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Lbp  -  lipopolysaccharide binding protein

Mus musculus

Synonyms: Bpifd2, LBP, Lipopolysaccharide-binding protein, Ly88
 
 
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Disease relevance of Lbp

 

Psychiatry related information on Lbp

  • RESULTS: Decreased levels of serum AGE, hydroxyproline concentration in mouse skin and spontaneous motor activity in D-galactose mouse aging model were detected after treated with ABP or LBP, while lymphocyte proliferation and IL-2 activity, learning and memory abilities, SOD activity of erythrocytes, were enhanced [4].
 

High impact information on Lbp

  • Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection [5].
  • We propose the iterative anionic groups along the glycan backbone of the cell wall are a crucial structure for recognition by LBP [6].
  • LBP was present in the CSF of patients with meningitis, and LBP-deficient mice failed to develop meningeal inflammation [6].
  • Despite these striking in vitro findings, no significant differences in TNF-alpha levels were observed in plasma from wild-type and LBP-deficient mice injected with LPS [7].
  • The role of LBP in promoting LPS responsiveness in vivo was tested in LBP-deficient mice produced by gene targeting in embryonic stem cells [7].
 

Chemical compound and disease context of Lbp

 

Biological context of Lbp

 

Anatomical context of Lbp

  • In the presence of LBP, 1/1,000 the concentration of LPS is sufficient to activate peripheral blood monocytes [1].
  • Previous studies with Kupffer cells have shown a variable effect of serum on LPS activation of these cells and led to the conclusion that, unlike extrahepatic mononuclear cells, Kupffer cells do not respond to LPS in an LBP-dependent fashion [1].
  • Polymorphonuclear leukocytes (PMN) and LPS-binding protein (LBP) are both components of the innate immune system [2].
  • Here, we report that LBP also plays an essential role in the innate immune response to Gram-positive pneumococci, specifically to their major inflammatory component, pneumococcal cell wall (PCW) [6].
  • LBP(-/-) mice were highly susceptible to E. coli peritonitis, as indicated by accelerated mortality, earlier bacterial dissemination to the blood, impaired bacterial clearance in the peritoneal cavity, and more severe remote organ damage [15].
 

Associations of Lbp with chemical compounds

 

Regulatory relationships of Lbp

  • The relative ability of different cationic peptides to block the binding of LPS to LBP correlated with their ability to block LPS-induced TNF-alpha production by the RAW 264.7 macrophage cell line [18].
 

Other interactions of Lbp

 

