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Related Concept Videos

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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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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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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.
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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.
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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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The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower...
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Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of &#946;2 Integrin Activation
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Integrin intra-heterodimer affinity inversely correlates with integrin activatability.

Guangyu Sun1, Emilie Guillon1, Scott A Holley1

  • 1Department of Molecular, Cellular and Developmental Biology, Yale University, 260 Whitney Avenue, New Haven, CT 06520, USA.

Cell Reports
|June 9, 2021
PubMed
Summary

Integrins mediate cell adhesion but are not activated on zebrafish cell surfaces, even with fibronectin. Weak integrin heterodimer affinity may increase integrin activatability.

Keywords:
cell adhesionfibronectinfluorescence cross-correlation spectroscopyfluorescence lifetime imagingfluorescence resonance energy transferintegrinintra-heterodimer stabilitymolecular dynamicssomitogenesiszebrafish

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Area of Science:

  • Cell Biology
  • Biophysics
  • Developmental Biology

Background:

  • Integrins are cell surface receptors crucial for cell adhesion to the extracellular matrix.
  • Integrin activation involves a conformational change, regulating cellular responses.
  • Previous studies focused on integrin α5β1 during zebrafish development.

Purpose of the Study:

  • To characterize integrin αV fibronectin receptors in zebrafish embryos.
  • To investigate the relationship between integrin heterodimer stability and activation in vivo.
  • To understand the biophysical mechanisms governing integrin function during development.

Main Methods:

  • Single-molecule biophysical measurements in living zebrafish embryos.
  • Fluorescence resonance energy transfer (FRET)-fluorescence lifetime imaging microscopy (FLIM) for integrin activation.
  • Fluorescence cross-correlation spectroscopy (FCCS) for integrin intra-heterodimer stability.

Main Results:

  • Integrin heterodimers αVβ3, αVβ5, and αVβ6 showed robust cell surface expression but were not activated in vivo, despite fibronectin presence.
  • Activatable integrins, like αVβ1, and specific αVβ3, αVβ5, αVβ6 variants displayed poor cell surface expression.
  • These activatable forms had a higher intra-heterodimer dissociation constant (KD), indicating weaker affinity.

Conclusions:

  • Robust cell surface expression of integrins does not guarantee in vivo activation.
  • Weak integrin intra-heterodimer affinity correlates with decreased cell surface stability.
  • Reduced heterodimer affinity may enhance integrin activatability, influencing zebrafish development.