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Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion

Alexander G Bobylev1, Roman S Fadeev1, Liya G Bobyleva1

  • 1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow, Russia.

International Journal of Molecular Sciences
|April 30, 2021
PubMed

Insights

Amyloid aggregates, like those from titin, disrupt cell adhesion and cytoskeleton organization in smooth muscle cells. This surface roughness may explain the anti-adhesive properties of various amyloid aggregates.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Materials Science

Background:

  • Amyloid aggregates, particularly amyloid β-proteins, are known for cytotoxic effects and impairing cell adhesion.
  • Smooth muscle cells are crucial for vascular function and are susceptible to external influences.

Purpose of the Study:

  • To investigate the impact of smooth-muscle titin amyloid aggregates on smooth muscle cell cultures.
  • To elucidate the mechanisms behind impaired cell adhesion caused by amyloid aggregates.
  • To explore the role of surface microtopology in the anti-adhesive properties of titin-amyloid aggregates.

Main Methods:

  • Culturing smooth muscle cells and exposing them to titin amyloid aggregates.
  • Utilizing atomic force microscopy to analyze the microtopology of titin-amyloid-aggregate-coated surfaces.
  • Measuring surface roughness and correlating it with cell adhesion properties.

Main Results:

  • Titin amyloid aggregates impaired smooth muscle cell adhesion, leading to actin cytoskeleton disorganization.
  • Observed formation of filopodia, lamellipodia, and stress fibers in affected cells.
  • Surface roughness of titin-amyloid-aggregate coatings (2.7–4.9 nm) correlated with significant anti-adhesive properties.

Conclusions:

  • Amyloid aggregates, due to their surface microtopology, can exhibit intrinsic anti-adhesive properties.
  • The findings suggest that similar effects may be observed with amyloid aggregates of other proteins.
  • Understanding these mechanisms is crucial for addressing the negative impact of amyloids on cell adhesion and related biological processes.
Keywords:
amyloidamyloid aggregationamyloidosiscytotoxicity of amyloid fibrilsprotein aggregationsmooth-muscle titin

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