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Lipopolysaccharide binding protein

LPS-binding protein
The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). Finally, this gene is found on chromosome 20, immediately downstream of the BPI gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CD14, CAN, HAD, Interleukin-6, TLR4
Papers on LPS-binding protein
Inhibition of lipopolysaccharide induced acute inflammation in lung by chlorination.
New
Lu et al., Beijing, China. In J Hazard Mater, Mar 2016
To explore the possible mechanisms, the nuclear magnetic resonance (NMR) results showed the chlorination happened in alkyl chain of LPS molecules, which could affect the interaction between LPS and LPS-binding protein.
Disaggregation of lipopolysaccharide by albumin, hemoglobin, or high density lipoprotein, forming complexes that prime neutrophils for enhanced release of superoxide.
New
Nishimura et al., Fukuoka, Japan. In Pathog Dis, Feb 2016
LPS primed neutrophils for enhanced release of formyl peptide-stimulated superoxide, in a serum- and LPS binding protein (LBP)-dependent manner.
Identification of the zinc finger protein ZRANB2 as a novel maternal LPS-binding protein that protects embryos of zebrafish against Gram-negative bacterial infections.
New
Zhang et al., China. In J Biol Chem, Feb 2016
Here we clearly demonstrate that ZRANB2 is a newly-identified LPS-binding protein present abundantly in the eggs/embryos of zebrafish.
Endotoxin-neutralizing activity and mechanism of action of a cationic α-helical antimicrobial octadecapeptide derived from α-amylase of rice.
New
Tanaka et al., Niigata, Japan. In Peptides, Jan 2016
In addition, AmyI-1-18 could block the binding of LPS-binding protein to LPS, although its ability was less than that of polymyxin B. These results suggest that AmyI-1-18 expressing antimicrobial and endotoxin-neutralizing activities is useful as a safe and potent host defense peptide against pathogenic Gram-negative bacteria in many fields of healthcare.
Mammalian Lipopolysaccharide Receptors Incorporated into the Retroviral Envelope Augment Virus Transmission.
New
Golovkina et al., Chicago, United States. In Cell Host Microbe, Nov 2015
We find that the viral envelope contains the mammalian LPS-binding factors CD14, TLR4, and MD-2, which, in conjunction with LPS-binding protein (LBP), bind LPS to the virus and augment transmission.
Endotoxemia of metabolic syndrome: a pivotal mediator of meta-inflammation.
Review
Rajamani et al., Sacramento, United States. In Metab Syndr Relat Disord, 2014
Lipopolysaccharides (LPS), or endotoxins, bind to LPS-binding protein and activate pattern recognition receptors, classically Toll-like receptor-4, mediating inflammation.
Recognition of lipopolysaccharide pattern by TLR4 complexes.
Review
Lee et al., South Korea. In Exp Mol Med, 2012
The common structural pattern of LPS in diverse bacterial species is recognized by a cascade of LPS receptors and accessory proteins, LPS binding protein (LBP), CD14 and the Toll-like receptor4 (TLR4)-MD-2 complex.
Association of lipopolysaccharide-binding protein gene polymorphisms with cerebral infarction in a Chinese population.
GeneRIF
Xia et al., Changsha, China. In J Thromb Thrombolysis, 2012
Association of lipopolysaccharide-binding protein gene polymorphisms with cerebral infarction in a Chinese population
Plasma level of lipopolysaccharide-binding protein is indicative of acute graft-versus-host disease following allogeneic hematopoietic stem cell transplantation.
GeneRIF
Huang et al., Wenzhou, China. In Int J Hematol, 2012
our study demonstrated that an elevated LBP level of >15000 ng/ml may serve as a biomarker for the prediction and monitoring of aGVHD.
LBP and sCD14 patterns in total hip replacement surgery performed during combined spinal/epidural anaesthesia.
GeneRIF
Reikerås et al., Oslo, Norway. In Scand J Clin Lab Invest, 2011
Aseptic trauma primes the innate immune system for the posttraumatic release of lipopolysaccharide binding protein and sCD14
Soluble CD14 subtype presepsin (sCD14-ST) and lipopolysaccharide binding protein (LBP) in neonatal sepsis: new clinical and analytical perspectives for two old biomarkers.
GeneRIF
Fanos et al., Genova, Italy. In J Matern Fetal Neonatal Med, 2011
The availability of commercial methods for the automated measurement of the soluble CD14 subtype presepsin and lipopolysaccharide binding protein represent a challenge for the evaluation in clinical practice of reliable markers of neonatal sepsis.
Invertebrate immune diversity.
Review
Smith et al., Washington, D.C., United States. In Dev Comp Immunol, 2011
These include a Toll/TLR system, a primitive complement system, an LPS binding protein, and a RAG core/Transib element.
Dual host-defence functions of SPLUNC2/PSP and synthetic peptides derived from the protein.
Review
Sotsky et al., Minneapolis, United States. In Biochem Soc Trans, 2011
Based on the predicted structure of PSP/SPLUNC2 and the location of known antibacterial and anti-inflammatory peptides in BPI (bactericidal/permeability-increasing protein) and LBP (LPS-binding protein), we designed GL13NH2 and GL13K, synthetic peptides that capture these proposed functions of PSP/SPLUNC2.
Granulin is a soluble cofactor for toll-like receptor 9 signaling.
Impact
Ploegh et al., Seoul, South Korea. In Immunity, 2011
TLR4 uses LPS binding protein, MD-2, and CD14 as accessories to respond to LPS.
Lipopolysaccharide-binding protein for monitoring of postoperative sepsis: complemental to C-reactive protein or redundant?
GeneRIF
Braun et al., Erlangen, Germany. In Plos One, 2010
During the first 14 days of postoperative sepsis, LBP plasma concentrations showed a time course that was very similar to CRP with a high concordance in the pattern of day-to-day changes
Diet-induced bacterial immunogens in the gastrointestinal tract of dairy cows: impacts on immunity and metabolism.
Review
Zhang et al., Chongqing, China. In Acta Vet Scand, 2010
Immune responses are subsequently caused by circulating LPS, and the systemic effects include increases in concentrations of neutrophils and the acute phase proteins such as serum amyloid-A (SAA), haptoglobin (Hp), LPS binding protein (LBP), and C-reactive protein (CRP) in blood.
Recognition of pneumococcal peptidoglycan: an expanded, pivotal role for LPS binding protein.
Impact
GeneRIF
Schumann et al., Berlin, Germany. In Immunity, 2003
plays an essential role in the innate immune response to Gram-positive pneumococci
Protective role of phospholipid oxidation products in endotoxin-induced tissue damage.
Impact
Leitinger et al., Vienna, Austria. In Nature, 2002
Lipopolysaccharide (LPS), an outer-membrane component of Gram-negative bacteria, interacts with LPS-binding protein and CD14, which present LPS to toll-like receptor 4 (refs 1, 2), which activates inflammatory gene expression through nuclear factor kappa B (NF kappa B) and mitogen-activated protein-kinase signalling.
Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signalling.
Impact
Godowski et al., San Francisco, United States. In Nature, 1998
Sensitive responses of myeloid cells to LPS require a plasma protein called LPS-binding protein and the glycosylphosphatidylinositol-anchored membrane protein CD14.
Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin.
Review
Impact
Tobias et al., Los Angeles, United States. In Annu Rev Immunol, 1994
The discovery in 1986 of a plasma protein termed LPS binding protein (LBP) led to the discovery of unanticipated mechanisms of LPS-induced cell activation.
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