中国神经再生研究(英文版) ›› 2023, Vol. 18 ›› Issue (12): 2689-2690.doi: 10.4103/1673-5374.374013

• 观点:退行性病与再生 • 上一篇    下一篇

冰山一角?被低估的非经典β—淀粉样蛋白对阿尔茨海默病的潜在作用

  

  • 出版日期:2023-12-15 发布日期:2023-06-15

The tip of the iceberg? The underestimated potential of non-canonical beta-amyloids for Alzheimer’s disease

Lukas Busch, Bernd Bufe*   

  1. Department of Informatics and Microsystems Technology, University of Applied Sciences Kaiserslautern, Zweibrücken, Germany
  • Online:2023-12-15 Published:2023-06-15
  • Contact: Bernd Bufe, PhD, Bernd.Bufe@hs-kl.de.
  • Supported by:
    We thank Kristina Endres (JGU Mainz) and Stefan Kins (TU Kaiserslautern) for providing valuable insights and thoughtful comments during the writing process that helped to improve this manuscript. 
    This work was supported by Ministerium für Wissenschaft und Gesundheit  (MWG), Rheinland Pfalz, NeurodegX Forschungskolleg (to BB). 

摘要: https://orcid.org/0000-0003-1610-0658 (Bernd Bufe)

Abstract: Formation and deposition of amyloid-beta (Aβ) are considered one of the main drivers of Alzheimer’s disease (AD). For more than 30 years, Aβ has challenged researchers through its complex physicochemical properties and multiple peptide processing steps that involve several proteases (Andreasson et al., 2007), ultimately creating many Aβ variants that trigger various physiological effects in neurons, glia, and peripheral immune cells (Busch et al., 2022a). Recent research identified various additional naturally occurring Aβ species with different lengths and chemical modifications. Their impact on AD pathology is currently not well understood, although some of them occur at much higher abundance than Aβ1–42 and Aβ1–40. Here, we highlight new findings that challenge traditional views and summarize recent findings that argue for a significant contribution of previously neglected Aβ variants to the development and progression of AD. Next, we provide an overview on the technical challenges and open questions associated with their study and highlight how different Aβ variants such as Aβ11–40 and Aβ17–40 may use formyl peptide receptor signaling to trigger distinct cellular effects in neurons, glia, and immune cells.