Relative concentrations of endotoxin-binding proteins in body fluids during infection

Opal, Steven M.; Palardy, John E.; Marra, Marian N.; McKelligon, B.M; Scott, Randy W.; Fisher, Charles J.

doi:10.1016/s0140-6736(94)91767-1

Cited by 86 publications

(51 citation statements)

References 20 publications

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“…2D). The ability of BPI to promote OM bleb-MDDC interaction in the presence of 20% serum suggests that a similar capacity for BPI may be possible at tissue sites of infection and inflammation where potentially competing endotoxin-binding proteins such as LBP will also be present (30,33,39,40). This potential likely reflects the very high affinity binding properties of BPI toward the Gram-negative bacterial OM that distinguishes it from LBP and other known host endotoxinbinding proteins (41)(42)(43).…”

Section: Discussionmentioning

confidence: 99%

“…However, when BPI is mobilized following Gram-negative bacteria invasion of tissue, other endotoxin-interactive proteins, including LBP and soluble CD14, also accumulate and so potentially compete with BPI for interaction with the cell-free endotoxin-rich particles. We tested the effects of 20% serum to roughly approximate levels of plasma proteins transudated to tissue during local inflammatory responses (33). Under these experimental conditions, the stimulatory effects of BPI on association of LOS aggregates and OM blebs to MDDC were blunted at low (Յ1 nM) BPI concentrations.…”

Section: Bpi Increases the Delivery Of N Meningitidis Serogroup B Lomentioning

confidence: 99%

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A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

Schultz

Hume

Zhang

et al. 2007

The Journal of Immunology

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The bactericidal/permeability-increasing protein (BPI) is thought to play an important role in killing and clearance of Gram-negative bacteria and the neutralization of endotoxin. A possible role for BPI in clearance of cell-free endotoxin has also been suggested based on studies with purified endotoxin aggregates and blood monocytes. Because the interaction of BPI with cell-free endotoxin, during infection, occurs mainly in tissue and most likely in the form of shed bacterial outer membrane vesicles (“blebs”), we examined the effect of BPI on interactions of metabolically labeled ([14C]-acetate) blebs purified from Neisseria meningitidis serogroup B with either human monocyte-derived macrophages or monocyte-derived dendritic cells (MDDC). BPI produced a dose-dependent increase (up to 3-fold) in delivery of 14C-labeled blebs to MDDC, but not to monocyte-derived macrophages in the presence or absence of serum. Both, fluorescently labeled blebs and BPI were internalized by MDDC under these conditions. The closely related LPS-binding protein, in contrast to BPI, did not increase association of the blebs with MDDC. BPI-enhanced delivery of the blebs to MDDC did not increase cell activation but permitted CD14-dependent signaling by the blebs as measured by changes in MDDC morphology, surface expression of CD80, CD83, CD86, and MHC class II and secretion of IL-8, RANTES, and IP-10. These findings suggest a novel role of BPI in the interaction of bacterial outer membrane vesicles with dendritic cells that may help link innate immune recognition of endotoxin to Ag delivery and presentation.

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Section: Discussionmentioning

confidence: 99%

Section: Bpi Increases the Delivery Of N Meningitidis Serogroup B Lomentioning

confidence: 99%

A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

Schultz

Hume

Zhang

et al. 2007

The Journal of Immunology

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“…However, in the case of cerebrospinal fluid (52), i.p. fluid (53), synovial fluid (54), or mucous membrane surfaces (55), it is still unknown whether or not increased concentrations of LBP may be involved in the inflammatory reactions or immune memory.…”

Section: Discussionmentioning

confidence: 99%

Lipopolysaccharide-Binding Protein Critically Regulates Lipopolysaccharide-Induced IFN-β Signaling Pathway in Human Monocytes

