of immune responses. The expression of Ia in B cells is determined by both the developmental stage of the B cell and by certain external stimuli. It has been demonstrated previously that treatment of B cells with lipopolysaccharide (LPS) results in increased surface expression of Ia protein. However, we have confirmed that LP

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17

Dentener, M. A., E. J. Von Asmuth, G. J. Francot, M. N. Marra, and W. A. Buurman. "Antagonistic effects of lipopolysaccharide binding protein and bactericidal/permeability-increasing protein on lipopolysaccharide-induced cytokine release by mononuclear phagocytes. Competition for binding to lipopolysaccharide." Journal of Immunology 151, no. 8 (1993): 4258–65. http://dx.doi.org/10.4049/jimmunol.151.8.4258.

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Abstract Serum proteins play an important role in LPS-induced cell activation. The LPS binding protein (LBP) enhances cellular responses to LPS, whereas the polymorphonuclear leukocyte product bactericidal/permeability-increasing protein (BPI) inhibits LPS-induced cell activation. In this study the influences of LBP and BPI, two proteins with opposite effects, but with considerable sequence homology, on LPS-induced mononuclear phagocytic cell cytokine release was studied. LBP was shown to enhance LPS-induced TNF-alpha, IL-6, and IL-8 release by mononuclear phagocytic cells, whereas BPI inhibit

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18

Lei, M. G., and D. C. Morrison. "Specific endotoxic lipopolysaccharide-binding proteins on murine splenocytes. I. Detection of lipopolysaccharide-binding sites on splenocytes and splenocyte subpopulations." Journal of Immunology 141, no. 3 (1988): 996–1005. http://dx.doi.org/10.4049/jimmunol.141.3.996.

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Abstract Experiments have been carried out using a unique radio-iodinated, disulfide-reducible, photoactivatable LPS derivative (ASD-LPS) to detect specific LPS-binding proteins on murine splenocytes. Fractionation of LPS-photo-cross-linked, reduced, and solubilized splenocyte extracts on two-dimensional polyacrylamide gels has allowed the identification of an 80-kDa LPS-binding protein with approximate pI of 6.5. This LPS-binding protein is present on partially purified populations of splenic B lymphocytes, T lymphocytes, and macrophages. It is also the dominant LPS-binding protein on the mur

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19

EBERHARD, A. David, and R. Scott VANDENBERG. "Annexins I and II bind to lipid A: a possible role in the inhibition of endotoxins." Biochemical Journal 330, no. 1 (1998): 67–72. http://dx.doi.org/10.1042/bj3300067.

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Annexins are Ca2+-dependent phospholipid-binding proteins with anti-inflammatory properties that are present on the surfaces of, and released from, certain cell types, such as leukocytes and secretory epithelia. The present study investigated the possibility that annexins may bind directly to bacterial endotoxin, inhibiting its interactions with cellular receptors or accessory binding proteins. An enzyme-linked immunoassay demonstrated calcium-dependent binding of low nanomolar concentrations of annexin-I and annexin-II p36/p11 heterotetramer to lipid A. In contrast, little or no annexin bindi

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20

El-Samalouti, Volker T., Jens Schletter, Helmut Brade, et al. "Detection of Lipopolysaccharide(LPS)-Binding Membrane Proteins by Immuno-Coprecipitation with LPS and Anti-LPS Antibodies." European Journal of Biochemistry 250, no. 2 (1997): 418–24. http://dx.doi.org/10.1111/j.1432-1033.1997.0418a.x.

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21

Lamping, N., A. Hö, B. Yu, et al. "IDENTIFICATION OF THE LIPOPOLYSACCHARIDE (LPS) BINDING SITE OF LPS BINDING PROTEIN (LBP) BY SITE-DIRECTED MUTAGENESIS, EVIDENCE FOR A SIMILAR LPS RECOGNITION MECHANISM IN DIFFERENT LPS BINDING PROTEINS." Shock 7, Supplement (1997): 21–22. http://dx.doi.org/10.1097/00024382-199703001-00087.

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22

Krasity, Benjamin C., Joshua V. Troll, Jerrold P. Weiss, and Margaret J. McFall-Ngai. "LBP/BPI proteins and their relatives: conservation over evolution and roles in mutualism." Biochemical Society Transactions 39, no. 4 (2011): 1039–44. http://dx.doi.org/10.1042/bst0391039.

