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Journal articles on the topic 'Alpha-Synuclein, Prion Protein, Aggregation'

Author: Grafiati

Published: 14 March 2023

Last updated: 27 July 2025

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1

de Boni, Laura, Aurelia Hays Watson, Ludovica Zaccagnini та ін. "Brain region-specific susceptibility of Lewy body pathology in synucleinopathies is governed by α-synuclein conformations". Acta Neuropathologica 143, № 4 (2022): 453–69. http://dx.doi.org/10.1007/s00401-022-02406-7.

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AbstractThe protein α-synuclein, a key player in Parkinson’s disease (PD) and other synucleinopathies, exists in different physiological conformations: cytosolic unfolded aggregation-prone monomers and helical aggregation-resistant multimers. It has been shown that familial PD-associated missense mutations within the α-synuclein gene destabilize the conformer equilibrium of physiologic α-synuclein in favor of unfolded monomers. Here, we characterized the relative levels of unfolded and helical forms of cytosolic α-synuclein in post-mortem human brain tissue and showed that the equilibrium of α

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Limanaqi, Fiona, Francesca Biagioni, Carla Letizia Busceti, et al. "Phytochemicals Bridging Autophagy Induction and Alpha-Synuclein Degradation in Parkinsonism." International Journal of Molecular Sciences 20, no. 13 (2019): 3274. http://dx.doi.org/10.3390/ijms20133274.

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Among nutraceuticals, phytochemical-rich compounds represent a source of naturally-derived bioactive principles, which are extensively studied for potential beneficial effects in a variety of disorders ranging from cardiovascular and metabolic diseases to cancer and neurodegeneration. In the brain, phytochemicals produce a number of biological effects such as modulation of neurotransmitter activity, growth factor induction, antioxidant and anti-inflammatory activity, stem cell modulation/neurogenesis, regulation of mitochondrial homeostasis, and counteracting protein aggregation through modula

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Chen, Merry, Julie Vincent, Alexis Ezeanii, Saurabh Wakade, Shobha Yerigenahally та Danielle E. Mor. "Heparan sulfate proteoglycans mediate prion-like α-synuclein toxicity in Parkinson’s in vivo models". Life Science Alliance 5, № 11 (2022): e202201366. http://dx.doi.org/10.26508/lsa.202201366.

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Parkinson’s disease (PD) is a debilitating neurodegenerative disorder characterized by progressive motor decline and the aggregation of α-synuclein protein. Growing evidence suggests that α-synuclein aggregates may spread from neurons of the digestive tract to the central nervous system in a prion-like manner, yet the mechanisms of α-synuclein transmission and neurotoxicity remain poorly understood. Animal models that are amenable to high-throughput investigations are needed to facilitate the discovery of disease mechanisms. Here we describe the first Caenorhabditis elegans models in which fee

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Krawczuk, Daria, Magdalena Groblewska, Jan Mroczko, Izabela Winkel та Barbara Mroczko. "The Role of α-Synuclein in Etiology of Neurodegenerative Diseases". International Journal of Molecular Sciences 25, № 17 (2024): 9197. http://dx.doi.org/10.3390/ijms25179197.

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A presynaptic protein called α-synuclein plays a crucial role in synaptic function and neurotransmitter release. However, its misfolding and aggregation have been implicated in a variety of neurodegenerative diseases, particularly Parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. Emerging evidence suggests that α-synuclein interacts with various cellular pathways, including mitochondrial dysfunction, oxidative stress, and neuroinflammation, which contributes to neuronal cell death. Moreover, α-synuclein has been involved in the propagation of neurodegenerative proces

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Iljina, Marija, Gonzalo A. Garcia, Mathew H. Horrocks, et al. "Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading." Proceedings of the National Academy of Sciences 113, no. 9 (2016): E1206—E1215. http://dx.doi.org/10.1073/pnas.1524128113.

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The protein alpha-synuclein (αS) self-assembles into small oligomeric species and subsequently into amyloid fibrils that accumulate and proliferate during the development of Parkinson’s disease. However, the quantitative characterization of the aggregation and spreading of αS remains challenging to achieve. Previously, we identified a conformational conversion step leading from the initially formed oligomers to more compact oligomers preceding fibril formation. Here, by a combination of single-molecule fluorescence measurements and kinetic analysis, we find that the reaction in solution involv

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Medvedeva, Maria, Natalia Kitsilovskaya, Yulia Stroylova, Irina Sevostyanova, Ali Akbar Saboury, and Vladimir Muronetz. "Hydroxycinnamic Acid Derivatives from Coffee Extracts Prevent Amyloid Transformation of Alpha-Synuclein." Biomedicines 10, no. 9 (2022): 2255. http://dx.doi.org/10.3390/biomedicines10092255.

