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Parkinson's disease and glucose metabolism impairment.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-02-17 DOI: 10.1186/s40035-025-00467-8
Liangjing Chen, Chunyu Wang, Lixia Qin, Hainan Zhang

Parkinson's disease (PD) is the second most common neurodegenerative disorder. PD patients exhibit varying degrees of abnormal glucose metabolism throughout disease stages. Abnormal glucose metabolism is closely linked to the PD pathogenesis and progression. Key glucose metabolism processes involved in PD include glucose transport, glycolysis, the tricarboxylic acid cycle, oxidative phosphorylation, the pentose phosphate pathway, and gluconeogenesis. Recent studies suggest that glucose metabolism is a potential therapeutic target for PD. In this review, we explore the connection between PD and abnormal glucose metabolism, focusing on the underlying pathophysiological mechanisms. We also summarize potential therapeutic drugs related to glucose metabolism based on results from current cellular and animal model studies.

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引用次数: 0
The C. elegans gba-3 gene encodes a glucocerebrosidase that exacerbates α-synuclein-mediated impairments in deletion mutants.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-02-13 DOI: 10.1186/s40035-024-00463-4
Ning Liu, Rongzhen Li, Xiaobing Huang, Merja Lakso, Garry Wong
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引用次数: 0
AMPA receptor diffusional trapping machinery as an early therapeutic target in neurodegenerative and neuropsychiatric disorders.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-02-11 DOI: 10.1186/s40035-025-00470-z
Daniel Choquet, Patricio Opazo, Hongyu Zhang

Over the past two decades, there has been a growing recognition of the physiological importance and pathological implications surrounding the surface diffusion of AMPA receptors (AMPARs) and their diffusional trapping at synapses. AMPAR surface diffusion entails the thermally powered random Brownian lateral movement of these receptors within the plasma membrane, facilitating dynamic exchanges between synaptic and extrasynaptic compartments. This process also enables the activity-dependent diffusional trapping and accumulation of AMPARs at synapses through transient binding to synaptic anchoring slots. Recent research highlights the critical role of synaptic recruitment of AMPARs via diffusional trapping in fundamental neural processes such as the development of the early phases of long-term potentiation (LTP), contextual fear memory, memory consolidation, and sensory input-induced cortical remapping. Furthermore, studies underscore that regulation of AMPAR diffusional trapping is altered across various neurological disease models, including Huntington's disease (HD), Alzheimer's disease (AD), and stress-related disorders like depression. Notably, pharmacological interventions aimed at correcting deficits in AMPAR diffusional trapping have demonstrated efficacy in restoring synapse numbers, LTP, and memory functions in these diverse disease models, despite their distinct pathogenic mechanisms. This review provides current insights into the molecular mechanisms underlying the dysregulation of AMPAR diffusional trapping, emphasizing its role as a converging point for multiple pathological signaling pathways. We propose that targeting AMPAR diffusional trapping represents a promising early therapeutic strategy to mitigate synaptic plasticity and memory deficits in a spectrum of brain disorders, encompassing but not limited to HD, AD, and stress-related conditions. This approach underscores an integrated therapeutic target amidst the complexity of these neurodegenerative and neuropsychiatric diseases.

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引用次数: 0
Refining α-synuclein seed amplification assays to distinguish Parkinson's disease from multiple system atrophy.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-02-07 DOI: 10.1186/s40035-025-00469-6
James A Wiseman, Clinton P Turner, Richard L M Faull, Glenda M Halliday, Birger Victor Dieriks

Background: Parkinson's disease (PD) and multiple system atrophy (MSA) are two distinct α-synucleinopathies traditionally differentiated through clinical symptoms. Early diagnosis of MSA is problematic, and seed amplification assays (SAAs), such as real-time quaking-induced conversion (RT-QuIC), offer the potential to distinguish these diseases through their underlying α-synuclein (α-Syn) pathology and proteoforms. Currently, SAAs provide a binary result, signifying either the presence or absence of α-Syn seeds. To enhance the diagnostic potential and biological relevance of these assays, there is a pressing need to incorporate quantification and stratification of α-Syn proteoform-specific aggregation kinetics into current SAA pipelines.

Methods: Optimal RT-QuIC assay conditions for α-Syn seeds extracted from PD and MSA patient brains were determined, and assay kinetics were assessed for α-Syn seeds from different pathologically relevant brain regions (medulla, substantia nigra, hippocampus, middle temporal gyrus, and cerebellum). The conformational profiles of disease- and region-specific α-Syn proteoforms were determined by subjecting the amplified reaction products to concentration-dependent proteolytic digestion with proteinase K.

