Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2020 Nov;34(11):2867-2888.
doi: 10.1002/ptr.6732. Epub 2020 Jun 3.

Resveratrol targeting tau proteins, amyloid-beta aggregations, and their adverse effects: An updated review

Affiliations
Review

Resveratrol targeting tau proteins, amyloid-beta aggregations, and their adverse effects: An updated review

Milad Ashrafizadeh et al. Phytother Res. 2020 Nov.

Abstract

Resveratrol (Res) is a non-flavonoid compound with pharmacological actions such as antioxidant, antiinflammatory, hepatoprotective, antidiabetes, and antitumor. This plant-derived chemical has a long history usage in treatment of diseases. The excellent therapeutic impacts of Res and its capability in penetration into blood-brain barrier have made it an appropriate candidate in the treatment of neurological disorders (NDs). Tau protein aggregations and amyloid-beta (Aβ) deposits are responsible for the induction of NDs. A variety of studies have elucidated the role of these aggregations in NDs and the underlying molecular pathways in their development. In the present review, based on the recently published articles, we describe that how Res administration could inhibit amyloidogenic pathway and stimulate processes such as autophagy to degrade Aβ aggregations. Besides, we demonstrate that Res supplementation is beneficial in dephosphorylation of tau proteins and suppressing their aggregations. Then, we discuss molecular pathways and relate them to the treatment of NDs.

Keywords: aggregation; amyloid-beta; neurological disorders; neuroprotective; resveratrol; tau protein.

PubMed Disclaimer

Similar articles

Cited by

References

REFERENCES

    1. Abubaker, A. A., Vara, D., Visconte, C., Eggleston, I., Torti, M., Canobbio, I., & Pula, G. (2019). Amyloid peptide beta1-42 induces integrin alphaIIbbeta3 activation, platelet adhesion, and Thrombus formation in a NADPH oxidase-dependent manner. Oxidative Medicine and Cellular Longevity, 2019, 1-12. https://doi.org/10.1155/2019/1050476
    1. Acharya, U. R., Hagiwara, Y., & Adeli, H. (2018). Automated seizure prediction. Epilepsy & Behavior, 88, 251-261. https://doi.org/10.1016/j.yebeh.2018.09.030
    1. Adabizadeh, M., Mehri, S., Rajabpour, M., Abnous, K., Rashedinia, M., & Hosseinzadeh, H. (2019). The effects of crocin on spatial memory impairment induced by hyoscine: Role of NMDA, AMPA, ERK, and CaMKII proteins in rat hippocampus. Iranian Journal of Basic Medical Sciences, 22(6), 601-609.
    1. Ai, Z., Li, C., Li, L., & He, G. (2015). Resveratrol inhibits beta-amyloid-induced neuronal apoptosis via regulation of p53 acetylation in PC12 cells. Molecular Medicine Reports, 11(4), 2429-2434. https://doi.org/10.3892/mmr.2014.3034
    1. Aktas, H. S., Ozel, Y., Ahmad, S., Pence, H. H., Ayaz-Adakul, B., Kudas, I., … Elcioglu, H. K. (2019). Protective effects of resveratrol on hepatic ischemia reperfusion injury in streptozotocin-induced diabetic rats. Molecular and Cellular Biochemistry, 460(1-2), 217-224. https://doi.org/10.1007/s11010-019-03582-z

MeSH terms

LinkOut - more resources