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LBP [LPS (lipopolysaccharide)-binding protein] and BPI (bactericidal/permeability-increasing protein) are components of the immune system that have been principally studied in mammals for their involvement in defence against bacterial pathogens. These proteins share a basic architecture and residues involved in LPS binding. Putative orthologues, i.e. proteins encoded by similar genes that diverged from a common ancestor, have been found in a number of non-mammalian vertebrate species and several non-vertebrates. Similar to other aspects of immunity, such as the activity of Toll-like receptors

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23

Triyatni, Miriam, Bertrand Saunier, Padma Maruvada, et al. "Interaction of Hepatitis C Virus-Like Particles and Cells: a Model System for Studying Viral Binding and Entry." Journal of Virology 76, no. 18 (2002): 9335–44. http://dx.doi.org/10.1128/jvi.76.18.9335-9344.2002.

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ABSTRACT Hepatitis C virus-like particles (HCV-LPs) containing the structural proteins of HCV H77 strain (1a genotype) was used as a model for HCV virion to study virus-cell interaction. HCV-LPs showed a buoyant density of 1.17 to 1.22 g/cm3 in a sucrose gradient and formed double-shelled particles 35 to 49 nm in diameter. Flow cytometry analysis by an indirect method (detection with anti-E2 antibody) and a direct method (use of dye-labeled HCV-LPs) showed that HCV-LPs binds to several human hepatic (primary hepatocytes, HepG2, HuH7, and NKNT-3) and T-cell (Molt-4) lines. HCV-LPs binding to ce

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24

Youn, Ju Ho, and Jeon-Soo Shin. "Identification of lipopolysaccharide binding site on High Mobility Group Box 1 Protein (98.23)." Journal of Immunology 182, no. 1_Supplement (2009): 98.23. http://dx.doi.org/10.4049/jimmunol.182.supp.98.23.

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Abstract Lipopolysaccharide (LPS), a bacterial endotoxin, triggers deleterious systemic inflammatory responses when released into blood circulation, causing severe sepsis, organ dysfunction and death. LPS binding components in serum play an important role in modifying LPS toxicity by facilitating its interaction with the LPS signaling receptor, which is expressed on LPS-responsive cells. We have previously shown that HMGB1 is able to bind LPS and this binding can increase LPS-induced TNF-α production in human peripheral blood monocytes. In this report, we identified several LPS binding regions

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Tobias, Peter S., Katrin Soldau, Nicole M. Iovine, Peter Elsbach, and Jerrold Weiss. "Lipopolysaccharide (LPS)-binding Proteins BPI and LBP Form Different Types of Complexes with LPS." Journal of Biological Chemistry 272, no. 30 (1997): 18682–85. http://dx.doi.org/10.1074/jbc.272.30.18682.

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26

Ding, A., E. Sanchez, M. Tancinco, and C. Nathan. "Interactions of bacterial lipopolysaccharide with microtubule proteins." Journal of Immunology 148, no. 9 (1992): 2853–58. http://dx.doi.org/10.4049/jimmunol.148.9.2853.

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Abstract Bacterial LPS is a potent stimulator of immune cells, but its mechanisms are unknown. A possible role for microtubules in LPS actions has been indicated by previous findings that the microtubule-active agent, taxol, can mimic some effects of LPS in macrophages from normal strains of mice, but not from genetically LPS-hyporesponsive strains. In this report we demonstrate that isolated microtubules from mouse brain can bind LPS in vitro. LPS and tubulin coeluted through a gel filtration column, and LPS was cross-linked to microtubule proteins with an iodinatable, photoreactive agent, su

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27

Bhat, Nayantara, Pin-Yu Perera, Joan M. Carboni, et al. "Use of a Photoactivatable Taxol Analogue to Identify Unique Cellular Targets in Murine Macrophages: Identification of Murine CD18 as a Major Taxol-Binding Protein and a Role for Mac-1 in Taxol-Induced Gene Expression." Journal of Immunology 162, no. 12 (1999): 7335–42. http://dx.doi.org/10.4049/jimmunol.162.12.7335.