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Earlier we showed that derivatives of hydroxycinnamic acids prevent amyloid transformation of alpha-synuclein and prion protein. The aim of this work was to determine the content of 3-hydroxycinnamic acid derivatives in coffee extracts and to evaluate their activity in relation to alpha-synuclein amyloid aggregation. Hydroxycinnamic acid derivatives were identified in aqueous and ethanol extracts of coffee beans by quantitative mass spectrometric analysis. Only 3,4-dimethoxycinnamic acid (13–53 μg/mL) was detected in significant amounts in the coffee extracts, while ferulic acid was present in

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Prusiner, Stanley B., Amanda L. Woerman, Daniel A. Mordes та ін. "Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism". Proceedings of the National Academy of Sciences 112, № 38 (2015): E5308—E5317. http://dx.doi.org/10.1073/pnas.1514475112.

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Prions are proteins that adopt alternative conformations that become self-propagating; the PrPSc prion causes the rare human disorder Creutzfeldt–Jakob disease (CJD). We report here that multiple system atrophy (MSA) is caused by a different human prion composed of the α-synuclein protein. MSA is a slowly evolving disorder characterized by progressive loss of autonomic nervous system function and often signs of parkinsonism; the neuropathological hallmark of MSA is glial cytoplasmic inclusions consisting of filaments of α-synuclein. To determine whether human α-synuclein forms prions, we exami

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Piccardo, Pedro, Juraj Cervenak, Ming Bu, Lindsay Miller та David M. Asher. "Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys". Journal of General Virology 95, № 7 (2014): 1612–18. http://dx.doi.org/10.1099/vir.0.062083-0.

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Proteins aggregate in several slowly progressive neurodegenerative diseases called ‘proteinopathies’. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well – a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are ‘sporadic’, without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy

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Vaquer-Alicea, Jaime, and Marc I. Diamond. "Propagation of Protein Aggregation in Neurodegenerative Diseases." Annual Review of Biochemistry 88, no. 1 (2019): 785–810. http://dx.doi.org/10.1146/annurev-biochem-061516-045049.

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Most common neurodegenerative diseases feature deposition of protein amyloids and degeneration of brain networks. Amyloids are ordered protein assemblies that can act as templates for their own replication through monomer addition. Evidence suggests that this characteristic may underlie the progression of pathology in neurodegenerative diseases. Many different amyloid proteins, including Aβ, tau, and α-synuclein, exhibit properties similar to those of infectious prion protein in experimental systems: discrete and self-replicating amyloid structures, transcellular propagation of aggregation, an

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Crestini, Alessio, Francesca Santilli, Stefano Martellucci, et al. "Prions and Neurodegenerative Diseases: A Focus on Alzheimer’s Disease." Journal of Alzheimer's Disease 85, no. 2 (2022): 503–18. http://dx.doi.org/10.3233/jad-215171.

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Specific protein misfolding and aggregation are mechanisms underlying various neurodegenerative diseases such as prion disease and Alzheimer’s disease (AD). The misfolded proteins are involved in prions, amyloid-β (Aβ), tau, and α-synuclein disorders; they share common structural, biological, and biochemical characteristics, as well as similar mechanisms of aggregation and self-propagation. Pathological features of AD include the appearance of plaques consisting of deposition of protein Aβ and neurofibrillary tangles formed by the hyperphosphorylated tau protein. Although it is not clear how p

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Austen, Brian M., Joseph M. Sheridan, Omar M. A. El-Agnaf, Hazel Goodwin, and Emma R. Frears. "Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases." Protein & Peptide Letters 7, no. 1 (2000): 1–8. http://dx.doi.org/10.2174/092986650701221205144944.

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P-Amyloid protein, the a-synuclein fragment NAC, and protease-resistant forms of prion proteins are found deposited in the pathological lesions associated with neurodegenerative disease. Chemical syntheses of these proteins are notoriously difficult due to aggregation of the peptides on the resin during synthesis. We report optimised solid-phase syntheses of several amyloid peptides in high yield and >90% initial purity.

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Jan, Asad, Nádia Pereira Gonçalves, Christian Bjerggaard Vaegter, Poul Henning Jensen, and Nelson Ferreira. "The Prion-Like Spreading of Alpha-Synuclein in Parkinson’s Disease: Update on Models and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (2021): 8338. http://dx.doi.org/10.3390/ijms22158338.

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The pathological aggregation of the presynaptic protein α-synuclein (α-syn) and propagation through synaptically coupled neuroanatomical tracts is increasingly thought to underlie the pathophysiological progression of Parkinson’s disease (PD) and related synucleinopathies. Although the precise molecular mechanisms responsible for the spreading of pathological α-syn accumulation in the CNS are not fully understood, growing evidence suggests that de novo α-syn misfolding and/or neuronal internalization of aggregated α-syn facilitates conformational templating of endogenous α-syn monomers in a me

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Longhena, Francesca, Gaia Faustini, Cristina Missale, Marina Pizzi, PierFranco Spano та Arianna Bellucci. "The Contribution ofα-Synuclein Spreading to Parkinson’s Disease Synaptopathy". Neural Plasticity 2017 (2017): 1–15. http://dx.doi.org/10.1155/2017/5012129.

