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淀粉样前体蛋白羧基末端片段作为阿尔茨海默病中内溶酶体功能障碍的催化剂。

Amyloid precursor protein carboxy-terminal fragments as catalyzers of endolysosomal dysfunction in Alzheimer's disease.

作者信息

Vrancx Céline, Annaert Wim

机构信息

Laboratory for Membrane Trafficking, VIB Center for Brain and Disease Research, Leuven, Belgium; Department of Neurosciences, KU Leuven, Leuven, Belgium.

Laboratory for Membrane Trafficking, VIB Center for Brain and Disease Research, Leuven, Belgium; Department of Neurosciences, KU Leuven, Leuven, Belgium.

出版信息

Trends Neurosci. 2025 Jul;48(7):538-551. doi: 10.1016/j.tins.2025.05.007. Epub 2025 Jun 12.

Abstract

Proteolytic processing of the amyloid precursor protein (APP) generates not only the well-known β-amyloid (Aβ) peptides but also APP C-terminal fragments (APP-CTFs). Recent evidence from studies in murine- or human-derived (neuronal) models suggests that APP-CTFs may independently contribute to Alzheimer's disease (AD) pathology by disrupting cellular homeostasis. This review highlights pathological effects unique to APP-CTFs that are independent of Aβ, shedding light on their distinct role in disease progression. We explore the mechanisms underlying APP-CTF-induced toxicity, with a focus on their contribution to endolysosomal dysfunction. APP-CTFs impair lysosomal function and disrupt calcium signaling between the endoplasmic reticulum and lysosomes, compounding organelle dysfunction. Understanding these mechanisms will aid the design of preventive therapeutic strategies that take into account the impact of APP-CTFs on AD pathology.

摘要

淀粉样前体蛋白(APP)的蛋白水解加工不仅产生了众所周知的β-淀粉样蛋白(Aβ)肽,还产生了APP C末端片段(APP-CTF)。最近在小鼠或人源(神经元)模型中的研究证据表明,APP-CTF可能通过破坏细胞内稳态独立地导致阿尔茨海默病(AD)病理。本综述强调了APP-CTF特有的、独立于Aβ的病理效应,揭示了它们在疾病进展中的独特作用。我们探讨了APP-CTF诱导毒性的潜在机制,重点关注它们对内溶酶体功能障碍的影响。APP-CTF损害溶酶体功能,破坏内质网和溶酶体之间的钙信号,加剧细胞器功能障碍。了解这些机制将有助于设计预防性治疗策略,该策略考虑到APP-CTF对AD病理的影响。

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