Disease relevance of Lbp

• A chimeric protein consisting of the N-terminal domain of lipopolysaccharide-binding protein and the C-terminal domain of bactericidal/permeability-increasing protein demonstrated a dose-dependent survival benefit (P = 0.001) and reduced endotoxin levels (P < 0.01) in neutropenic rats with Pseudomonas aeruginosa sepsis [1].
• BACKGROUND: It is suggested that endotoxin, proinflammatory cytokines, and lipopolysaccharide-binding protein (LBP) play an important role in the development of alcoholic liver disease [2].
• Effect of hemorrhagic shock on endotoxin-inducing TNF production and intra-tissue lipopolysaccharide-binding protein mRNA expression and their relationship [3].
• Induction of hepatocyte lipopolysaccharide binding protein in models of sepsis and the acute-phase response [4].
• To determine the conditions that stimulate LBP production in vivo, we measured the induction of LBP in models of inflammation produced by LPS, Corynebacterium parvum, and turpentine injection [4].

Psychiatry related information on Lbp

• In the Wis/LBP rats, moreover, the hippocampal AVP content decreased during selection (r = -0.645, P less than 0.01), while the acquisition response latency increased (r = 0.549, P less than 0.01) [5].

High impact information on Lbp

• The data presented here support the concept that the 60-kD glycoprotein we have termed LBP is a newly recognized acute phase reactant that may modulate the biochemical and biologic properties of LPS in vivo [6].
• These results suggest that the tolerance observed despite sustained hepatic expression of proinflammatory cytokines is counteracted by the anti-inflammatory cytokines and by down-regulation of CD14 and LBP [7].
• Close to 70% of the hepatocytes attach to LBP after 15 minutes of incubation at 37 degrees C. Cell adhesion was Mg++ and Mn(++)-dependent and Ca(++)- and insulin-independent [8].
• Therefore, we compared the adhesion of hepatocytes to laminin 1 and a matrix extracted with dilute acetic acid from liver biomatrix (LBP) [8].
• In 12 human colon cell lines, the level of LBP mRNA was higher in poorly differentiated cells [9].

Chemical compound and disease context of Lbp

• To determine the pathophysiological roles of macrophages in alcoholic liver disease, we examined the effect of ethanol on TNF-alpha secretion of rat Kupffer cells, alveolar macrophages, and peritoneal macrophages in the presence or absence of LBP [10].
• The effects of polysaccharide extracted from Lycium barbarum (LBP) on blood glucose, oxidative stress and DNA damage in rats with non-insulin dependent diabetes mellitus (NIDDM) were studied [11].

Biological context of Lbp

• LPS binding protein (LBP) is a glycoprotein present in normal serum that becomes markedly elevated during acute phase responses [12].
• Molecular cloning, characterization, and tissue distribution of rat lipopolysaccharide binding protein. Evidence for extrahepatic expression [12].
• The deduced amino acid sequence of rat LBP was highly homologous with that reported for rabbit and human LBP [12].
• While the expression of S19 and LBP mRNAs was not changed due to cell growth states, HLA-I mRNA levels were found to be low in proliferating HT29 cells but highly induced in contact-inhibited cells [9].
• These findings indicate that LBP and sCD14 will rapidly transfer LPS to certain membranes based on the kinetics of the movement of LPS into these membranes [13].

Anatomical context of Lbp

• Normal rat hepatic stellate cells respond to endotoxin in LBP-independent manner to produce inhibitor(s) of DNA synthesis in hepatocytes [14].
• Products of lipopolysaccharide-activated macrophages (tumor necrosis factor-alpha, transforming growth factor-beta) but not lipopolysaccharide modify DNA synthesis by rat trophoblast cells exhibiting the 80-kDa lipopolysaccharide-binding protein [15].
• Our observation that LBP and sCD14 can transport LPS into phospholipid bilayers suggests that LBP and membrane CD14 may transport LPS into the phospholipid bilayer of cells such as monocytes and neutrophils [13].
• Role of alveolar macrophages in innate immunity in neonates: evidence for selective lipopolysaccharide binding protein production by rat neonatal alveolar macrophages [16].
• We have also demonstrated an LPS inducible expression of messenger RNA for LPS binding protein (LBP) in neonatal AM that was not observed in AM from adult animals or in peritoneal macrophages [16].

Associations of Lbp with chemical compounds

• Surfactant protein a inhibits lipopolysaccharide-induced immune cell activation by preventing the interaction of lipopolysaccharide with lipopolysaccharide-binding protein [17].
• We show that synthetic cell-adhesion peptide sequences present in laminin 1 (RGD and YIGSR) or an antibody to the cell-binding domain (SIKVAV) of the alpha 1 chain do not prevent hepatocyte adhesion to LBP [8].
• 3) Inclusion of sCD14 is absolutely necessary to observe LBP-dependent neutralization of LPS by sphingomyelin, globoside, and phosphatidylserine [13].
• Ethanol significantly increased the mRNA expression of the endotoxin (LPS) receptor CD14 and the LPS binding protein LBP, but not that of the pro-inflammatory cytokines TNF-alpha and IL-1beta [18].
• Neonatal capsaicin-treatment, a procedure that selectively destroys a subpopulation of DRG neurons with fine unmyelinated axons, had no effect on the reduction of 110/140 LBP in the DRG induced by sciatic nerve constriction [19].

Other interactions of Lbp

• Induction of lipopolysaccharide-binding protein gene expression in cultured rat pulmonary artery smooth muscle cells by interleukin 1 beta [20].
• Tissue lipopolysaccharide-binding protein expression in rats after thermal injury: potential role of TNF-alpha [21].

Analytical, diagnostic and therapeutic context of Lbp

• Binding competition experiments employing a surface plasmon resonance technique showed that Re-LPS preincubated with SP-A bound to LBP to a significantly lesser extent than Re-LPS alone [17].
• Use of the rat LBP cDNA clone for Northern blot analysis reveals that LBP mRNA levels are markedly up-regulated in liver during acute phase responses [12].
• The direct interaction of LPS and LBP was inferred from two types of evidence: first, immunoprecipitation of [3H]LPS from APRS by anti-LBP sera; and second, by the 125I-labeling of LBP when APRS-containing 125I-labeled 2-(p-azidosalicylamido)ethyl 1,3'-dithiopropionyl-LPS was photolysed [6].
• Northern blot analysis for CD14, LBP, and TLR2 mRNA, immunohistochemistry for LBP, liver enzyme analysis, and gel shift assay for NF-kappaB and AP-1 were performed [22].
• LBP mRNA and protein and CD14 mRNA were significantly up-regulated peaking at 6 to 12 hr after reperfusion [22].

References