Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ1‑40‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system
| Autor: | Yu Guo, Yi Zhang, Jing Guo, Dao-Yin Gong, Jinhao Zeng, Jun-Rong Yu, Yan-Wei Hao, Pei-Jun Xie, Bin Li |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Cancer Research Oncogene biology Tau protein Hyperphosphorylation Cell cycle Biochemistry Cell biology 03 medical and health sciences 030104 developmental biology 0302 clinical medicine Enzyme Oncology chemistry Proteasome Ubiquitin Apoptosis 030220 oncology & carcinogenesis Genetics biology.protein Molecular Medicine Molecular Biology |
| Zdroj: | Molecular Medicine Reports. 23 |
| ISSN: | 1791-3004 1791-2997 |
| Popis: | Yuan‑zhi‑san (YZS) is a classic type of Traditional Chinese Medicine, which has been reported to aid in the treatment of Alzheimer's disease (AD). The present study aimed to investigate the effects of YZS on tau protein aggregation, a hallmark of AD pathology, and its possible mechanisms. The results demonstrated that YZS improved learning and memory abilities, and decreased the severity of AD pathology in β‑amyloid (Aβ1‑40)‑induced AD rats. Moreover, YZS administration inhibited the hyperphosphorylation of tau protein at Ser199 and Thr231 sites. Several vital enzymes in the ubiquitin‑proteasome system (UPS), including ubiquitin‑activating enzyme E1a/b, ubiquitin‑conjugating enzyme E2a, carboxyl terminus of Hsc70‑interacting protein, ubiquitin C‑236 terminal hydrolase L1 and 26S proteasome, were all significantly downregulated in AD rats, which indicated an impaired enzymatic cascade in the UPS. In addition, it was identified that YZS treatment partly increased the expression levels of these enzymes in the brains of AD rats. In conclusion, the present results suggested that YZS could effectively suppress the hyperphosphorylation of tau proteins, which may be partially associated with its beneficial role in restoring functionality of the UPS. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|