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Abstract Taxol, a potent antitumor agent that binds β-tubulin and promotes microtubule assembly, results in mitotic arrest at the G2/M phase of the cell cycle. More recently, Taxol was shown to be a potent LPS mimetic in murine, but not in human macrophages, stimulating signaling pathways and gene expression indistinguishably from LPS. Although structurally unrelated to LPS, Taxol’s LPS-mimetic activities are blocked by inactive structural analogues of LPS, indicating that despite the species-restricted effects of Taxol, LPS and Taxol share a common receptor/signaling complex that might be imp

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28

Wellnitz, Sabine, Bettina Klumpp, Heidi Barth, et al. "Binding of Hepatitis C Virus-Like Particles Derived from Infectious Clone H77C to Defined Human Cell Lines." Journal of Virology 76, no. 3 (2002): 1181–93. http://dx.doi.org/10.1128/jvi.76.3.1181-1193.2002.

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ABSTRACT Hepatitis C virus (HCV) is a leading cause of chronic hepatitis in the world. The study of viral entry and infection has been hampered by the inability to efficiently propagate the virus in cultured cells and the lack of a small-animal model. Recent studies have shown that in insect cells, the HCV structural proteins assemble into HCV-like particles (HCV-LPs) with morphological, biophysical, and antigenic properties similar to those of putative virions isolated from HCV-infected humans. In this study, we used HCV-LPs derived from infectious clone H77C as a tool to examine virus-cell i

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29

Lin, Shih-Chang, Henry H. Wortis та Janet Stavnezer. "The Ability of CD40L, but Not Lipopolysaccharide, To Initiate Immunoglobulin Switching to Immunoglobulin G1 Is Explained by Differential Induction of NF-κB/Rel Proteins". Molecular and Cellular Biology 18, № 9 (1998): 5523–32. http://dx.doi.org/10.1128/mcb.18.9.5523.

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ABSTRACT Antibodies of the immunoglobulin G1 class are induced in mice by T-cell-dependent antigens but not by lipopolysaccharide (LPS). CD40 engagement contributes to this preferential isotype production by activating NF-κB/Rel to induce germ line γ1 transcripts, which are essential for class switch recombination. Although LPS also activates NF-κB, it poorly induces germ line γ1 transcripts. Western blot analyses show that CD40 ligand (CD40L) induces all NF-κB/Rel proteins, whereas LPS activates predominantly p50 and c-Rel. Electrophoretic mobility shift assays show that in CD40L-treated cell

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30

Koraha, Jun, Naoko Tsuneyoshi, Masao Kimoto, Jean-Francois Gauchat, Hiroshi Nakatake, and Kenji Fukudome. "Comparison of Lipopolysaccharide-Binding Functions of CD14 and MD-2." Clinical Diagnostic Laboratory Immunology 12, no. 11 (2005): 1292–97. http://dx.doi.org/10.1128/cdli.12.11.1292-1297.2005.

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ABSTRACT Prior to being recognized by the cell surface Toll-like receptor 4/MD-2 complex, lipopolysaccharide (LPS) in the bacterial outer membrane has to be processed by LPS-binding protein and CD14. CD14 forms a complex with monomeric LPS extracted by LPS-binding protein and transfers LPS to the cell surface signaling complex. In a previous study, we prepared a functional recombinant MD-2 using a bacterial expression system. We expressed the recombinant protein in Escherichia coli as a fusion protein with thioredoxin and demonstrated specific binding to LPS. In this study, we prepared recombi

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Rabinovich-Ernst, Orna, Clinton Bradfield, SungHwan Yoon, et al. "TurboID biotin-tagging mass spectrometry identifies specific caspase-11-associated proteins regulating non-canonical inflammasome activation." Journal of Immunology 206, no. 1_Supplement (2021): 15.06. http://dx.doi.org/10.4049/jimmunol.206.supp.15.06.