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Synaptopathies are diseases with synapse defects as shared pathogenic features, encompassing neurodegenerative disorders such as Parkinson’s disease (PD). In sporadic PD, the most common age-related neurodegenerative movement disorder, nigrostriatal dopaminergic deficits are responsible for the onset of motor symptoms that have been related toα-synuclein deposition at synaptic sites. Indeed,α-synuclein accumulation can impair synaptic dopamine release and induces the death of nigrostriatal neurons. While in physiological conditions the protein can interact with and modulate synaptic vesicle pr

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Bétemps, Dominique, Jean-Noël Arsac, Simon Nicot, et al. "Protease-Sensitive and -Resistant Forms of Human and Murine Alpha-Synucleins in Distinct Brain Regions of Transgenic Mice (M83) Expressing the Human Mutated A53T Protein." Biomolecules 13, no. 12 (2023): 1788. http://dx.doi.org/10.3390/biom13121788.

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Human neurodegenerative diseases associated with the misfolding of the alpha-synuclein (aS) protein (synucleinopathies) are similar to prion diseases to the extent that lesions are spread by similar molecular mechanisms. In a transgenic mouse model (M83) overexpressing a mutated (A53T) form of human aS, we had previously found that Protein Misfolding Cyclic Amplification (PMCA) triggered the aggregation of aS, which is associated with a high resistance to the proteinase K (PK) digestion of both human and murine aS, a major hallmark of the disease-associated prion protein. In addition, PMCA was

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Singh, Serena, and Mari L. DeMarco. "In Vitro Conversion Assays Diagnostic for Neurodegenerative Proteinopathies." Journal of Applied Laboratory Medicine 5, no. 1 (2019): 142–57. http://dx.doi.org/10.1373/jalm.2019.029801.

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Abstract Background In vitro conversion assays, including real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification (PMCA) techniques, were first developed to study the conversion process of the prion protein to its misfolded, disease-associated conformation. The intrinsic property of prion proteins to propagate their misfolded structure was later exploited to detect subfemtogram quantities of the misfolded protein present in tissues and fluids from humans and animals with transmissible spongiform encephalopathies. Currently, conversion assays are used clinical

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Tabner, B. J., S. Turnbull, N. J. Fullwood, M. German, and D. Allsop. "The production of hydrogen peroxide during early-stage protein aggregation: a common pathological mechanism in different neurodegenerative diseases?" Biochemical Society Transactions 33, no. 4 (2005): 548–50. http://dx.doi.org/10.1042/bst0330548.

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By means of an ESR spin-trapping method, we have shown that Aβ (amyloid β), α-synuclein and various toxic forms of the prion protein all appear to generate H2O2in vitro. A fundamental molecular mechanism underlying the pathogenesis of cell death in several different neurodegenerative diseases could be the direct production of H2O2 during the early stages of protein aggregation.

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Marreiros, Rita, Andreas Müller-Schiffmann, Svenja V. Trossbach та ін. "Disruption of cellular proteostasis by H1N1 influenza A virus causes α-synuclein aggregation". Proceedings of the National Academy of Sciences 117, № 12 (2020): 6741–51. http://dx.doi.org/10.1073/pnas.1906466117.

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Neurodegenerative diseases feature specific misfolded or misassembled proteins associated with neurotoxicity. The precise mechanisms by which protein aggregates first arise in the majority of sporadic cases have remained unclear. Likely, a first critical mass of misfolded proteins starts a vicious cycle of a prion-like expansion. We hypothesize that viruses, having evolved to hijack the host cellular machinery for catalyzing their replication, lead to profound disturbances of cellular proteostasis, resulting in such a critical mass of protein aggregates. Here, we investigated the effect of inf

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Xia, Yuxing, Grace M. Lloyd та Benoit I. Giasson. "Targeted proteolytic products of τ and α-synuclein in neurodegeneration". Essays in Biochemistry 65, № 7 (2021): 905–12. http://dx.doi.org/10.1042/ebc20210028.

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Abstract CNS pathological inclusions comprising τ or α-synuclein (αSyn) define a spectrum of neurodegenerative diseases, and these can often present concurrently in the same individuals. The aggregation of both proteins is clearly associated with neurodegeneration and the deleterious properties of each protein is further supported by mutations in each gene (MAPT and SNCA, respectively) resulting in disease. The initiating events in most sporadic neurodegenerative diseases are still unclear but growing evidence suggests that the aberrant proteolytic cleavage of τ and αSyn results in products th

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Zhytniakivska, Olha, Tanmay Chaturvedi, and Mette Hedegaard Thomsen. "Plant-Based Inhibitors of Protein Aggregation." Biomolecules 15, no. 4 (2025): 481. https://doi.org/10.3390/biom15040481.

