Open Access

Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ1‑40‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system

  • Authors:
    • Bin Li
    • Pei-Jun Xie
    • Yan-Wei Hao
    • Yu Guo
    • Jun-Rong Yu
    • Dao-Yin Gong
    • Jing Guo
    • Jin-Hao Zeng
    • Yi Zhang
  • View Affiliations

  • Published online on: February 15, 2021     https://doi.org/10.3892/mmr.2021.11918
  • Article Number: 279
  • Copyright: © Li et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

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.
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April-2021
Volume 23 Issue 4

Print ISSN: 1791-2997
Online ISSN:1791-3004

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Spandidos Publications style
Li B, Xie P, Hao Y, Guo Y, Yu J, Gong D, Guo J, Zeng J and Zhang Y: Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ<sub>1‑40</sub>‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system. Mol Med Rep 23: 279, 2021
APA
Li, B., Xie, P., Hao, Y., Guo, Y., Yu, J., Gong, D. ... Zhang, Y. (2021). Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ<sub>1‑40</sub>‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system. Molecular Medicine Reports, 23, 279. https://doi.org/10.3892/mmr.2021.11918
MLA
Li, B., Xie, P., Hao, Y., Guo, Y., Yu, J., Gong, D., Guo, J., Zeng, J., Zhang, Y."Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ<sub>1‑40</sub>‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system". Molecular Medicine Reports 23.4 (2021): 279.
Chicago
Li, B., Xie, P., Hao, Y., Guo, Y., Yu, J., Gong, D., Guo, J., Zeng, J., Zhang, Y."Yuan‑zhi‑san inhibits tau protein aggregation in an Aβ<sub>1‑40</sub>‑induced Alzheimer's disease rat model via the ubiquitin‑proteasome system". Molecular Medicine Reports 23, no. 4 (2021): 279. https://doi.org/10.3892/mmr.2021.11918