Results: Using our protocol, PD and MSA could be accurately delineated using proteoform-specific aggregation kinetics, including α-Syn aggregation rate, maximum relative fluorescence, the gradient of amplification, and core protofilament size. MSA cases yielded significantly higher values than PD cases across all four kinetic parameters in brain tissues, with the MSA-cerebellar phenotype having higher maximum relative fluorescence than the MSA-Parkinsonian phenotype. Statistical significance was maintained when the data were analysed regionally and when all regions were grouped.

Conclusions: Our RT-QuIC protocol and analysis pipeline can distinguish between PD and MSA, and between MSA phenotypes. MSA α-Syn seeds induce faster propagation and exhibit higher aggregation kinetics than PD α-Syn, mirroring the biological differences observed in brain tissue. With further validation of these quantitative parameters, we propose that SAAs could advance from a yes/no diagnostic to a theranostic biomarker that could be utilised in developing therapeutics.

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引用次数: 0
Second-generation anti-amyloid monoclonal antibodies for Alzheimer's disease: current landscape and future perspectives.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-27 DOI: 10.1186/s40035-025-00465-w
Byeong-Hyeon Kim, Sujin Kim, Yunkwon Nam, Yong Ho Park, Seong Min Shin, Minho Moon

Alzheimer's disease (AD) is the most common type of dementia. Monoclonal antibodies (MABs) serve as a promising therapeutic approach for AD by selectively targeting key pathogenic factors, such as amyloid-β (Aβ) peptide, tau protein, and neuroinflammation. Specifically, based on their efficacy in removing Aβ plaques from the brains of patients with AD, the U.S. Food and Drug Administration has approved three anti-amyloid MABs, aducanumab (Aduhelm®), lecanemab (Leqembi®), and donanemab (Kisunla™). Notably, lecanemab received traditional approval after demonstrating clinical benefit, supporting the Aβ cascade hypothesis. These MABs targeting Aβ are categorized based on their affinity to diverse conformational features of Aβ, including monomer, fibril, protofibril, and plaque forms of Aβ as well as pyroglutamate Aβ. First-generation MABs targeting the non-toxic monomeric Aβ, such as solanezumab, bapineuzumab, and crenezumab, failed to demonstrate clinical benefit for AD in clinical trials. In contrast, second-generation MABs, including aducanumab, lecanemab, donanemab, and gantenerumab directed against pathogenic Aβ species and aggregates have shown that reducing Aβ deposition can be an effective strategy to slow cognitive impairment in AD. In this review, we provide a comprehensive overview of the current status, mechanisms, outcomes, and limitations of second-generation MABs for the clinical treatment of AD. Moreover, we discuss the perspectives and future directions of anti-amyloid MABs in the treatment of AD.

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引用次数: 0
Correction: Inflammasomes in neurodegenerative diseases.
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-23 DOI: 10.1186/s40035-025-00468-7
Qianchen Wang, Songwei Yang, Xuan Zhang, Shanshan Zhang, Liping Chen, Wanxue Wang, Naihong Chen, Jiaqing Yan
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引用次数: 0
Application of antisense oligonucleotide drugs in amyotrophic lateral sclerosis and Huntington's disease. 反义寡核苷酸药物在肌萎缩性侧索硬化和亨廷顿病中的应用。
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-21 DOI: 10.1186/s40035-025-00466-9
Kaili Ou, Qingqing Jia, Dandan Li, Shihua Li, Xiao-Jiang Li, Peng Yin

Amyotrophic lateral sclerosis (ALS) and Huntington's disease (HD) are diverse in clinical presentation and are caused by complex and multiple factors, including genetic mutations and environmental factors. Numerous therapeutic approaches have been developed based on the genetic causes and potential mechanisms of ALS and HD. Currently, available treatments for various neurodegenerative diseases can alleviate symptoms but do not provide a definitive cure. Gene therapy, which aims to modify or express specific proteins for neuroprotection or correction, is considered a powerful tool in managing neurodegenerative conditions. To date, antisense oligonucleotide (ASO) drugs targeting the pathological genes associated with ALS and HD have shown promising results in numerous animal studies and several clinical trials. This review provides a comprehensive overview of the development, mechanisms of action, limitations, and clinical applications of ASO drugs in neurodegenerative diseases, with a specific focus on ALS and HD therapeutic strategies.