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The assembly of amyloidogenic proteins and peptides into toxic oligomeric and fibrillar aggregates is closely connected to the onset and progression of more than 50 protein diseases, such as Alzheimer’s disease, Parkinson’s disease, prion disease, and type 2 diabetes, to name only a few. Considerable research efforts at identifying the therapeutic strategies against these maladies are currently focused on preventing and inhibiting pathogenic protein aggregation by various agents. Plant-based extracts and compounds have emerged as promising sources of potential inhibitors due to their dual role

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Costanzo, Maddalena, and Chiara Zurzolo. "The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration." Biochemical Journal 452, no. 1 (2013): 1–17. http://dx.doi.org/10.1042/bj20121898.

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The misfolding and aggregation of specific proteins is a common hallmark of many neurodegenerative disorders, including highly prevalent illnesses such as Alzheimer's and Parkinson's diseases, as well as rarer disorders such as Huntington's and prion diseases. Among these, only prion diseases are ‘infectious’. By seeding misfolding of the PrPC (normal conformer prion protein) into PrPSc (abnormal disease-specific conformation of prion protein), prions spread from the periphery of the body to the central nervous system and can also be transmitted between individuals of the same or different spe

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Yi, Ling-Xiao, Eng King Tan та Zhi Dong Zhou. "The α-Synuclein Seeding Amplification Assay for Parkinson’s Disease". International Journal of Molecular Sciences 26, № 1 (2025): 389. https://doi.org/10.3390/ijms26010389.

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Parkinson’s disease (PD) is the second most common neurodegenerative disease in the world. Currently, PD is incurable, and the diagnosis of PD mainly relies on clinical manifestations. The central pathological event in PD is the abnormal aggregation and deposition of misfolded α-synuclein (α-Syn) protein aggregates in the Lewy body (LB) in affected brain areas. Behaving as a prion-like seeding, the misfolded α-syn protein can induce and facilitate the aggregation of native unfolded α-Syn protein to aggravate α-Syn protein aggregation, leading to PD progression. Recently, in a blood-based α-Syn

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Villar-Piqué, Anna, Tomás Lopes da Fonseca, Ricardo Sant’Anna та ін. "Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity". Proceedings of the National Academy of Sciences 113, № 42 (2016): E6506—E6515. http://dx.doi.org/10.1073/pnas.1606791113.

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Synucleinopathies are a group of progressive disorders characterized by the abnormal aggregation and accumulation of α-synuclein (aSyn), an abundant neuronal protein that can adopt different conformations and biological properties. Recently, aSyn pathology was shown to spread between neurons in a prion-like manner. Proteins like aSyn that exhibit self-propagating capacity appear to be able to adopt different stable conformational states, known as protein strains, which can be modulated both by environmental and by protein-intrinsic factors. Here, we analyzed these factors and found that the un

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Chen, Merry, та Danielle E. Mor. "Gut-to-Brain α-Synuclein Transmission in Parkinson’s Disease: Evidence for Prion-like Mechanisms". International Journal of Molecular Sciences 24, № 8 (2023): 7205. http://dx.doi.org/10.3390/ijms24087205.

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Parkinson’s disease (PD) is a multifactorial disorder involving both motor and non-motor symptoms caused by the progressive death of distinct neuronal populations, including dopaminergic neurons in the substantia nigra. The deposition of aggregated α-synuclein protein into Lewy body inclusions is a hallmark of the disorder, and α-synuclein pathology has been found in the enteric nervous system (ENS) of PD patients up to two decades prior to diagnosis. In combination with the high occurrence of gastrointestinal dysfunction in early stages of PD, current evidence strongly suggests that some form

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Lo, Chih Hung, Lenny Yi Tong Cheong, and Jialiu Zeng. "Nanoplatforms Targeting Intrinsically Disordered Protein Aggregation for Translational Neuroscience Applications." Nanomaterials 15, no. 10 (2025): 704. https://doi.org/10.3390/nano15100704.

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Intrinsically disordered proteins (IDPs), such as tau, beta-amyloid (Aβ), and alpha-synuclein (αSyn), are prone to misfolding, resulting in pathological aggregation and propagation that drive neurodegenerative diseases, including Alzheimer’s disease (AD), frontotemporal dementia (FTD), and Parkinson’s disease (PD). Misfolded IDPs are prone to aggregate into oligomers and fibrils, exacerbating disease progression by disrupting cellular functions in the central nervous system, triggering neuroinflammation and neurodegeneration. Furthermore, aggregated IDPs exhibit prion-like behavior, acting as

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Pinotsi, Dorothea, Claire H. Michel, Alexander K. Buell та ін. "Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons". Proceedings of the National Academy of Sciences 113, № 14 (2016): 3815–19. http://dx.doi.org/10.1073/pnas.1516546113.

