Journal of Movement Disorders

Review Articles

Drug Repositioning and Repurposing for Disease-Modifying Effects in Parkinson’s Disease: Seong Ho Jeong, Phil Hyu Lee; J Mov Disord. 2025;18(2):113-126. Published online February 7, 2025; DOI: https://doi.org/10.14802/jmd.25008

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Parkinson’s disease (PD) is the second most prevalent neurodegenerative disorder and is characterized by progressive dopaminergic and nondopaminergic neuronal loss and the presence of Lewy bodies, which are primarily composed of aggregated α-synuclein. Despite advancements in symptomatic therapies, such as dopamine replacement and deep brain stimulation, no disease-modifying therapies (DMTs) have been identified to slow or arrest neurodegeneration in patients with PD. Challenges in DMT development include disease heterogeneity, the absence of reliable biomarkers, and the multifaceted pathophysiology of PD, encompassing neuroinflammation, mitochondrial dysfunction, lysosomal impairment, and oxidative stress. Drug repositioning and repurposing strategies using existing drugs for new therapeutic applications offer promising approaches to accelerate the development of DMTs for PD. These strategies minimize time, cost, and risk by using compounds with established safety profiles. Prominent candidates include glucagon-like peptide-1 receptor agonists, dipeptidyl peptidase-4 inhibitors, ambroxol, calcium channel blockers, statins, iron-chelating agents, c-Abl inhibitors, and memantine. Although preclinical and early clinical studies have demonstrated encouraging results, numerous phase III trials have yielded unfavorable outcomes, elucidating the complexity of PD pathophysiology and the need for innovative trial designs. This review evaluates the potential of prioritized repurposed drugs for PD, focusing on their mechanisms, preclinical evidence, and clinical trial outcomes, and highlights the ongoing challenges and opportunities in this field.

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Teneligliptin, a DPP4 inhibitor protects dopaminergic neurons in PD models via inhibiting of oxidative stress and ferroptosis
Linting Huang, Jiakai Pi, Liqin Gu, Zirou Liao, Wenya Wang
European Journal of Pharmacology.2025; 1002: 177782. CrossRef
Deciphering the Janus‐Faced Nature of the Apolipoprotein Superfamily in Parkinsonian Neurodegeneration: Molecular Crosstalk Between the Astroglial Secretome and Neuronal Homeostasis
Yingying Dai, Mingxia Bi, Qian Jiao, Xixun Du, Xi Chen, Chunling Yan, Hong Jiang
Movement Disorders.2025; 40(11): 2299. CrossRef
Glucagon-Like Peptide-1 Receptor Agonists Are Promising for the Treatment of Brain Diseases: an Outlook from the Perspective of Integrative Physiology
N. V. Gulyaeva
Journal of Evolutionary Biochemistry and Physiology.2025; 61(5): 1326. CrossRef
Therapeutic innovation through drug repurposing: A multidimensional approach toward treating Parkinson's disease
Saswati Swagatika Sahoo, Sudhir Kumar Paidesetty, Pratap Kumar Sahu, Swagata Pattanaik, Rambabu Dandela
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α-Synuclein: A Promising Biomarker for Parkinson’s Disease and Related Disorders: Taku Hatano, Ayami Okuzumi, Gen Matsumoto, Taiji Tsunemi, Nobutaka Hattori; J Mov Disord. 2024;17(2):127-137. Published online April 9, 2024; DOI: https://doi.org/10.14802/jmd.24075

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Abstract PDF

Mutations in the SNCA gene, which encodes α-synuclein (α-syn), play a key role in the development of genetic Parkinson’s disease (PD). α-Syn is a major component of Lewy bodies in PD and glial cytoplasmic inclusions in multiple system atrophy (MSA). Rapid eye movement sleep behavior disorder patients often progress to PD, dementia with Lewy bodies, or MSA, which are collectively known as α-synucleinopathies. The loss of dopaminergic neurons with Lewy bodies precedes motor dysfunction in these diseases, but the mechanisms of neurodegeneration due to α-syn aggregation are poorly understood. Monitoring α-syn aggregation in vivo could serve as a diagnostic biomarker and help elucidate pathogenesis, necessitating a simple and accurate detection method. Seed amplification assays (SAAs), such as real-time quaking-induced conversion and protein misfolding cyclic amplification, are used to detect small amounts of abnormally structured α-syn protofibrils, which are central to aggregation. These methods are promising for the early diagnosis of α-synucleinopathy. Differences in α-syn filament structures between α-synucleinopathies, as observed through transmission electron microscopy and cryo-electron microscopy, suggest their role in the pathogenesis of neurodegeneration. SAAs may differentiate between subtypes of α-synucleinopathy and other diseases. Efforts are also being made to identify α-syn from blood using various methods. This review introduces body fluid α-syn biomarkers based on pathogenic α-syn seeds, which are expected to redefine α-synucleinopathy diagnosis and staging, improving clinical research accuracy and facilitating biomarker development.