肌萎缩性侧索硬化症(ALS)和亨廷顿舞蹈病(HD)的临床表现多样,是由复杂的多种因素引起的,包括基因突变和环境因素。基于ALS和HD的遗传原因和潜在机制,已经开发了许多治疗方法。目前,对各种神经退行性疾病的现有治疗方法可以减轻症状,但不能提供明确的治愈方法。基因治疗,其目的是修改或表达特定蛋白质的神经保护或纠正,被认为是管理神经退行性疾病的有力工具。迄今为止,针对ALS和HD相关病理基因的反义寡核苷酸(ASO)药物在大量动物研究和一些临床试验中显示出令人鼓舞的结果。本文综述了ASO药物在神经退行性疾病中的发展、作用机制、局限性和临床应用,重点介绍了ALS和HD的治疗策略。
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引用次数: 0
Correction: CD2AP deficiency aggravates Alzheimer's disease phenotypes and pathology through p38 MAPK activation. 更正:CD2AP缺乏通过p38 MAPK激活加重阿尔茨海默病的表型和病理。
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-17 DOI: 10.1186/s40035-024-00464-3
Yan-Yan Xue, Zhe-Sheng Zhang, Rong-Rong Lin, Hui-Fen Huang, Ke-Qing Zhu, Dian-Fu Chen, Zhi-Ying Wu, Qing-Qing Tao
{"title":"Correction: CD2AP deficiency aggravates Alzheimer's disease phenotypes and pathology through p38 MAPK activation.","authors":"Yan-Yan Xue, Zhe-Sheng Zhang, Rong-Rong Lin, Hui-Fen Huang, Ke-Qing Zhu, Dian-Fu Chen, Zhi-Ying Wu, Qing-Qing Tao","doi":"10.1186/s40035-024-00464-3","DOIUrl":"https://doi.org/10.1186/s40035-024-00464-3","url":null,"abstract":"","PeriodicalId":23269,"journal":{"name":"Translational Neurodegeneration","volume":"14 1","pages":"3"},"PeriodicalIF":10.8,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11740521/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143012285","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Cerebrospinal fluid cyclase-associated protein 2 is increased in Alzheimer's disease and correlates with tau pathology. 脑脊液环化酶相关蛋白2在阿尔茨海默病中升高并与tau病理相关。
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-16 DOI: 10.1186/s40035-024-00462-5
Alessandro Padovani, Andrea Pilotto, Silvia Pelucchi, Laura D'Andrea, Ramona Stringhi, Federica Gorla, Bahar Aksan, Salvatore Caratozzolo, Alberto Benussi, Alice Galli, Clara Tirloni, Daniela Mauceri, Antonio Canale, Silvana Archetti, Barbara Borroni, Monica Di Luca, Elena Marcello
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引用次数: 0
Peripheral proteinopathy in neurodegenerative diseases. 神经退行性疾病中的外周蛋白病。
IF 10.8 1区 医学 Q1 NEUROSCIENCES Pub Date : 2025-01-16 DOI: 10.1186/s40035-024-00461-6
Bin Xu, Xia Lei, Ying Yang, Jiayi Yu, Jun Chen, Zhi Xu, Keqiang Ye, Jing Zhang

Proteinopathies in neurology typically refer to pathological changes in proteins associated with neurological diseases, such as the aggregation of amyloid β and Tau in Alzheimer's disease, α-synuclein in Parkinson's disease and multiple system atrophy, and TAR DNA-binding protein 43 in amyotrophic lateral sclerosis and frontotemporal dementia. Interestingly, these proteins are also commonly found in peripheral tissues, raising important questions about their roles in neurological disorders. Multiple studies have shown that peripherally derived pathological proteins not only travel to the brain through various routes, aggravating brain pathology, but also contribute significantly to peripheral dysfunction, highlighting their crucial impact on neurological diseases. Investigating how these peripherally derived proteins influence the progression of neurological disorders could open new horizons for achieving early diagnosis and treatment. This review summarizes the distribution, transportation pathways, and pathogenic mechanisms of several neurodegenerative disease-related pathological proteins in the periphery, proposing that targeting these peripheral pathological proteins could be a promising strategy for preventing and managing neurological diseases.

神经学中的蛋白质病变通常是指与神经系统疾病相关的蛋白质的病理改变,如阿尔茨海默病中淀粉样蛋白β和Tau的聚集,帕金森病和多系统萎缩中的α-突触核蛋白,肌萎缩侧索硬化症和额颞叶痴呆中的TAR dna结合蛋白43。有趣的是,这些蛋白质也普遍存在于外周组织中,这就提出了它们在神经系统疾病中所起作用的重要问题。多项研究表明,外周来源的病理蛋白不仅通过多种途径进入大脑,加重大脑病理,而且还对外周功能障碍有重要贡献,突出了它们在神经系统疾病中的重要作用。研究这些外周来源的蛋白质如何影响神经系统疾病的进展,可以为实现早期诊断和治疗开辟新的视野。本文综述了几种神经退行性疾病相关的外周病理蛋白的分布、转运途径和致病机制,提出靶向这些外周病理蛋白可能是预防和治疗神经系统疾病的一种有前途的策略。
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Translational Neurodegeneration
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