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糖基化在衰老和神经退行性疾病中的作用。

Glycosylation in aging and neurodegenerative diseases.

出版信息

Acta Biochim Biophys Sin (Shanghai). 2024 Aug 15;56(8):1208-1220. doi: 10.3724/abbs.2024136.

DOI:10.3724/abbs.2024136
PMID:39225075
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11466714/
Abstract

Aging, a complex biological process, involves the progressive decline of physiological functions across various systems, leading to increased susceptibility to neurodegenerative diseases. In society, demographic aging imposes significant economic and social burdens due to these conditions. This review specifically examines the association of protein glycosylation with aging and neurodegenerative diseases. Glycosylation, a critical post-translational modification, influences numerous aspects of protein function that are pivotal in aging and the pathophysiology of diseases such as Alzheimer's disease, Parkinson's disease, and other neurodegenerative conditions. We highlight the alterations in glycosylation patterns observed during aging, their implications in the onset and progression of neurodegenerative diseases, and the potential of glycosylation profiles as biomarkers for early detection, prognosis, and monitoring of these age-associated conditions, and delve into the mechanisms of glycosylation. Furthermore, this review explores their role in regulating protein function and mediating critical biological interactions in these diseases. By examining the changes in glycosylation profiles associated with each part, this review underscores the potential of glycosylation research as a tool to enhance our understanding of aging and its related diseases.

摘要

衰老是一个复杂的生物学过程,涉及到各个系统生理功能的逐渐衰退,导致易患神经退行性疾病。在社会中,由于这些情况,人口老龄化带来了巨大的经济和社会负担。本综述特别研究了蛋白质糖基化与衰老和神经退行性疾病的关系。糖基化是一种关键的翻译后修饰,影响着蛋白质功能的许多方面,这些方面在衰老和阿尔茨海默病、帕金森病和其他神经退行性疾病等疾病的病理生理学中起着关键作用。我们强调了在衰老过程中观察到的糖基化模式的改变,它们在神经退行性疾病的发生和进展中的意义,以及糖基化谱作为这些与年龄相关疾病的早期检测、预后和监测的生物标志物的潜力,并深入探讨了糖基化的机制。此外,本综述还研究了它们在调节蛋白质功能和介导这些疾病中关键生物学相互作用中的作用。通过检查与每个部分相关的糖基化谱的变化,本综述强调了糖基化研究作为增强我们对衰老及其相关疾病的理解的一种工具的潜力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/3055f7605409/t4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/7d644a7c1b40/t1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/91dd68d5ba54/t2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/53fe3a0a6a65/t3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/3055f7605409/t4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/7d644a7c1b40/t1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/91dd68d5ba54/t2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/53fe3a0a6a65/t3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4839/11466714/3055f7605409/t4.jpg

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Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures.磷酸化和 O-GlcNAc 化在同一个α-突触核蛋白位点产生不同的纤维结构。
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