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New strategies for visualizing self-assembly processes at the nanoscale give deep insights into the molecular origins of disease. An example is the self-assembly of misfolded proteins into amyloid fibrils, which is related to a range of neurodegenerative disorders, such as Parkinson's and Alzheimer's diseases. Here, we probe the links between the mechanism of α-synuclein (AS) aggregation and its associated toxicity by using optical nanoscopy directly in a neuronal cell culture model of Parkinson’s disease. Using superresolution microscopy, we show that protein fibrils are taken up by neuronal

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Cehlar, Ondrej, Stefana Njemoga, Marian Horvath, Erik Cizmazia, Zuzana Bednarikova та Exequiel E. Barrera. "Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies". International Journal of Molecular Sciences 25, № 23 (2024): 13049. https://doi.org/10.3390/ijms252313049.

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In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and soli

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Arias-Carrión, Oscar, Magdalena Guerra-Crespo, Francisco J. Padilla-Godínez, Luis O. Soto-Rojas та Elías Manjarrez. "α-Synuclein Pathology in Synucleinopathies: Mechanisms, Biomarkers, and Therapeutic Challenges". International Journal of Molecular Sciences 26, № 11 (2025): 5405. https://doi.org/10.3390/ijms26115405.

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Parkinson’s disease and related synucleinopathies, including dementia with Lewy bodies and multiple system atrophy, are characterised by the pathological aggregation of the α-synuclein (aSyn) protein in neuronal and glial cells, leading to cellular dysfunction and neurodegeneration. This review synthesizes knowledge of aSyn biology, including its structure, aggregation mechanisms, cellular interactions, and systemic influences. We highlight the structural diversity of aSyn aggregates, ranging from oligomers to fibrils, their strain-like properties, and their prion-like propagation. While the r

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Carlson, George A., and Stanley B. Prusiner. "How an Infection of Sheep Revealed Prion Mechanisms in Alzheimer’s Disease and Other Neurodegenerative Disorders." International Journal of Molecular Sciences 22, no. 9 (2021): 4861. http://dx.doi.org/10.3390/ijms22094861.

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Although it is not yet universally accepted that all neurodegenerative diseases (NDs) are prion disorders, there is little disagreement that Alzheimer’s disease (AD), Parkinson’s disease, frontotemporal dementia (FTD), and other NDs are a consequence of protein misfolding, aggregation, and spread. This widely accepted perspective arose from the prion hypothesis, which resulted from investigations on scrapie, a common transmissible disease of sheep and goats. The prion hypothesis argued that the causative infectious agent of scrapie was a novel proteinaceous pathogen devoid of functional nuclei

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Malchiodi-Albedi, Fiorella, Silvia Paradisi, Andrea Matteucci, Claudio Frank, and Marco Diociaiuti. "Amyloid Oligomer Neurotoxicity, Calcium Dysregulation, and Lipid Rafts." International Journal of Alzheimer's Disease 2011 (2011): 1–17. http://dx.doi.org/10.4061/2011/906964.

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Amyloid proteins constitute a chemically heterogeneous group of proteins, which share some biophysical and biological characteristics, the principal of which are the high propensity to acquire an incorrect folding and the tendency to aggregate. A number of diseases are associated with misfolding and aggregation of proteins, although only in some of them—most notably Alzheimer's disease (AD) and transmissible spongiform encephalopathies (TSEs)—a pathogenetic link with misfolded proteins is now widely recognized. Lipid rafts (LRs) have been involved in the pathophysiology of diseases associated

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Sorrentino, Zachary A., та Benoit I. Giasson. "The emerging role of α-synuclein truncation in aggregation and disease". Journal of Biological Chemistry 295, № 30 (2020): 10224–44. http://dx.doi.org/10.1074/jbc.rev120.011743.

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α-Synuclein (αsyn) is an abundant brain neuronal protein that can misfold and polymerize to form toxic fibrils coalescing into pathologic inclusions in neurodegenerative diseases, including Parkinson's disease, Lewy body dementia, and multiple system atrophy. These fibrils may induce further αsyn misfolding and propagation of pathologic fibrils in a prion-like process. It is unclear why αsyn initially misfolds, but a growing body of literature suggests a critical role of partial proteolytic processing resulting in various truncations of the highly charged and flexible carboxyl-terminal region.

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Choi, Jung Il, Hyunjo Lee, Dong Jun Kim, Eun Suk Park, Kyung Yeon Lee та Hui-Jun Yang. "Astemizole, a Second-Generation Histamine H1-Receptor Antagonist, Did Not Attenuate the Aggregation Process of α-Synuclein In Vitro". Biomedicines 12, № 3 (2024): 611. http://dx.doi.org/10.3390/biomedicines12030611.