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Abstract While it has been demonstrated that cytosolic LPS can directly activate caspase11, the cellular processes regulating the non-canonical inflammasome response remain poorly defined. Caspase11 and caspase1 show substantial structural similarity, however, unlike the activation of caspase1 by NLR inflammasomes, there are no sensor or adaptor proteins known to be involved in transmitting cytosolic LPS signal to caspase11. Also, while caspase11 has been shown to associate with LPS, it lacks a characteristic LPS binding domain as observed in many other LPS binding proteins such as MD2 and LBP

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Fux, Alexandra C., Cristiane Casonato Melo, Sara Michelini, et al. "Heterogeneity of Lipopolysaccharide as Source of Variability in Bioassays and LPS-Binding Proteins as Remedy." International Journal of Molecular Sciences 24, no. 9 (2023): 8395. http://dx.doi.org/10.3390/ijms24098395.

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Lipopolysaccharide (LPS), also referred to as endotoxin, is the major component of Gram-negative bacteria’s outer cell wall. It is one of the main types of pathogen-associated molecular patterns (PAMPs) that are known to elicit severe immune reactions in the event of a pathogen trespassing the epithelial barrier and reaching the bloodstream. Associated symptoms include fever and septic shock, which in severe cases, might even lead to death. Thus, the detection of LPS in medical devices and injectable pharmaceuticals is of utmost importance. However, the term LPS does not describe one single mo

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33

Solov’eva, Tamara Fedorovna, Svetlana Ivanovna Bakholdina, and Gennadii Alexandrovich Naberezhnykh. "Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis." Marine Drugs 21, no. 11 (2023): 581. http://dx.doi.org/10.3390/md21110581.

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Sepsis is a life-threatening complication of an infectious process that results from the excessive and uncontrolled activation of the host’s pro-inflammatory immune response to a pathogen. Lipopolysaccharide (LPS), also known as endotoxin, which is a major component of Gram-negative bacteria’s outer membrane, plays a key role in the development of Gram-negative sepsis and septic shock in humans. To date, no specific and effective drug against sepsis has been developed. This review summarizes data on LPS-binding proteins from marine invertebrates (ILBPs) that inhibit LPS toxic effects and are o

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34

Ghafouri, B., E. Kihlström, B. Ståhlbom, C. Tagesson, and M. Lindahl. "PLUNC (palate, lung and nasal epithelial clone) proteins in human nasal lavage fluid." Biochemical Society Transactions 31, no. 4 (2003): 810–14. http://dx.doi.org/10.1042/bst0310810.

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PLUNC (palate, lung and nasal epithelial clone) is a newly discovered gene that is expressed in the upper respiratory tract and is suggested to be of importance in host defence against bacteria. We have identified two forms of the PLUNC protein in human nasal lavage fluid (NLF) using two-dimensional gel electrophoresis (2-DE) and MS. The apparent molecular masses and isoelectric points of these forms are 24.8 kDa/pI 5.4 and 25.1 kDa/pI 5.5. Notably, the 24.8 kDa/pI 5.4 form of PLUNC is an abundant protein in the 2-DE protein patterns of NLF from healthy subjects. Decreased levels of PLUNC were

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35

Vesy, C. J., R. L. Kitchens, G. Wolfbauer, J. J. Albers, and R. S. Munford. "Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein Release Lipopolysaccharides from Gram-Negative Bacterial Membranes." Infection and Immunity 68, no. 5 (2000): 2410–17. http://dx.doi.org/10.1128/iai.68.5.2410-2417.2000.

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ABSTRACT Although animals mobilize their innate defenses against gram-negative bacteria when they sense the lipid A moiety of bacterial lipopolysaccharide (LPS), excessive responses to this conserved bacterial molecule can be harmful. Of the known ways for decreasing the stimulatory potency of LPS in blood, the binding and neutralization of LPS by plasma lipoproteins is most prominent. The mechanisms by which host lipoproteins take up the native LPS that is found in bacterial membranes are poorly understood, however, since almost all studies of host-LPS interactions have used purified LPS aggr

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36

Roth, Robert I. "Hemoglobin Enhances the Binding of Bacterial Endotoxin to Human Endothelial Cells." Thrombosis and Haemostasis 76, no. 02 (1996): 258–62. http://dx.doi.org/10.1055/s-0038-1650565.

