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Related Concept Videos

Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Gross Anatomy of the Lungs01:17

Gross Anatomy of the Lungs

The lungs are a pair of vital organs connected to the trachea via the left and right bronchi. The base of these organs meets the dome-shaped muscle known as the diaphragm. Encased by the pleurae, the lungs contact the mediastinum. The right lung is shorter yet wider, and has a larger volume than the left lung. The left lung has an indentation known as the cardiac notch. The superior region of the lungs is referred to as the apex, whereas the base is the lower region near the diaphragm. The...

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Related Experiment Video

Updated: May 12, 2026

The Utilization of Oropharyngeal Intratracheal PAMP Administration and Bronchoalveolar Lavage to Evaluate the Host Immune Response in Mice
12:27

The Utilization of Oropharyngeal Intratracheal PAMP Administration and Bronchoalveolar Lavage to Evaluate the Host Immune Response in Mice

Published on: April 2, 2014

Zonulin as prehaptoglobin2 regulates lung permeability and activates the complement system.

Daniel Rittirsch1, Michael A Flierl, Brian A Nadeau

  • 1Department of Pathology, University of Michigan, Ann Arbor, MI, USA. drittirsch@gmail.com

American Journal of Physiology. Lung Cellular and Molecular Physiology
|April 9, 2013
PubMed
Summary

Zonulin, a protein regulating cell junctions, exacerbates acute lung injury (ALI) by increasing permeability and complement activation. Blocking zonulin with an antagonist (AT-1001) or antibody significantly reduced ALI severity in mice.

Keywords:
C3aC5aacute lung injuryinflammationtight junctions

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Area of Science:

  • Pulmonary Medicine
  • Immunology
  • Cell Biology

Background:

  • Zonulin regulates tight junctions (TJ) in epithelial and endothelial cells, primarily studied in the gut.
  • Its role in other organs, like the lungs, and its specific involvement in acute lung injury (ALI) remain less understood.
  • Prehaptoglobin2 is identified as zonulin, linked to complement system-activating serine proteases.

Purpose of the Study:

  • To investigate the role of zonulin in the development of acute lung injury (ALI) in a mouse model.
  • To evaluate the therapeutic potential of a zonulin antagonist (AT-1001) and the effects of a zonulin agonist (AT-1002) on ALI.

Main Methods:

  • Induction of ALI in C57BL/6 male mice via intrapulmonary IgG immune complexes or bacterial lipopolysaccharide.
  • Administration of zonulin antagonist (AT-1001), agonist (AT-1002), or neutralizing antibody via intratracheal or intravenous routes.
  • Quantification of ALI severity by measuring albumin leak, neutrophil accumulation, and proinflammatory cytokines; assessment of TJ protein integrity via confocal microscopy.

Main Results:

  • Zonulin antagonist AT-1001 and neutralizing antibody dose-dependently attenuated ALI, reducing albumin leak, neutrophil infiltration, and cytokine levels.
  • Confocal microscopy revealed discontinuous and fragmented tight junction proteins in injured lungs.
  • The zonulin agonist AT-1002 worsened ALI, while zonulin induced complement component C3a and C5a generation in vitro and in vivo.

Conclusions:

  • Zonulin significantly contributes to the development of ALI by increasing vascular permeability, promoting neutrophil and cytokine buildup, and activating the complement system.
  • Targeting zonulin with antagonists like AT-1001 shows therapeutic promise for mitigating ALI.
  • Zonulin's pro-inflammatory and permeability-enhancing effects highlight its critical role in lung injury pathogenesis.