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Related Experiment Videos

Agrin binds alpha-synuclein and modulates alpha-synuclein fibrillation.

I-Hsuan Liu1, Vladimir N Uversky, Larissa A Munishkina

  • 1Biomedical/Biotechnology Research Institute, North Carolina Central University, Durham, NC 27707, USA.

Glycobiology
|July 23, 2005
PubMed
Summary

Agrin protein accelerates the formation of toxic alpha-synuclein fibrils, a key factor in Parkinson's disease (PD). This finding suggests shared mechanisms in neurodegenerative disorders like PD and Alzheimer's disease (AD).

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Corrigendum to "Enhancing intrinsic TGF-β signaling via heparan sulfate glycosaminoglycan regulation to promote mesenchymal stem cell capabilities and chondrogenesis for cartilage repair" [Int. J. Biol. Macromol. 282 (2024) 137242].

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Agrin's role in the brain extends beyond synaptogenesis.
  • Agrin is implicated in Alzheimer's disease (AD) pathology, specifically beta-amyloid plaque formation.
  • Alpha-synuclein is central to Parkinson's disease (PD) pathogenesis, with fibril formation enhanced by certain molecules.

Purpose of the Study:

  • To investigate the role of agrin in Parkinson's disease (PD).
  • To determine if agrin influences alpha-synuclein aggregation.
  • To explore the presence of agrin in PD-associated lesions.

Main Methods:

  • Investigated agrin's interaction with alpha-synuclein in vitro.
  • Assessed agrin's effect on alpha-synuclein conformational changes and fibril formation.

Related Experiment Videos

  • Examined agrin colocalization with alpha-synuclein in human PD brain tissue.

    • Main Results:

    • Agrin binds to alpha-synuclein in a heparan sulfate-dependent manner.
    • Agrin induces beta-sheet structure and enhances the insolubility of alpha-synuclein.
    • Agrin accelerates the formation of alpha-synuclein protofibrils and fibrils.
    • Agrin colocalizes with alpha-synuclein in Lewy bodies in the substantia nigra of PD brains.

    Conclusions:

    • Agrin accelerates the formation of insoluble alpha-synuclein fibrils, relevant to PD.
    • Agrin's involvement in both AD and PD suggests shared molecular pathways in neurodegeneration.
    • Agrin may be a potential therapeutic target for neurodegenerative diseases.