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SummaryHuman endothelial cells, when incubated with bacterial endotoxin (lipopolysaccharide, LPS), modify their surface in association with prominent production of procoagulant tissue factor (TF) activity. This deleterious biological effect of LPS has been shown previously to be enhanced approximately 10-fold by the presence of hemoglobin (Hb), a recently recognized LPS binding protein that causes disaggregation of LPS and increases the biological activity of LPS in a number of in vitro assays. The present study was performed to test the hypothesis that Hb enhances the LPS-induced procoagulant

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Zarewych, D. M., A. L. Kindzelskii, R. F. Todd, and H. R. Petty. "LPS induces CD14 association with complement receptor type 3, which is reversed by neutrophil adhesion." Journal of Immunology 156, no. 2 (1996): 430–33. http://dx.doi.org/10.4049/jimmunol.156.2.430.

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Abstract CD14, a glycosylphosphatidyl inositol (GPI)-linked membrane protein, is a key membrane binding site for LPS (endotoxin). Although CD14 lacks transmembrane and cytoplasmic sequences, it activates CR3-mediated leukocyte adhesion and cytokine release. Since CR3 has been shown to interact with other GPI-linked membrane proteins, we tested the hypothesis that CD14 can physically associate with CR3. Using qualitative and quantitative resonance energy transfer microscopy, we show that LPS in the presence of serum or LPS binding protein triggers formation of CD14-CR3 complexes. Kinetic studie

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Beamer, Lesa J., Daniel Fischer, and David Eisenberg. "Detecting distant relatives of mammalian LPS-binding and lipid transport proteins." Protein Science 7, no. 7 (1998): 1643–46. http://dx.doi.org/10.1002/pro.5560070721.

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de Haas, Carla J. C., Marijke E. van der Tol, Kok P. M. Van Kessel, Jan Verhoef, and Jos A. G. Van Strijp. "A Synthetic Lipopolysaccharide-Binding Peptide Based on Amino Acids 27–39 of Serum Amyloid P Component Inhibits Lipopolysaccharide-Induced Responses in Human Blood." Journal of Immunology 161, no. 7 (1998): 3607–15. http://dx.doi.org/10.4049/jimmunol.161.7.3607.

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Abstract LPS-binding proteins in plasma play an important role in modifying LPS toxicity. Significant properties have already been attributed to the LPS-binding protein (LBP). It accelerates LPS toxicity as well as incorporation into high-density lipoproteins, leading to neutralization of LPS in serum. A search for other LPS-binding components in serum, using LPS-coated magnetic beads, revealed a new LPS-binding protein. N-terminal microsequencing identified this protein as serum amyloid P component (SAP). Purified SAP bound to smooth and rough types of LPS via the lipid A part. SAP inhibited

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An, M. R., C. C. Hsieh, P. D. Reisner, et al. "Evidence for posttranscriptional regulation of C/EBPalpha and C/EBPbeta isoform expression during the lipopolysaccharide-mediated acute-phase response." Molecular and Cellular Biology 16, no. 5 (1996): 2295–306. http://dx.doi.org/10.1128/mcb.16.5.2295.

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The mRNAs of the CCAAT/enhancer-binding trans-activator proteins (C/EBPalpha and C/EBPbeta) serve as templates for the differential translation of several isoforms which have specific transcriptional regulatory functions. By using an oligonucleotide corresponding to the C/EBP binding site of the mouse alpha1-acid glycoprotein promoter, we detected multiple forms of C/EBPalpha and C/EBP++ beta proteins in the mouse liver that have DNA-binding activity. By using specific antisera, we detected C/EBPalphas with molecular masses of 42, 38, 30, and 20 kDa that have DNA-binding activity. The pool lev

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Han, Ji, Yong Lee, Jun Im, et al. "Astaxanthin Ameliorates Lipopolysaccharide-Induced Neuroinflammation, Oxidative Stress and Memory Dysfunction through Inactivation of the Signal Transducer and Activator of Transcription 3 Pathway." Marine Drugs 17, no. 2 (2019): 123. http://dx.doi.org/10.3390/md17020123.

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Astaxanthin (AXT), a xanthophyll carotenoid compound, has potent antioxidant, anti-inflammatory and neuroprotective properties. Neuroinflammation and oxidative stress are significant in the pathogenesis and development of Alzheimer’s disease (AD). Here, we studied whether AXT could alleviate neuroinflammation, oxidative stress and memory loss in lipopolysaccharide (LPS) administered mice model. Additionally, we investigated the anti-oxidant activity and the anti-neuroinflammatory response of AXT in LPS-treated BV-2 microglial cells. The AXT administration ameliorated LPS-induced memory loss. T

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MALHOTRA, Rajneesh, Richard PRIEST, and Michael I. BIRD. "Role for L-selectin in lipopolysaccharide-induced activation of neutrophils." Biochemical Journal 320, no. 2 (1996): 589–93. http://dx.doi.org/10.1042/bj3200589.

