该综述描述了阿尔茨海默病(AD)发病机制中伴侣和共同伴侣功能受损之间的相关性。该研究旨在突出该领域的重要研究领域。如Hsp90或Hsp70的伴侣是调节细胞稳态的关键试剂。由于某些条件,比如衰老,他们的活动受到损害,导致β-淀粉样蛋白和tau聚集。这导致神经认知障碍的发展。共同伴侣的失调是这种情况的原因之一。PP5,Cdc37,CacyBP/SIPTRAP1,CHIP蛋白,FKBP52或STIP1在AD发病机制中起关键作用。PP5、Cdc37、CacyBP/SIPTRAP1和FKBP52是Hsp90共同伴侣。CHIP蛋白是一种可切换Hsp70/Hsp90复合物的共同伴侣,STIP1与Hsp70结合。精确过程的识别允许有效治疗方法的发明。潜在的药物可以降低tau水平或抑制tau积累和聚集。一些物质对Aβ毒性具有神经保护作用。需要对伴侣和共同伴侣的进一步研究,以更全面地理解该主题的基本原则并改善AD的预防和治疗。
The review describes correlations between impaired functioning of
chaperones and co-
chaperones in Alzheimer\'s disease (AD) pathogenesis. The study aims to highlight significant lines of research in this field.
Chaperones like Hsp90 or Hsp70 are critical agents in regulating cell homeostasis. Due to some conditions, like aging, their activity is damaged, resulting in β-amyloid and tau aggregation. This leads to the development of neurocognitive impairment. Dysregulation of co-
chaperones is one of the causes of this condition. Disorders in the functioning of molecules like PP5, Cdc37, CacyBP/SIPTRAP1, CHIP protein, FKBP52, or STIP1 play a key role in AD pathogenesis. PP5, Cdc37, CacyBP/SIPTRAP1, and FKBP52 are Hsp90 co-
chaperones. CHIP protein is a co-chaperone that switches Hsp70/Hsp90 complexes, and STIP1 binds to Hsp70. Recognition of precise processes allows for the invention of effective treatment methods. Potential drugs may either reduce tau levels or inhibit tau accumulation and aggregation. Some substances neuroprotect from Aβ toxicity. Further studies on
chaperones and co-
chaperones are required to understand the fundamental tenets of this topic more entirely and improve the prevention and treatment of AD.