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The antihistamine astemizole has shown disease-modifying effects in several preclinical disease models of Parkinson’s disease (PD). Astemizole also interacts with an anomalous aggregation of Alzheimer’s disease-related amyloid-β (Aβ) peptide and has inhibitory activity on the human prion protein PrPSc. We hypothesized that the proposed preclinical benefits of astemizole on PD can be associated with the attenuation of pathological α-synuclein (α-syn) aggregation. We tested the effects of astemizole on the fibrillation processes of amyloid peptides using thioflavin T aggregation monitoring, Cong

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Hudák, Anett, and Tamás Letoha. "Endocytic Pathways Unveil the Role of Syndecans in the Seeding and Spreading of Pathological Protein Aggregates: Insights into Neurodegenerative Disorders." International Journal of Molecular Sciences 26, no. 9 (2025): 4037. https://doi.org/10.3390/ijms26094037.

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Alzheimer’s disease and other neurodegenerative disorders are characterized by the accumulation of misfolded proteins, such as amyloid-beta, tau, and α-synuclein, which disrupt neuronal function and contribute to cognitive decline. Heparan sulfate proteoglycans, particularly syndecans, play a pivotal role in the seeding, aggregation, and spreading of toxic protein aggregates through endocytic pathways. Among these, syndecan-3 is particularly critical in regulating the internalization of misfolded proteins, facilitating their propagation in a prion-like manner. This review examines the mechanis

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Cheng, Jingjing, Qingqing Lu, Li Song та Margaret S. Ho. "α-Synuclein Trafficking in Parkinson’s Disease: Insights From Fly and Mouse Models". ASN Neuro 10 (січень 2018): 175909141881258. http://dx.doi.org/10.1177/1759091418812587.

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Protein aggregation and accumulation are common pathological hallmarks in neurodegenerative diseases. To efficiently clear and eliminate such aggregation becomes an important cellular strategy for cell survival. Lewy bodies inclusion and aggregation of α-Synuclein (α-Syn) during the pathogenesis of Parkinson’s disease (PD) serve as a good example and are potentially linked to other pathological PD features such as progressive dopaminergic neuron cell death, behavioral defects, and nonmotor symptoms like anosmia, cognitive impairment, and depression. Years of research have revealed a variety of

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Esteves, A. R., D. M. Arduíno, D. F. F. Silva, C. R. Oliveira, and S. M. Cardoso. "Mitochondrial Dysfunction: The Road to Alpha-Synuclein Oligomerization in PD." Parkinson's Disease 2011 (2011): 1–20. http://dx.doi.org/10.4061/2011/693761.

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While the etiology of Parkinson's disease remains largely elusive, there is accumulating evidence suggesting that mitochondrial dysfunction occurs prior to the onset of symptoms in Parkinson's disease. Mitochondria are remarkably primed to play a vital role in neuronal cell survival since they are key regulators of energy metabolism (as ATP producers), of intracellular calcium homeostasis, of NAD+/NADH ratio, and of endogenous reactive oxygen species production and programmed cell death. In this paper, we focus on mitochondrial dysfunction-mediated alpha-synuclein aggregation. We highlight som

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Cahill, Catherine M., Rozaleen Aleyadeh, Jin Gao, Changning Wang, and Jack T. Rogers. "Alpha-Synuclein in Alcohol Use Disorder, Connections with Parkinson’s Disease and Potential Therapeutic Role of 5’ Untranslated Region-Directed Small Molecules." Biomolecules 10, no. 10 (2020): 1465. http://dx.doi.org/10.3390/biom10101465.

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Alpha-synuclein (α-Syn) is a 140-amino acid (aa) protein encoded by the Synuclein alpha SNCA gene. It is the synaptic protein associated with Parkinson’s disease (PD) and is the most highly expressed protein in the Lewy bodies associated with PD and other alpha synucleopathies, including Lewy body dementia (LBD) and multiple system atrophy (MSA). Iron deposits are present in the core of Lewy bodies, and there are reports suggesting that divalent metal ions including Cu2+ and Fe2+ enhance the aggregation of α-Syn. Differential expression of α-Syn is associated with alcohol use disorder (AUD), a

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Beekes, Michael. "The Neural Gut–Brain Axis of Pathological Protein Aggregation in Parkinson’s Disease and Its Counterpart in Peroral Prion Infections." Viruses 13, no. 7 (2021): 1394. http://dx.doi.org/10.3390/v13071394.

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A neuropathological hallmark of Parkinson’s disease (PD) is the cerebral deposition of abnormally aggregated α-synuclein (αSyn). PD-associated αSyn (αSynPD) aggregates are assumed to act, in a prion-like manner, as proteinaceous nuclei (“seeds”) capable of self-templated propagation. Braak and colleagues put forward the idea of a neural gut-brain axis mediating the centripetal spread of αSynPD pathology from the enteric nervous system (ENS) to the brain in PD. This has sparked great interest and initiated passionate discussions both in support of and opposing the suggested hypothesis. A preced

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Folke, Jonas, Emil Bergholt, Bente Pakkenberg, Susana Aznar, and Tomasz Brudek. "Alpha-Synuclein Autoimmune Decline in Prodromal Multiple System Atrophy and Parkinson’s Disease." International Journal of Molecular Sciences 23, no. 12 (2022): 6554. http://dx.doi.org/10.3390/ijms23126554.