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The activation of leucocytes by bacterial cell wall lipopolysaccharide (LPS) contributes to the pathogenesis of septic shock. LPS is known to interact with several cell-surface proteins, including CD14, when presented as a complex with serum LPS-binding protein. However, the identity of the receptor responsible for LPS signalling and leucocyte activation is unknown. Interestingly, mice deficient in cell-surface L-selectin were dramatically resistant to the lethal effects of high doses of LPS in a model of septic shock. Recently we reported that L-selectin binds to cardiolipin and other charged

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Cowan, Douglas B., Dimitrios N. Poutias, Pedro J. Del Nido, and Francis X. McGowan. "CD14-independent activation of cardiomyocyte signal transduction by bacterial endotoxin." American Journal of Physiology-Heart and Circulatory Physiology 279, no. 2 (2000): H619—H629. http://dx.doi.org/10.1152/ajpheart.2000.279.2.h619.

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In the heart, lipopolysaccharide (LPS) induces the production of proinflammatory cytokines that cause myocardial dysfunction; however, the signaling pathways involved in cardiomyocyte responses are poorly understood. We studied LPS-induced signaling by treating cardiomyocyte cultures with 0.01–10 μg/ml LPS for 0–24 h in the presence or absence of 2.5% serum. Cytosolic and nuclear proteins were analyzed for expression and activation of protein kinases. Members of the extracellular signal-regulated kinase (ERK) and signal transducer and activators of transcription (STAT) protein families were un

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Gutsmann, Thomas, Iosu Razquin-Olazarán, Ina Kowalski, et al. "New Antiseptic Peptides To Protect against Endotoxin-Mediated Shock." Antimicrobial Agents and Chemotherapy 54, no. 9 (2010): 3817–24. http://dx.doi.org/10.1128/aac.00534-10.

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ABSTRACT Systemic bacterial infections are associated with high mortality. The access of bacteria or constituents thereof to systemic circulation induces the massive release of immunomodulatory mediators, ultimately causing tissue hypoperfusion and multiple-organ failure despite adequate antibiotic treatment. Lipid A, the “endotoxic principle” of bacterial lipopolysaccharide (LPS), is one of the major bacterial immunostimuli. Here we demonstrate the biological efficacy of rationally designed new synthetic antilipopolysaccharide peptides (SALPs) based on the Limulus anti-LPS factor for systemic

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Phillips, JD, DV Kinikini, Y. Yu, B. Guo, and EA Leibold. "Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells." Blood 87, no. 7 (1996): 2983–92. http://dx.doi.org/10.1182/blood.v87.7.2983.bloodjournal8772983.

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Iron-regulatory proteins (IRP1 and IRP2) are RNA-binding proteins that bind to stem-loop structures known as iron-responsive elements (IREs). IREs are located in the 5′- or 3′-untranslated regions (UTRs) of specific mRNAs that encode proteins involved in iron homeostasis. The binding of IRPs to 5′ IREs represses translation of the mRNA, whereas the binding of IRPs to 3′ IREs stabilizes the mRNA. IRP1 and IRP2 binding activities are regulated by intracellular iron levels. In addition, nitric oxide (NO.) increases the affinity of IRP1 for IREs. The role of NO. in the regulation of IRP1 and IRP2

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Tsai, Eunice Y., James V. Falvo, Alla V. Tsytsykova, et al. "A Lipopolysaccharide-Specific Enhancer Complex Involving Ets, Elk-1, Sp1, and CREB Binding Protein and p300 Is Recruited to the Tumor Necrosis Factor Alpha Promoter In Vivo." Molecular and Cellular Biology 20, no. 16 (2000): 6084–94. http://dx.doi.org/10.1128/mcb.20.16.6084-6094.2000.

