Cirsium japonicum var. Maackii Improves Cognitive Impairment under Amyloid Beta25-35-Induced Alzheimer's Disease Model.

Qi Qi Pang,Eun Ju Cho,Ji-Hyun Kim,Ji Myung Choi,Sanghyun Lee,Jia-Le Song,Nahide Gulsah Deniz

doi:10.1155/2022/4513998

Abstract

Abnormal production and degradation of amyloid beta (Aβ) in the brain lead to oxidative stress and cognitive impairment in Alzheimer's disease (AD). Cirsium japonicum var. maackii (CJM) is widely used as an herbal medicine and has antibacterial and anti-inflammatory properties. This study focused on the protective effect of the ethyl acetate fraction from CJM (ECJM) on Aβ25-35-induced control mice. In the T-maze and novel object recognition test, ECJM provided higher spatial memory and object recognition compared to Aβ25-35 treatment alone. In the Morris water maze test, ECJM-administered mice showed greater learning and memory abilities than Aβ25-35-induced control mice. Additionally, ECJM-administered mice experienced inhibited lipid peroxidation and nitric oxide production in a dose-dependent manner. The present study indicates that ECJM improves cognitive impairment by inhibiting oxidative stress in Aβ25-35-induced mice. Therefore, CJM may be useful for the treatment of AD and may be a potential material for functional foods.

Highlights

Alzheimer’s disease (AD) is a neurodegenerative disease, and its main feature is the excessive accumulation of amyloid beta (Aβ) peptides in the brain [1]
The nitric oxide (NO) production in the ECJM50, ECJM100, and donepezil groups in the kidneys showed no significant difference when compared with the control group. These results indicated that the levels of NO in the brain, liver, and kidney were significantly increased by injection of Aβ25-35, and the administration of ethyl acetate fraction from CJM (ECJM) and donepezil inhibited NO production in tissues
The present results indicated that Aβ25-35 elevated lipid peroxidation in the brain, liver, and kidney, but oral administration of ECJM attenuated the lipid peroxidation caused by Aβ25-35

Summary

Introduction

Alzheimer’s disease (AD) is a neurodegenerative disease, and its main feature is the excessive accumulation of amyloid beta (Aβ) peptides in the brain [1]. Aβ is derived from amyloid precursor protein (APP) through the proteolytic cleavage of a family of enzymes (β- and γ-secretase), which leads to memory loss and cognitive decline by the formation of senile plaques [2]. Previous studies have demonstrated that the accumulation and aggregation of Aβ (i.e., oligomers and senile plaques) are highly neurotoxic and form Aβ deposit/fibrils, which can contribute to AD development [3]. Aβ oligomers in the early stage and Aβ plaques in later stages are established, so they are observed in the AD brain for decades before the onset of memory/behavior/cognitive symptoms [4]. The Aβ25-35 fragment used in the present study, a core toxic fragment cleaved from the full-length Aβ peptide, plays a critical role in the development of AD by inducing oxidative stress, neurotoxicity, and inflammatory response [5]

Methods

Results

Conclusion