糖基化
P3肽
阿尔茨海默病的生物化学
淀粉样前体蛋白
氧化应激
愤怒(情绪)
早老素
神经毒性
化学
BACE1-AS系列
淀粉样蛋白(真菌学)
肽
阿尔茨海默病
发病机制
β淀粉样蛋白
老年斑
细胞生物学
活性氧
淀粉样前体蛋白分泌酶
小胶质细胞
生物化学
受体
生物
神经科学
医学
疾病
免疫学
炎症
内科学
毒性
无机化学
有机化学
出处
期刊:Drug research
[Georg Thieme Verlag KG]
日期:2023-03-20
卷期号:73 (05): 251-254
被引量:4
摘要
Neurofibrillary tangles and plaques containing tau serve as the biological markers for Alzheimer disease (AD) and pathogenesis is widely believed to be driven by the production and deposition of the β-amyloid peptide (Aβ). The β-amyloid peptide (Aβ) that results from the modification of the amyloid precursor protein (APP) by builds up as amyloid deposits in neuronal cells. Thus, a protein misfolding process is involved in the production of amyloid. In a native, aqueous buffer, amyloid fibrils are usually exceedingly stable and nearly insoluble. Although amyloid is essentially a foreign substance made of self-proteins, the immune system has difficulty identifying and eliminating it as such for unknown reasons. While the amyloidal deposit may have a direct role in the disease mechanism in some disease states involving amyloidal deposition, this is not always the case. Current research has shown that PS1 (presenilin 1) and BACE (beta-site APP-cleaving enzyme) have - and -secretase activity that increases β-amyloid peptide (Aβ). Wealth of data has shown that oxidative stress and AD are closely connected that causes the death of neuronal cells by producing reactive oxygen species (ROS). Additionally, it has been demonstrated that advanced glycation end products (AGEs) and β-amyloidal peptide (Aβ) together increase neurotoxicity. The objective of this review is to compile the most recent and intriguing data of AGEs and receptor for advanced glycation end products (RAGE) pathways which are responsible for AD.
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