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ABSTRACT The tumor necrosis factor alpha (TNF-α) gene is rapidly activated by lipopolysaccharide (LPS). Here, we show that extracellular signal-regulated kinase (ERK) kinase activity but not calcineurin phosphatase activity is required for LPS-stimulated TNF-α gene expression. In LPS-stimulated macrophages, the ERK substrates Ets and Elk-1 bind to the TNF-α promoter in vivo. Strikingly, Ets and Elk-1 bind to two TNF-α nuclear factor of activated T cells (NFAT)-binding sites, which are required for calcineurin and NFAT-dependent TNF-α gene expression in lymphocytes. The transcription factors AT

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delaTorre, Andrew, Rebecca A. Schroeder, Cecile Punzalan та Paul C. Kuo. "Endotoxin-Mediated S-Nitrosylation of p50 Alters NF-κB-Dependent Gene Transcription in ANA-1 Murine Macrophages". Journal of Immunology 162, № 7 (1999): 4101–8. http://dx.doi.org/10.4049/jimmunol.162.7.4101.

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Abstract Nitric oxide (NO) regulates cellular function, in part, by S-nitrosylating active site thiol groups of proteins. Ex vivo S-nitrosylation of NF-κB p50 significantly decreases its capacity for DNA binding. To determine the cellular relevance of this observation, we utilized the ANA-l murine macrophage model of endotoxin (LPS)-mediated NO synthesis. In selected instances, the NO synthase inhibitor, l-arginine methyl ester (L-NAME; 100 μM), or the NO donor, S-nitroso-N-acetylcysteine (SNAC; 100 μM), was added. In contrast to that of LPS cells, nuclear extracts from LPS + L-NAME cells demo

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Bosshart, Herbert, and Michael Heinzelmann. "Arginine-Rich Cationic Polypeptides Amplify Lipopolysaccharide-Induced Monocyte Activation." Infection and Immunity 70, no. 12 (2002): 6904–10. http://dx.doi.org/10.1128/iai.70.12.6904-6910.2002.

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ABSTRACT The human neutrophil-derived cationic protein CAP37, also known as azurocidin or heparin-binding protein, enhances the lipopolysaccharide (LPS)-induced release of tumor necrosis factor alpha (TNF-α) in isolated human monocytes. We measured the release of the proinflammatory cytokine interleukin-8 (IL-8) in human whole blood and found that in addition to CAP37, other arginine-rich cationic polypeptides, such as the small structurally related protamines, enhance LPS-induced monocyte activation. As CAP37 and protamines share high levels of arginine content, we tested different synthetic

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Zhang, T., V. Kruys, G. Huez, and C. Gueydan. "AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors." Biochemical Society Transactions 30, no. 6 (2002): 952–58. http://dx.doi.org/10.1042/bst0300952.

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Tumour necrosis factor (TNF)-α mRNA contains an AU-rich element (ARE) in its 3′ untranslated region (3′UTR), which determines its half-life and translational efficiency. In unstimulated macrophages, TNF-α mRNA is repressed translationally, and becomes efficiently translated upon cell activation. Gel retardation experiments and screening of a macrophage cDNA expression library with the TNF-α ARE allowed the identification of TIA-1-related protein (TIAR), T-cell intracellular antigen-1 (TIA-1) and tristetraprolin (TTP) as TNF-α ARE-binding proteins. Whereas TIAR and TIA-1 bind the TNF-α ARE inde

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Chiba, Hirofumi, Hitomi Sano, Daisuke Iwaki, et al. "Rat Mannose-Binding Protein A Binds CD14." Infection and Immunity 69, no. 3 (2001): 1587–92. http://dx.doi.org/10.1128/iai.69.3.1587-1592.2001.

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ABSTRACT Lipopolysaccharide (LPS) has been known to induce inflammation by interacting with CD14, which serves as a receptor for LPS. Mannose-binding protein (MBP) belongs to the collectin subgroup of the C-type lectin superfamily, along with surfactant proteins SP-A and SP-D. We have recently demonstrated that SP-A modulates LPS-induced cellular responses by interaction with CD14 (H. Sano, H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki, J. Immunol. 163:387–395, 2000) and that SP-D also interacts with CD14 (H. Sano, H. Chiba, D. Iwaki, H. Sohma, D. R. Voelker, and Y. Kuroki, J. Bio

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