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Amyloid-β 1-42 fibrils regulate SH-SY5Y cell adhesion in a delayed manner.

Urša Pečar Fonović¹, Slavko Kralj^1,2,3, Janko Kos^1,4

¹Faculty of Pharmacy, University of Ljubljana, Aškerčeva, Slovenia.

Journal of Alzheimer'S Disease : JAD

|March 18, 2026

Summary

Alzheimer's disease pathology involves amyloid-β (Aβ) fibrils disrupting cell adhesion in neurons. Aβ₄₂ fibrils, not monomers, impaired cell adhesion in SH-SY5Y cells, suggesting a therapeutic target.

Keywords:

Alzheimer's disease SH-SY5Y amyloid-β fibrils cell adhesion

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Area of Science:

Neuroscience
Molecular Biology
Cell Biology

Background:

Alzheimer's disease (AD) is characterized by amyloid-β (Aβ) peptide accumulation.
Aβ is linked to disrupted cell adhesion, impacting neuronal integrity.
Both Aβ precursor and Aβ peptides are implicated in cell adhesion disruption.

Purpose of the Study:

To investigate the effect of Aβ₄₂ fibrils versus monomers on cell adhesion.
To understand the molecular mechanisms of Aβ-induced cell adhesion disruption.
To identify potential therapeutic targets for Alzheimer's disease progression.

Main Methods:

Utilized SH-SY5Y neuroblastoma cells for experiments.
Pretreated cells with Aβ₄₂ fibrils and Aβ₄₂ monomers.
Assessed the impact on cell adhesion.

Main Results:

Aβ₄₂ fibrils significantly affected cell adhesion in SH-SY5Y cells.
Aβ₄₂ monomers did not show a similar effect on cell adhesion.
This highlights a fibril-specific mechanism in Aβ's impact on cell adhesion.

Conclusions:

Aβ₄₂ fibrils, but not monomers, disrupt cell adhesion pathways.
Understanding these mechanisms could lead to novel therapeutic strategies for Alzheimer's disease.
Targeting Aβ fibril interactions with adhesion molecules may preserve neuronal connectivity.