Kato

Ogasawara

Homma

et al. 2004

The Journal of Immunology

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LPS binding to Toll-like receptor 4 induces a large number of genes through activation of NF-κB and IFN-regulatory factor-3 (IRF-3). However, no previous reports have tested the role of serum proteins in LPS-induced gene expression profiles. To investigate how serum proteins affect LPS-induced signaling, we investigated LPS-inducible genes in PBMC using an oligonucleotide probe-array system. Approximately 120 genes up-regulated by LPS were hierarchically divided into two clusters. Induction of one cluster, containing only IFN-inducible genes, was serum dependent. Real-time PCR analysis confirmed that IFN-inducible genes were induced only in the presence of serum, whereas inflammatory genes were induced both in the presence and absence of serum. Further analysis demonstrated that addition of LPS-binding protein (LBP), but not of soluble CD14 to the serum-free medium enabled the induction of IFN-inducible genes and IFN-β itself by LPS in human monocytes. The mRNAs for IFN-β and IFN-inducible genes were induced by LPS only in the presence of serum from LBP+/+ mice, and not in the presence of serum from LBP−/− mice. Blocking experiments also confirmed the involvement of LBP in this phenomenon. Immunoblotting analysis showed that phosphorylation of c-Jun N-terminal kinase, p38, IRF-3, tyrosine kinase 2, and STAT1 by LPS, but not of NF-κB and extracellular signal-regulated kinase was abrogated in the absence of LBP. This critical role for LBP implies the presence of possible mechanisms linking LBP to the intracellular signaling between Toll-like receptor 4 and IRF-3, leading to the induction of IFN-β by LPS.

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“…The activation of host cells by endotoxin requires the extraction and transfer of individual endotoxin molecules to a host cell surface receptor complex containing MD-2 and Toll-like receptor (TLR) 4 [74][75][76]. This transfer does not occur directly but rather requires first the interaction of LBP with the endotoxin-rich GNB outer membrane and transfer of endotoxin monomers to either soluble or membrane-bound CD14.…”

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

“…These combined actions can take place both within neutrophils after uptake of the PLA2 and complement with bacteria during phagocytosis [97,98] and in the extracellular inflammatory fluid [40,86,[99][100][101]. Levels of BPI in cell-free inflammatory fluid of neutrophil-rich exudates are functionally significant (≥10 nM) and co-exist with other antimicrobial host factors that can act in concert with BPI [76,86,[100][101][102][103][104]. Thus, in cooperation with other cellular and humoral components of the innate immune system, BPI can contribute to killing of invading GNB.…”

Section: Bpi Actions During Host: Gnb Interactionsmentioning

confidence: 99%

The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

Schultz

Weiss

2007

Clinica Chimica Acta

111

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Gram-negative bacteria (GNB) and their endotoxin present a constant environmental challenge. Endotoxins can potently signal mobilization of host defenses against invading GNB but also potentially induce severe pathophysiology, necessitating controlled initiation and resolution of endotoxin-induced inflammation to maintain host integrity. The bactericidal/permeability-increasing protein (BPI) is a pluripotent protein expressed, in humans, mainly neutrophils. BPI exhibits strong anti-microbial activity against GNB and potent endotoxin-neutralizing activity. BPI mobilized with neutrophils in response to invading GNB can promote intracellular and extracellular bacterial killing, endotoxin neutralization and clearance, and delivery of GNB outer membrane antigens to dendritic cells. Tissue expression by dermal fibroblasts and epithelia could further amplify local levels of BPI and local interaction with GNB and endotoxin, helping to constrain local tissue infection and inflammation and prevent systemic infection and systemic inflammation. This review article focuses on the structural and functional properties of BPI with respect to its contribution to host defense during GNB infections and endotoxin-induced inflammation and the genesis of auto-antibodies against BPI that can blunt BPI activity and potentially contribute to chronic inflammatory disease.

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Relative concentrations of endotoxin-binding proteins in body fluids during infection

Cited by 86 publications

References 20 publications

A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

Lipopolysaccharide-Binding Protein Critically Regulates Lipopolysaccharide-Induced IFN-β Signaling Pathway in Human Monocytes

The bactericidal/permeability-increasing protein (BPI) in infection and inflammatory disease

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