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Related Concept Videos

Integrins01:10

Integrins

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Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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Activation of Integrins01:15

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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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Related Experiment Video

Updated: Jul 5, 2025

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of &#946;2 Integrin Activation
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Endoplasmic Reticulum Protein 72 Regulates Integrin Mac-1 Activity to Influence Neutrophil Recruitment.

Yaofeng Li1, Xulin Xu1,2, Haoqing Jerry Wang3,4

  • 1Department of Pharmacology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases (Y.L., X.X., L.L., L.W., C.F.), Huazhong University of Science and Technology, Wuhan, Hubei, China.

Arteriosclerosis, Thrombosis, and Vascular Biology
|January 11, 2024
PubMed
Summary
This summary is machine-generated.

Endoplasmic reticulum-resident protein 72 (ERp72) regulates neutrophil integrin Mac-1 activation by catalyzing disulfide rearrangement. This finding suggests ERp72 as a potential therapeutic target for neutrophil-associated vasculopathy.

Keywords:
ERp72disulfidesisomerasesmacrophage-1 antigenmicroscopyneutrophil infiltrationneutrophils

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Integrins are crucial for neutrophil adhesion and migration during vascular inflammation.
  • Thiol exchange mechanisms regulate integrin function.
  • The role of ERp72, a thiol isomerase, in Mac-1 regulation on neutrophils was unclear.

Purpose of the Study:

  • To investigate the role of ERp72 in regulating the function of Mac-1 (integrin αMβ2) on neutrophils.
  • To elucidate the molecular mechanisms by which ERp72 influences Mac-1 activity.
  • To assess the therapeutic potential of ERp72 in neutrophil-associated vasculopathy.

Main Methods:

  • Intravital microscopy for in vivo neutrophil behavior.
  • Flow cytometry and static adhesion assays for in vitro integrin function.
  • Confocal microscopy, co-immunoprecipitation, and mass spectrometry to analyze ERp72-Mac-1 interactions and disulfide bonds.
  • Biomembrane force probe to measure Mac-1 binding affinity.
  • Murine model of acute lung injury to evaluate ERp72's role in vivo.

Main Results:

  • ERp72-deficient neutrophils showed impaired Mac-1 activation, leading to reduced adhesion and crawling.
  • ERp72 directly interacts with Mac-1 on the neutrophil surface, catalyzing disulfide bond reduction in the αM subunit.
  • Recombinant ERp72 enhanced Mac-1 binding affinity and rescued adhesion defects.
  • Deletion of ERp72 ameliorated lung injury and improved survival in a murine model.

Conclusions:

  • Extracellular ERp72 is a key regulator of Mac-1 integrin activity through disulfide rearrangement.
  • ERp72 represents a novel therapeutic target for treating neutrophil-associated vasculopathy.