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Multiple-system trophy (MSA) and Parkinson’s Disease (PD) are both progressive, neurodegenerative diseases characterized by neuropathological deposition of aggregated alpha-synuclein (αSyn). The causes behind this aggregation are still unknown. We have reported aberrancies in MSA and PD patients in naturally occurring autoantibodies (nAbs) against αSyn (anti-αSyn-nAbs), which are important partakers in anti-aggregatory processes, immune-mediated clearance, and anti-inflammatory functions. To elaborate further on the timeline of autoimmune aberrancies towards αSyn, we investigated here the Immu

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Yu, Kun-Hua, and Cheng-I. Lee. "Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress." Pharmaceutics 12, no. 11 (2020): 1081. http://dx.doi.org/10.3390/pharmaceutics12111081.

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Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β peptide (Aβ) and α-synuclein. However, the disaggregating ability is unclear in PrP fibrils. In this study, we examined the amyloid fibril-disaggregating activity of quercetin on mouse prion protein (moPrP) and characterized quercetin-bound moPrP fibrils by imaging, proteinase resistance, hemolysis assay, cell viability, and cellular oxidative

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Näsström, Thomas, Jörgen Ådén, Fumina Shibata, Per Ola Andersson та Björn C. G. Karlsson. "A Capped Peptide of the Aggregation Prone NAC 71–82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations". International Journal of Molecular Sciences 21, № 5 (2020): 1629. http://dx.doi.org/10.3390/ijms21051629.

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Although Lewy bodies and Lewy neurites are hallmarks of Parkinson’s disease (PD) and dementia with Lewy bodies (DLB), misfolded α-synuclein oligomers are nowadays believed to be key for the development of these diseases. Attempts to target soluble misfolded species of the full-length protein have been limited so far, probably due to the fast aggregation kinetics and burial of aggregation prone segments in final cross-β-sheet fibrils. A previous characterisation study of fibrils prepared from a capped peptide of the non-amyloid β-component (NAC) 71–82 amino acid stretch of α-synuclein demonstra

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Munoz-Montesino, Carola, Christina Sizun, Mohammed Moudjou, et al. "Generating Bona Fide Mammalian Prions with Internal Deletions." Journal of Virology 90, no. 15 (2016): 6963–75. http://dx.doi.org/10.1128/jvi.00555-16.

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ABSTRACTMammalian prions are PrP proteins with altered structures causing transmissible fatal neurodegenerative diseases. They are self-perpetuating through formation of beta-sheet-rich assemblies that seed conformational change of cellular PrP. Pathological PrP usually forms an insoluble protease-resistant core exhibiting beta-sheet structures but no more alpha-helical content, loosing the three alpha-helices contained in the correctly folded PrP. The lack of a high-resolution prion structure makes it difficult to understand the dynamics of conversion and to identify elements of the protein i

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Bertsch, Uwe, Konstanze F. Winklhofer, Thomas Hirschberger, et al. "Systematic Identification of Antiprion Drugs by High-Throughput Screening Based on Scanning for Intensely Fluorescent Targets." Journal of Virology 79, no. 12 (2005): 7785–91. http://dx.doi.org/10.1128/jvi.79.12.7785-7791.2005.

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ABSTRACT Conformational changes and aggregation of specific proteins are hallmarks of a number of diseases, like Alzheimer's disease, Parkinson's disease, and prion diseases. In the case of prion diseases, the prion protein (PrP), a neuronal glycoprotein, undergoes a conformational change from the normal, mainly alpha-helical conformation to a disease-associated, mainly beta-sheeted scrapie isoform (PrPSc), which forms amyloid aggregates. This conversion, which is crucial for disease progression, depends on direct PrPC/PrPSc interaction. We developed a high-throughput assay based on scanning f

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Naskar, Soumick, and Nidhi Gour. "Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases." Life 13, no. 7 (2023): 1523. http://dx.doi.org/10.3390/life13071523.

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Amyloids were conventionally referred to as extracellular and intracellular accumulation of Aβ42 peptide, which causes the formation of plaques and neurofibrillary tangles inside the brain leading to the pathogenesis in Alzheimer’s disease. Subsequently, amyloid-like deposition was found in the etiology of prion diseases, Parkinson’s disease, type II diabetes, and cancer, which was attributed to the aggregation of prion protein, α-Synuclein, islet amyloid polypeptide protein, and p53 protein, respectively. Hence, traditionally amyloids were considered aggregates formed exclusively by proteins

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Harischandra, Dilshan S., Dharmin Rokad, Matthew L. Neal та ін. "Manganese promotes the aggregation and prion-like cell-to-cell exosomal transmission of α-synuclein". Science Signaling 12, № 572 (2019): eaau4543. http://dx.doi.org/10.1126/scisignal.aau4543.

