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Co-treatment with the Seed of L. and the Aerial Part of Synergistically Suppresses Aβ-induced Neurotoxicity by Altering APP Processing

Overview
Journal Food Sci Nutr
Specialty Biotechnology
Date 2024 Mar 8
PMID 38455162
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Abstract

Accumulation of β-amyloid peptide (Aβ) induces neurotoxicity, which is the primary risk factor in the pathogenesis of Alzheimer's disease (AD). The cleavage of amyloid precursor protein (APP) by the β- (BACE) and γ- (PS1, PS2) secretases is a critical step in the amyloidogenic pathway. The induction of neuronal apoptosis by Aβ involves increased expression of B-cell lymphoma protein 2 (Bcl-2)-associated X (Bax) and decreased Bcl-2 expression. The seed of L. (CTS) and the aerial part of (TC) are traditional herbs used to treat several neurodegenerative diseases. In this study, the neuroprotective effects of co-treatment with CTS and TC on Aβ-induced neurotoxicity in SH-SY5Y neuroblastoma cells and the underlying mechanisms were investigated. CTS, TC, and the co-treatment (CTS + TC) were added to Aβ-treated SH-SY5Y cells. CTS + TC synergistically increased cell viability and inhibited reactive oxygen species production. CTS + TC resulted in significant downregulation of BACE, PS1, PS2, and APP, as well as the 99-aa C-terminal domain of APP, compared with either CTS or TC alone. Compared with the single herbs, co-treatment with CTS and TC markedly decreased the expression of Bax and increased the expression of Bcl-2, consistent with its anti-apoptotic effects. These findings suggest that co-treatment with CTS and TC may be useful for AD prevention.

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Co-treatment with the seed of L. and the aerial part of synergistically suppresses Aβ-induced neurotoxicity by altering APP processing.

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PMID: 38455162 PMC: 10916591. DOI: 10.1002/fsn3.3768.

References
1.
Pulina M, Hopkins M, Haroutunian V, Greengard P, Bustos V . C99 selectively accumulates in vulnerable neurons in Alzheimer's disease. Alzheimers Dement. 2019; 16(2):273-282. DOI: 10.1016/j.jalz.2019.09.002. View

2.
Peng X, Wang X, Dong J, Qin X, Li Z, Yang H . Rare Hybrid Dimers with Anti-Acetylcholinesterase Activities from a Safflower (Carthamus tinctorius L.) Seed Oil Cake. J Agric Food Chem. 2017; 65(43):9453-9459. DOI: 10.1021/acs.jafc.7b03431. View

3.
Bolduc D, Montagna D, Seghers M, Wolfe M, Selkoe D . The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase. Elife. 2016; 5. PMC: 5134833. DOI: 10.7554/eLife.17578. View

4.
Prasansuklab A, Tencomnao T . Amyloidosis in Alzheimer's Disease: The Toxicity of Amyloid Beta (A β ), Mechanisms of Its Accumulation and Implications of Medicinal Plants for Therapy. Evid Based Complement Alternat Med. 2013; 2013:413808. PMC: 3671299. DOI: 10.1155/2013/413808. View

5.
Castro M, Hadziselimovic A, Sanders C . The vexing complexity of the amyloidogenic pathway. Protein Sci. 2019; 28(7):1177-1193. PMC: 6566549. DOI: 10.1002/pro.3606. View