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Bulat I. Khairutdinov, Diliara R. Khaibrakhmanova, Evgeniia V. Leisi, Ekaterina R. Sidorova, Yegor A. Sofronov, Vladimir I. Muronetz, Yuriy F. Zuev, Igor A. Sedov
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Alpha-Synuclein Neurobiology in Parkinson’s Disease: A Comprehensive Review of Its Role, Mechanisms, and Therapeutic Perspectives
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Ke Xu, Yu Zhang, Yue Shi, Yake Zhang, Chengguang Zhang, Tianjiao Wang, Peizhu Lv, Yan Bai, Shun Wang
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Ultrastructures of α-Synuclein Filaments in Synucleinopathy Brains and Experimental Models: Airi Tarutani, Masato Hasegawa; J Mov Disord. 2024;17(1):15-29. Published online November 22, 2023; DOI: https://doi.org/10.14802/jmd.23213

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Abstract PDF

Intracellular α-synuclein (α-syn) inclusions are a neuropathological hallmark of Lewy body disease (LBD) and multiple system atrophy (MSA), both of which are termed synucleinopathies. LBD is defined by Lewy bodies and Lewy neurites in neurons, while MSA displays glial cytoplasmic inclusions in oligodendrocytes. Pathological α-syn adopts an ordered filamentous structure with a 5–10 nm filament diameter, and this conformational change has been suggested to be involved in the disease onset and progression. Synucleinopathies also exhibit characteristic ultrastructural and biochemical properties of α-syn filaments, and α-syn strains with distinct conformations have been identified. Numerous experimental studies have supported the idea that pathological α-syn self-amplifies and spreads throughout the brain, during which processes the conformation of α-syn filaments may drive the disease specificity. In this review, we summarize the ultrastructural features and heterogeneity of α-syn filaments in the brains of patients with synucleinopathy and in experimental models of seeded α-syn aggregation.

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Positron emission tomography tracers for synucleinopathies
Jie Xiang, Zhentao Zhang, Shengxi Wu, Keqiang Ye
Molecular Neurodegeneration.2025;[Epub] CrossRef
Correlative light and electron microscopy imaging of proteinaceous deposits in cell cultures and brain tissues
Peizhou Jiang, Dennis W. Dickson
Acta Neuropathologica Communications.2025;[Epub] CrossRef
Liganded magnetic nanoparticles for magnetic resonance imaging of α-synuclein
Hope Pan, Melinda Balbirnie, Ke Hou, Naomi S. Sta Maria, Shruti Sahay, Paul Denver, Stefano Lepore, Mychica Jones, Xiaohong Zuo, Chunni Zhu, Hilda Mirbaha, Hedieh Shahpasand-Kroner, Marisa Mekkittikul, Jiahui Lu, Carolyn J. Hu, Xinyi Cheng, Romany Abskhar
npj Parkinson's Disease.2025;[Epub] CrossRef
α-Synuclein: A Promising Biomarker for Parkinson’s Disease and Related Disorders
Taku Hatano, Ayami Okuzumi, Gen Matsumoto, Taiji Tsunemi, Nobutaka Hattori
Journal of Movement Disorders.2024; 17(2): 127. CrossRef
Exploring the Potential of Biomimetic Peptides in Targeting Fibrillar and Filamentous Alpha-Synuclein—An In Silico and Experimental Approach to Parkinson’s Disease
Sophia A. Frantzeskos, Mary A. Biggs, Ipsita A. Banerjee
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Brief communication

Sensitivity of Detecting Alpha-Synuclein Accumulation in the Gastrointestinal Tract and Tissue Volume Examined: Chaewon Shin, Seong-Ik Kim, Sung-Hye Park, Jung Hwan Shin, Chan Young Lee, Han-Kwang Yang, Hyuk-Joon Lee, Seong-Ho Kong, Yun-Suhk Suh, Han-Joon Kim, Beomseok Jeon; J Mov Disord. 2022;15(3):264-268. Published online July 26, 2022; DOI: https://doi.org/10.14802/jmd.22042

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Abstract PDF Supplementary Material

Objective
This study aimed to evaluate whether a larger tissue volume increases the sensitivity of detecting alpha-synuclein (AS) pathology in the gastrointestinal (GI) tract.
Methods
Nine patients with Parkinson’s disease (PD) or idiopathic rapid eye movement sleep disorder (iRBD) who underwent GI operation and had full-depth intestinal blocks were included. All patients were selected from our previous study population. A total of 10 slides (5 serial sections from the proximal and distal blocks) per patient were analyzed.
Results
In previous studies, pathologic evaluation revealed phosphorylated AS (+) in 5/9 patients (55.6%) and in 1/5 controls (20.0%); in this extensive examination, this increased to 8/9 patients (88.9%) but remained the same in controls (20.0%). The severity and distribution of positive findings were similar between patients with iRBD and PD.
Conclusion
Examining a large tissue volume increased the sensitivity of detecting AS accumulation in the GI tract.

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Gut-initiated alpha synuclein fibrils drive parkinsonism phenotypes: temporal mapping of REM sleep behavior disorder-like and other non-motor symptoms
Daniel Dautan, Wojciech Paslawski, Sergio G. Montejo, Daniel C. Doyon, Valentina I. Brioschi, Roberta Marongiu, Michael G. Kaplitt, Rong Chen, Valina L. Dawson, Xiaoqun Zhang, Ted M. Dawson, Per Svenningsson
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Journal of Parkinson’s Disease.2024; 14(4): 823. CrossRef

Review Article

Mechanism of Anti-α-Synuclein Immunotherapy: Jun Sung Lee, Seung-Jae Lee; J Mov Disord. 2016;9(1):14-19. Published online January 25, 2016; DOI: https://doi.org/10.14802/jmd.15059

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Abstract PDF

Immunization therapy targeting α-synuclein has emerged as a promising approach for Parkinson’s disease and perhaps for other synucleinopathies. Several antibodies have shown therapeutic effects in mouse models of synucleinopathies and have alleviated the pathological and behavioral phenotypes of these mice. The mechanisms through which the immunization therapy works were initially puzzling, especially given that α-synuclein is a typical cytosolic protein. Recent studies, however, suggested that extracellular α-synuclein is an important pathogenic entity, and hence, a target for immunotherapy. Here, we review the literature describing immunization therapy for synucleinopathies in mouse models and provide current thoughts on the potential mechanisms underlying the therapeutic effects of α-synuclein immunotherapy.

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