Analytical, diagnostic and therapeutic context of Lbp

References

  1. Kupffer cell activation by lipopolysaccharide in rats: role for lipopolysaccharide binding protein and toll-like receptor 4. Su, G.L., Klein, R.D., Aminlari, A., Zhang, H.Y., Steinstraesser, L., Alarcon, W.H., Remick, D.G., Wang, S.C. Hepatology (2000) [Pubmed]
  2. The role of lipopolysaccharide binding protein in resistance to Salmonella infections in mice. Fierer, J., Swancutt, M.A., Heumann, D., Golenbock, D. J. Immunol. (2002) [Pubmed]
  3. Roles of endotoxin-related signaling molecules in the progression of acute necrotizing pancreatitis in mice. Wang, X., Wu, L., Wu, K., Zhang, R., Dong, Y. Pancreas (2005) [Pubmed]
  4. Inhibiting effects of Achyranthes bidentata polysaccharide and Lycium barbarum polysaccharide on nonenzyme glycation in D-galactose induced mouse aging model. Deng, H.B., Cui, D.P., Jiang, J.M., Feng, Y.C., Cai, N.S., Li, D.D. Biomed. Environ. Sci. (2003) [Pubmed]
  5. Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection. Jack, R.S., Fan, X., Bernheiden, M., Rune, G., Ehlers, M., Weber, A., Kirsch, G., Mentel, R., Fürll, B., Freudenberg, M., Schmitz, G., Stelter, F., Schütt, C. Nature (1997) [Pubmed]
  6. Recognition of pneumococcal peptidoglycan: an expanded, pivotal role for LPS binding protein. Weber, J.R., Freyer, D., Alexander, C., Schröder, N.W., Reiss, A., Küster, C., Pfeil, D., Tuomanen, E.I., Schumann, R.R. Immunity (2003) [Pubmed]
  7. Targeted deletion of the lipopolysaccharide (LPS)-binding protein gene leads to profound suppression of LPS responses ex vivo, whereas in vivo responses remain intact. Wurfel, M.M., Monks, B.G., Ingalls, R.R., Dedrick, R.L., Delude, R., Zhou, D., Lamping, N., Schumann, R.R., Thieringer, R., Fenton, M.J., Wright, S.D., Golenbock, D. J. Exp. Med. (1997) [Pubmed]
  8. Role of lipopolysaccharide-binding protein in early alcohol-induced liver injury in mice. Uesugi, T., Froh, M., Arteel, G.E., Bradford, B.U., Wheeler, M.D., Gäbele, E., Isayama, F., Thurman, R.G. J. Immunol. (2002) [Pubmed]
  9. Lipopolysaccharide-binding protein modulates acetaminophen-induced liver injury in mice. Su, G.L., Gong, K.Q., Fan, M.H., Kelley, W.M., Hsieh, J., Sun, J.M., Hemmila, M.R., Arbabi, S., Remick, D.G., Wang, S.C. Hepatology (2005) [Pubmed]
  10. Lipopolysaccharide binding protein potentiates airway reactivity in a murine model of allergic asthma. Strohmeier, G.R., Walsh, J.H., Klings, E.S., Farber, H.W., Cruikshank, W.W., Center, D.M., Fenton, M.J. J. Immunol. (2001) [Pubmed]
  11. LPS signaling enhances hepatic fibrogenesis caused by experimental cholestasis in mice. Isayama, F., Hines, I.N., Kremer, M., Milton, R.J., Byrd, C.L., Perry, A.W., McKim, S.E., Parsons, C., Rippe, R.A., Wheeler, M.D. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  12. Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis. Pethe, K., Bifani, P., Drobecq, H., Sergheraert, C., Debrie, A.S., Locht, C., Menozzi, F.D. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  13. Neutrophil influx in response to a peritoneal infection with Salmonella is delayed in lipopolysaccharide-binding protein or CD14-deficient mice. Yang, K.K., Dorner, B.G., Merkel, U., Ryffel, B., Schütt, C., Golenbock, D., Freeman, M.W., Jack, R.S. J. Immunol. (2002) [Pubmed]
  14. Critical role of lipopolysaccharide-binding protein and CD14 in immune responses against gram-negative bacteria. Le Roy, D., Di Padova, F., Adachi, Y., Glauser, M.P., Calandra, T., Heumann, D. J. Immunol. (2001) [Pubmed]
  15. Lipopolysaccharide binding protein is an essential component of the innate immune response to Escherichia coli peritonitis in mice. Knapp, S., de Vos, A.F., Florquin, S., Golenbock, D.T., van der Poll, T. Infect. Immun. (2003) [Pubmed]
  16. Isolation, partial characterization, and concentration in experimental sepsis of baboon lipopolysaccharide-binding protein. Haudek, S.B., Natmessnig, B.E., Redl, H., Schlag, G., Hatlen, L.E., Tobias, P.S. J. Lab. Clin. Med. (2000) [Pubmed]
  17. Protective effect of paeoniflorin on immunological liver injury induced by bacillus Calmette-Guerin plus lipopolysaccharide: modulation of tumour necrosis factor-alpha and interleukin-6 MRNA. Liu, D.F., Wei, W., Song, L.H. Clin. Exp. Pharmacol. Physiol. (2006) [Pubmed]
  18. Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein. Scott, M.G., Vreugdenhil, A.C., Buurman, W.A., Hancock, R.E., Gold, M.R. J. Immunol. (2000) [Pubmed]
  19. Upregulation of TNF-alpha and IL-6 mRNA in mouse liver induced by bacille Calmette-Guerin plus lipopolysaccharide. Liu, D.F., Wei, W., Song, L.H. Acta Pharmacol. Sin. (2006) [Pubmed]
  20. The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. Qureshi, N., Perera, P.Y., Shen, J., Zhang, G., Lenschat, A., Splitter, G., Morrison, D.C., Vogel, S.N. J. Immunol. (2003) [Pubmed]
  21. Lipopolysaccharide-binding protein modulates hepatic damage and the inflammatory response after hemorrhagic shock and resuscitation. Lehnert, M., Uehara, T., Bradford, B.U., Lind, H., Zhong, Z., Brenner, D.A., Marzi, I., Lemasters, J.J. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  22. The laminin binding protein p40 is involved in inducing limb abnormality of mouse fetuses as the effects of methoxyacetic acid treatment. Ruyani, A., Sudarwati, S., Sutasurya, L.A., Sumarsono, S.H., Gloe, T. Toxicol. Sci. (2003) [Pubmed]
 
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