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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,...
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.
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...
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
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...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

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Related Experiment Video

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Quantitation of Endothelial Cell Adhesiveness In Vitro
10:24

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Published on: June 18, 2015

CHO cells expressing the high affinity alpha(IIb)beta3 T562N integrin demonstrate enhanced adhesion under shear.

P Legendre1, A Salsmann, J Rayes

  • 1INSERM U143, Le Kremlin-Bicetre, France.

Journal of Thrombosis and Haemostasis : JTH
|January 18, 2006
PubMed
Summary

The high-affinity alpha(IIb)beta3 receptor enhances cell adhesion under flow conditions, unlike the wild-type receptor. This study reveals that alpha(IIb)beta3 activation stabilizes integrin binding to fibrinogen and VWF under shear forces.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Platelet adhesion is crucial for vascular functions and is mediated by alpha(IIb)beta3 integrins.
  • The functional state of alpha(IIb)beta3 influences its sensitivity to shear forces in the vasculature.

Purpose of the Study:

  • To investigate how the affinity state of alpha(IIb)beta3 affects cell attachment under flow conditions.
  • To compare the adhesive properties of Chinese hamster ovary cells expressing wild-type (low affinity) alpha(IIb)beta3 versus a high-affinity T562N mutant.

Main Methods:

  • A real-time videomicroscopy adhesion assay was employed to study cell attachment.
  • Experiments were conducted under controlled flow conditions using von Willebrand factor (VWF) or fibrinogen as adhesion substrates.

Main Results:

  • The high-affinity alpha(IIb)beta3 T562N receptor supported significantly greater cell adhesion to fibrinogen and VWF compared to the wild-type receptor at varying shear rates (50 s⁻¹ and 100 s⁻¹).
  • Specific peptide inhibitors, HHLGGAKQAGDV (H12) and Arg-Gly-Asp-Ser (RGDS), demonstrated distinct roles in initial attachment and stabilization of adhesion, respectively.
  • A lower concentration of RGDS was needed to inhibit adhesion mediated by the high-affinity T562N receptor, indicating altered binding dynamics.

Conclusions:

  • Alpha(IIb)beta3 receptor activation is linked to stabilized integrin interactions with fibrinogen and VWF under shear stress.
  • The affinity state of alpha(IIb)beta3 plays a critical role in regulating cell adhesion dynamics in response to physiological flow conditions.