The role of pro-inflammatory S100A9 in Alzheimer’s disease amyloid-neuroinflammatory cascade

Clicks: 133
ID: 117505
2013
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #322 of 438 articles by views in acta neuropathologica

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 438 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Pro-inflammatory S100A9 protein is increasingly recognized as an important contributor to inflammation-related neurodegeneration. Here, we provide insights into S100A9 specific mechanisms of action in Alzheimer’s disease (AD). Due to its inherent amyloidogenicity S100A9 contributes to amyloid plaque formation together with Aβ. In traumatic brain injury (TBI) S100A9 itself rapidly forms amyloid plaques, which were reactive with oligomer-specific antibodies, but not with Aβ and amyloid fibrillar antibodies. They may serve as precursor-plaques for AD, implicating TBI as an AD risk factor. S100A9 was observed in some hippocampal and cortical neurons in TBI, AD and non-demented aging. In vitro S100A9 forms neurotoxic linear and annular amyloids resembling Aβ protofilaments. S100A9 amyloid cytotoxicity and native S100A9 pro-inflammatory signaling can be mitigated by its co-aggregation with Aβ, which results in a variety of micron-scale amyloid complexes. NMR and molecular docking demonstrated transient interactions between native S100A9 and Aβ. Thus, abundantly present in AD brain pro-inflammatory S100A9, possessing also intrinsic amyloidogenic properties and ability to modulate Aβ aggregation, can serve as a link between the AD amyloid and neuroinflammatory cascades and as a prospective therapeutic target.
Reference Key
wang2013actathe Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Chao Wang;Alexey G. Klechikov;Anna L. Gharibyan;Sebastian K. T. S. Wärmländer;Jüri Jarvet;Lina Zhao;Xueen Jia;S. K. Shankar;Anders Olofsson;Thomas Brännström;Yuguang Mu;Astrid Gräslund;Ludmilla A. Morozova-Roche;Chao Wang;Alexey G. Klechikov;Anna L. Gharibyan;Sebastian K. T. S. Wärmländer;Jüri Jarvet;Lina Zhao;Xueen Jia;S. K. Shankar;Anders Olofsson;Thomas Brännström;Yuguang Mu;Astrid Gräslund;Ludmilla A. Morozova-Roche;
Journal acta neuropathologica
Year 2013
DOI
doi:10.1007/s00401-013-1208-4
URL
https://link.springer.com/article/10.1007/s00401-013-1208-4
Keywords
pathology neurosciences

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.