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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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Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
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β1-Integrin-Mediated Adhesion Is Lipid-Bilayer Dependent.

Seoyoung Son1, George J Moroney2, Peter J Butler1

  • 1Intercollege Graduate Degree Program in Bioengineering and Department of Biomedical Engineering, The Pennsylvania State University, University Park, Pennsylvania.

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Altering cell membrane biophysics with benzyl alcohol thins liquid-disordered domains, enhancing integrin-Arg-Gly-Asp-peptide adhesion and focal adhesion size, impacting cell migration.

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Area of Science:

  • Cellular mechanobiology
  • Membrane biophysics
  • Integrin adhesion dynamics

Background:

  • Integrin-mediated adhesion is crucial for cell functions like locomotion and mechanobiology.
  • The influence of cell membrane biophysics and dynamics on integrin adhesion remains largely unexplored.

Purpose of the Study:

  • To investigate how modulating membrane biophysics affects integrin adhesion kinetics and cell behavior.
  • To elucidate the role of lipid domains in regulating integrin-mediated cell adhesion and migration.

Main Methods:

  • Human aortic endothelial cells were treated with amphiphiles to alter membrane properties.
  • Single-integrin-molecule adhesion kinetics were measured using optical traps.
  • Integrin diffusion and molecular brightness were assessed via fluorescence correlation spectroscopy.
  • Cell migration was quantified using wound-healing assays.

Main Results:

  • Benzyl alcohol (BA), which thins liquid-disordered (Ld) domains, increased β1-integrin-Arg-Gly-Asp-peptide affinity by 18% and valency.
  • BA treatment led to larger focal adhesions and reduced cell migration speeds.
  • Vitamin E, which thickens liquid-ordered (Lo) domains, did not alter integrin affinity but reduced binding probability, resulting in smaller focal adhesions.
  • Triton X-100 showed no significant effects on integrin binding kinetics, focal adhesion size, or migration speed.

Conclusions:

  • Thinning of Ld lipid domains by amphiphiles is critical for enhancing β1-integrin-Arg-Gly-Asp-peptide affinity and valency.
  • Membrane biophysics, specifically Ld domain properties, plays a significant role in modulating integrin adhesion, nascent adhesion formation, and cell migration.