Degradation of Angelica sinensis polysaccharide: Structures and protective activities against ethanol-induced acute liver injury

化学 生物化学 多糖 超氧化物歧化酶 当归 肝损伤 乳酸脱氢酶 过氧化氢酶 谷胱甘肽过氧化物酶 谷胱甘肽 丙二醛 药理学 抗氧化剂 生物 医学 替代医学 中医药 病理
作者
Yu Zhang,Haoyu Wang,Yuheng Zheng,Zhijing Wu,Junxi Liu,Fang Cheng,Kaiping Wang
出处
期刊:Carbohydrate Polymers [Elsevier BV]
卷期号:328: 121745-121745 被引量:36
标识
DOI:10.1016/j.carbpol.2023.121745
摘要

Angelica sinensis polysaccharide (ASP) possesses diverse bioactivities; however, its metabolic fate following oral administration remains poorly understood. To intuitively determine its intestinal digestion behavior after oral administration, ASP was labeled with fluorescein, and it was found to accumulate and be degraded in the cecum and colon. Therefore, we investigated the in vitro enzymatic degradation behavior and identified the products. The results showed that ASP could be degraded into fragments with molecular weights similar to those of the fragments observed in vivo. Structural characterization revealed that ASP is a highly branched acid heteropolysaccharide with AG type II domains, and its backbone is predominantly composed of 1,3-Galp, →3,6)-Galp-(1→6)-Galp-(1→, 1,4-Manp, 1,4-Rhap, 1,3-Glcp, 1,2,3,4-Galp, 1,3,4,6-Galp, 1,3,4-GalAp and 1,4-GlcAp, with branches of Araf, Glcp and Galp. In addition, the high molecular weight enzymatic degradation products (ASP H) maintained a backbone structure almost identical to that of ASP, but exhibited only partial branch changes. Then, the results of ethanol-induced acute liver injury experiments revealed that ASP and ASP H reduced the expression of aspartate aminotransferase (AST), alanine aminotransferase (ALT), lactate dehydrogenase (LDH), and malondialdehyde (MDA) and increased the superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) levels, thereby relieving ethanol-induced acute liver injury.
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