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Related Concept Videos

Integrins01:10

Integrins

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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...
Selectins01:25

Selectins

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, which...

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Overview: assays for studying integrin-dependent cell adhesion.

Alexandre Chigaev1, Larry A Sklar

  • 1Department of Pathology and Cancer Center, University of New Mexico Health Sciences Center, Albuquerque, NM, USA. achigaev@salud.unm.edu

Methods in Molecular Biology (Clifton, N.J.)
|September 13, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces real-time methods to measure integrin-ligand interactions, overcoming challenges with low-affinity binding. These techniques help understand integrin activation and cell adhesion regulation.

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Area of Science:

  • Cell biology
  • Biochemistry
  • Biophysics

Background:

  • Integrin receptors mediate cell adhesion by interacting with specific ligands.
  • Low binding affinities of typical integrin ligands complicate kinetic measurements.
  • Understanding integrin activation is crucial for cell adhesion processes.

Purpose of the Study:

  • To present real-time methodologies for studying integrin-ligand interactions.
  • To differentiate between integrin conformation and affinity regulation.
  • To advance the understanding of integrin activation mechanisms.

Main Methods:

  • Utilizing a ligand-mimetic probe for inside-out integrin regulation studies.
  • Employing real-time cell aggregation and disaggregation kinetics.
  • Monitoring ligand-induced epitopes via G-protein-coupled receptor signaling.

Main Results:

  • Demonstrated real-time measurement of integrin-ligand binding kinetics.
  • Distinguished between integrin conformational changes and affinity modulation.
  • Provided experimental data supporting the current integrin activation model.

Conclusions:

  • Novel real-time methods facilitate the study of integrin-ligand dynamics.
  • These techniques offer insights into the regulation of cell adhesion.
  • The findings contribute to a refined model of integrin activation.