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Related Concept Videos

Inflammatory Response01:28

Inflammatory Response

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An inflammatory response is a localized, nonspecific immune reaction that occurs when a tissue is injured. It is characterized by redness, swelling, heat, and pain, which are commonly called the cardinal signs and symptoms of inflammation. Inflammation can sometimes result in a loss of function.
Inflammation can be triggered by various stimuli, such as impact, abrasion, chemical irritation, infections, and extreme hot or cold temperatures. These can damage cells and connective tissue fibers,...
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Inflammatory Response II: Inflammatory Exudate and Tissue Repair01:24

Inflammatory Response II: Inflammatory Exudate and Tissue Repair

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The immune system's inflammatory response destroys the invading pathogen, permitting the tissue to heal. The changes during the cellular and vascular stages allow exudate formation at the site of inflammation. The inflammatory exudate released from the wound has high protein content and a specific gravity above 1.020.
The typical wound exudate is odorless, transparent, straw-colored, thin, and watery. Exudate, however, can differ depending on the state of wound healing. Likewise, the...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
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Inflammatory Response I: Vascular and Cellular01:30

Inflammatory Response I: Vascular and Cellular

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The inflammatory response is the body's defense against infection, injury, or irritation from bacteria, trauma, toxins, or heat. Inflammation helps locate and destroy pathogens and remove damaged tissue elements to heal the body. During this initial phase, fluid, blood products, and nutrients migrate to the injured area, resulting in redness, heat, swelling, ache, and loss of function. Moreover, signs of systemic inflammation include fever, increased WBC count, malaise, anorexia, nausea,...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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Legionella pneumophila Outer Membrane Vesicles: Isolation and Analysis of Their Pro-inflammatory Potential on Macrophages
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Legionella pneumophila Outer Membrane Vesicles: Isolation and Analysis of Their Pro-inflammatory Potential on Macrophages

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LPS-neutralizing peptides reduce outer membrane vesicle-induced inflammatory responses.

Anja Pfalzgraff1, Wilmar Correa2, Lena Heinbockel3

  • 1Institute of Pharmacy (Pharmacology and Toxicology), Freie Universität Berlin, Berlin, Germany.

Biochimica Et Biophysica Acta. Molecular and Cell Biology of Lipids
|June 5, 2019
PubMed
Summary

Synthetic peptide Pep19-2.5 effectively neutralizes inflammation caused by bacterial outer membrane vesicles (OMVs) and their released lipopolysaccharide (LPS) in immune cells, inhibiting pyroptosis and IL-1β release.

Keywords:
Cytoplasmic lipopolysaccharideInterleukin-1betaOuter membrane vesiclesP2X7 receptorPyroptosisSynthetic anti-endotoxin peptides

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Increased Recovery Time and Decreased LPS Administration to Study the Vagus Nerve Stimulation Mechanisms in Limited Inflammatory Responses
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Area of Science:

  • Immunology and Microbiology
  • Bacterial Pathogenesis
  • Drug Discovery

Background:

  • Gram-negative bacteria secrete outer membrane vesicles (OMVs) that trigger potent inflammatory responses.
  • Intracellular lipopolysaccharide (LPS) released from OMVs activates inflammasomes, leading to pyroptosis and sepsis.
  • Synthetic peptide Pep19-2.5 has previously shown potential in neutralizing LPS-induced inflammation.

Purpose of the Study:

  • To investigate the efficacy of Pep19-2.5 in suppressing OMV-induced cytoplasmic LPS inflammation under physiological conditions.
  • To elucidate the mechanisms underlying Pep19-2.5's anti-inflammatory action in macrophages and monocytes.

Main Methods:

  • Isothermal titration calorimetry and Limulus Amebocyte Lysate assay to assess OMV-Pep19-2.5 interaction and endotoxin blocking.
  • In vitro studies using THP-1 and primary human macrophages/monocytes to measure cytokine release (IL-1β, TNF) and pyroptosis.
  • Assessment of Pep19-2.5 internalization via the P2X7 receptor and evaluation of cell-type specific neutralization efficiency.

Main Results:

  • Pep19-2.5 demonstrated exothermic binding with E. coli OMVs and strong endotoxin neutralization.
  • Pep19-2.5 and polymyxin B reduced OMV-induced IL-1β, TNF release, and pyroptosis in macrophages.
  • TAK-242 inhibited OMV-induced TNF and IL-1β but not pyroptosis; Pep19-2.5 internalization was P2X7 receptor-dependent in macrophages.

Conclusions:

  • LPS-neutralizing peptides like Pep19-2.5 inhibit OMV-induced inflammasome activation and IL-1 axis signaling.
  • Pep19-2.5's mechanism involves P2X7 receptor-mediated internalization and cell-type specific neutralization of cytoplasmic LPS.
  • Findings offer insights into peptide-based strategies for treating sepsis and other inflammatory conditions driven by bacterial OMVs.