LBP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLBP, BPIFD2, lipopolysaccharide binding protein
External IDsOMIM: 151990 MGI: 1098776 HomoloGene: 3055 GeneCards: LBP
Orthologs
SpeciesHumanMouse
Entrez

3929

16803

Ensembl

ENSG00000129988

ENSMUSG00000016024

UniProt

P18428

Q61805

RefSeq (mRNA)

NM_004139

NM_008489

RefSeq (protein)

NP_004130

NP_032515

Location (UCSC)Chr 20: 38.35 – 38.38 MbChr 2: 158.15 – 158.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Lipopolysaccharide binding protein (LBP) is a protein that in humans is encoded by the LBP gene.[5][6]

LBP is a soluble acute-phase protein that binds to bacterial lipopolysaccharide (or LPS) to elicit immune responses by presenting the LPS to important cell surface pattern recognition receptors called CD14 and TLR4.[7]

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.[6]

Clinical significance

LPS exposure induces LBP production.[8] LBP is synthesized by the liver, adipose tissue, and intestinal cells.[8] Dietary glucose and saturated fats acutely increase plasma LBP.[8]

The proinflammatory activity of plasma LPS is increased by LBP, which is higher in obesity.[9]

Plasma LBP is used as a better biomarker of plasma LPS than LPS itself due to the short half-life of LPS.[8]

Interactions

Lipopolysaccharide-binding protein has been shown to interact with CD14, TLR2, TLR4 and the co-receptor MD-2.[10][11][12]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129988 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016024 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gray PW, Corcorran AE, Eddy RL Jr, Byers MG, Shows TB (March 1993). "The genes for the lipopolysaccharide binding protein (LBP) and the bactericidal permeability increasing protein (BPI) are encoded in the same region of human chromosome 20". Genomics. 15 (1): 188–90. doi:10.1006/geno.1993.1030. PMID 8432532.
  6. ^ a b "Entrez Gene: LBP lipopolysaccharide binding protein".
  7. ^ Muta T, Takeshige K (2001). "Essential roles of CD14 and lipopolysaccharide-binding protein for activation of toll-like receptor (TLR)2 as well as TLR4 Reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations". Eur. J. Biochem. 268 (16): 4580–9. doi:10.1046/j.1432-1327.2001.02385.x. PMID 11502220.
  8. ^ a b c d Djuric Z (2017). "Obesity-associated cancer risk: the role of intestinal microbiota in the etiology of the host proinflammatory state". Translational Research. 179: 155–167. doi:10.1016/j.trsl.2016.07.017. PMC 5164980. PMID 27522986.
  9. ^ Tuomi K, Logomarsino JV (2016). "Bacterial Lipopolysaccharide, Lipopolysaccharide-Binding Protein, and Other Inflammatory Markers in Obesity and After Bariatric Surgery". Metabolic Syndrome and Related Disorders. 14 (6): 279–288. doi:10.1089/met.2015.0170. PMID 27228236.
  10. ^ Thomas CJ, Kapoor Mili, Sharma Shilpi, Bausinger Huguette, Zyilan Umit, Lipsker Dan, Hanau Daniel, Surolia Avadhesha (November 2002). "Evidence of a trimolecular complex involving LPS, LPS binding protein and soluble CD14 as an effector of LPS response". FEBS Lett. 531 (2): 184–8. doi:10.1016/S0014-5793(02)03499-3. ISSN 0014-5793. PMID 12417309. S2CID 25135963.
  11. ^ Yu B, Wright S D (1995). "LPS-dependent interaction of Mac-2-binding protein with immobilized CD14". J. Inflamm. 45 (2): 115–25. ISSN 1078-7852. PMID 7583357.
  12. ^ Erridge C, Pridmore A, Eley A, Stewart J, Poxton IR (2004). "Lipopolysaccharides of Bacteroides fragilis, Chlamydia trachomatis and Pseudomonas aeruginosa signal via toll-like receptor 2". Journal of Medical Microbiology. 53 (Pt 8): 735–40. doi:10.1099/jmm.0.45598-0. PMID 15272059.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


Signaling pathway: TLR signaling pathway
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