Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 68, Issue 7, Pages 2054-2062Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.9b07022
Keywords
tanshinone IIA; Alzheimer's disease; Tau protein; ubiquitin-proteasome pathway
Funding
- National Natural Science Foundation of China [31871734, 31970366, 21877081]
- Guangdong Natural Science Foundation [2018A0303130054, 2018A030313507]
- Science and Technology Innovation Commission of Shenzhen [JCYJ20170818143107733, JCY20170818142053544, JCYJ20180507182405562, JCYJ20180305124211995, JCYJ20180305125619343]
- Guangdong Natural Science Foundation for Major Cultivation Project [2018B030336001]
- National Key Project for Synthetic Biology [SQ2018YFA090029]
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Alzheimer's disease (AD) is a common neurodegenerative disease which is partly characterized by the aggregation of hyperphosphorylated Tau proteins forming neurofibrillary tangles that promote AD pathogenesis. In this study, we investigated the effects of tanshinone IIA (Tan IIA) isolated from Salvia miltiorrhiza on Tau degradation in the treatment of AD. The results showed that Tan IIA reduced the Tau expression and attenuated Tau phosphorylation in N2a cells, Tau-overexpressing cells, and 3xTg-AD mouse primary neuron cells. Moreover, Tan IIA increased polyubiquitinated Tau accumulation and induced proteasomal degradation of the Tau protein. Additionally, Tan IIA became bound to the Tau protein and inhibited the formation of heparin-induced Tau fibrils. In summary, Tan IIA can increase polyubiquitinated Tau accumulation and induce the proteasomal degradation of the Tau protein and the binding of Tan IIA to the Tau protein, inhibiting the formation of Tau fibrils. Tan IIA may be further explored as a potential candidate for AD treatment.
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