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MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide and induces its fibrillization

Ce Zhang1, Yonggang Liu, Jonathan Gilthorpe

  • 1Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden. phyzce@nus.edu.sg

Plos One
|March 30, 2012
PubMed

Insights

Inflammation protein S100A9 binds to amyloid-beta (Aβ) peptides, promoting the formation of Alzheimer's disease (AD) amyloid plaques. This interaction may represent a protective brain response by reducing S100A9 toxicity.

Area of Science:

  • Neuroscience
  • Immunology
  • Biochemistry

Background:

  • Local inflammation is increasingly implicated in Alzheimer's disease (AD) pathology.
  • The precise mechanisms linking inflammation to AD pathogenesis remain unclear.

Purpose of the Study:

  • To investigate the interaction between the pro-inflammatory protein S100A9 and amyloid-beta (Aβ) peptides.
  • To elucidate the role of S100A9 in the formation of amyloid structures and its impact on cytotoxicity in the context of AD.

Main Methods:

  • Biochemical assays to assess the interaction between S100A9 and Aβ1-40.
  • Analysis of fibrillar structure formation.
  • Cytotoxicity assays to evaluate the impact of the interaction on cell viability.

Main Results:

  • The pro-inflammatory protein S100A9 directly interacts with the Aβ1-40 peptide.
  • This interaction promotes the formation of fibrillar β-amyloid structures.
  • Binding of S100A9 to Aβ1-40 amyloid structures reduces S100A9-mediated cytotoxicity.

Conclusions:

  • Secretion of S100A9 during inflammation contributes to the formation of amyloid plaques in the brain.
  • Amyloid plaque formation, in part mediated by S100A9, may serve as a protective mechanism by sequestering toxic S100A9 species in Alzheimer's disease patients.

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