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The aggregation of α-synuclein (αSyn) is considered a key pathophysiological feature of certain neurodegenerative disorders, collectively termed synucleinopathies. Given that a prion-like, cell-to-cell transfer of misfolded αSyn has been recognized in the spreading of αSyn pathology in synucleinopathies, we investigated the biological mechanisms underlying the propagation of the disease with respect to environmental neurotoxic stress. Considering the potential role of the divalent metal manganese (Mn2+) in protein aggregation, we characterized its effect on αSyn misfolding and transmission in

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Underwood, Rachel, Bing Wang, Christine Carico, Robert H. Whitaker, William J. Placzek та Talene A. Yacoubian. "The GTPase Rab27b regulates the release, autophagic clearance, and toxicity of α-synuclein". Journal of Biological Chemistry 295, № 23 (2020): 8005–16. http://dx.doi.org/10.1074/jbc.ra120.013337.

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α-Synuclein (αsyn) is the primary component of proteinaceous aggregates termed Lewy bodies that pathologically define synucleinopathies including Parkinson's disease (PD) and dementia with Lewy bodies (DLB). αsyn is hypothesized to spread through the brain in a prion-like fashion by misfolded protein forming a template for aggregation of endogenous αsyn. The cell-to-cell release and uptake of αsyn are considered important processes for its prion-like spread. Rab27b is one of several GTPases essential to the endosomal-lysosomal pathway and is implicated in protein secretion and clearance, but i

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O’Day, Danton H. "The Search for a Universal Treatment for Defined and Mixed Pathology Neurodegenerative Diseases." International Journal of Molecular Sciences 25, no. 24 (2024): 13424. https://doi.org/10.3390/ijms252413424.

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The predominant neurodegenerative diseases, Alzheimer’s disease, Parkinson’s disease, dementia with Lewy Bodies, Huntington’s disease, amyotrophic lateral sclerosis, and frontotemporal dementia, are rarely pure diseases but, instead, show a diversity of mixed pathologies. At some level, all of them share a combination of one or more different toxic biomarker proteins: amyloid beta (Aβ), phosphorylated Tau (pTau), alpha-synuclein (αSyn), mutant huntingtin (mHtt), fused in sarcoma, superoxide dismutase 1, and TAR DNA-binding protein 43. These toxic proteins share some common attributes, making t

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Miraglia, Fabiana, and Emanuela Colla. "Microbiome, Parkinson’s Disease and Molecular Mimicry." Cells 8, no. 3 (2019): 222. http://dx.doi.org/10.3390/cells8030222.

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Parkinson’s Disease (PD) is typically classified as a neurodegenerative disease affecting the motor system. Recent evidence, however, has uncovered the presence of Lewy bodies in locations outside the CNS, in direct contact with the external environment, including the olfactory bulbs and the enteric nervous system. This, combined with the ability of alpha-synuclein (αS) to propagate in a prion-like manner, has supported the hypothesis that the resident microbial community, commonly referred to as microbiota, might play a causative role in the development of PD. In this article, we will be revi

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Lashuel, Hilal A., and Peter T. Lansbury. "Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?" Quarterly Reviews of Biophysics 39, no. 2 (2006): 167–201. http://dx.doi.org/10.1017/s0033583506004422.

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1. Introduction 22. What is the significance of the shared structural properties of disease-associated protein fibrils? 32.1 Mechanism of amyloid fibril formation in vitro 62.1.1 In vitro fibril formation involves transient population of ordered aggregates of intermediate stability, or protofibrils 63. Toxic properties of protofibrils 73.1 Protofibrils, rather than fibrils, are likely to be pathogenic 73.2 The toxic protofibril may be a mixture of related species 83.3 Morphological similarities of protofibrils suggest a common mechanism of toxicity 93.4 Are the amyloid diseases a subset of a m

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Uçar, Buket, Nadia Stefanova та Christian Humpel. "Spreading of Aggregated α-Synuclein in Sagittal Organotypic Mouse Brain Slices". Biomolecules 12, № 2 (2022): 163. http://dx.doi.org/10.3390/biom12020163.

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The accumulation of α-synuclein (α-syn) in the brain plays a role in synucleinopathies and it is hypothesized to spread in a prion-like fashion between connected brain regions. In the present study, we aim to investigate this spreading in well-characterized sagittal organotypic whole brain slices taken from postnatal wild type (WT) and transgenic mice overexpressing human α-syn under the promoter of proteolipid protein (PLP). Collagen hydrogels were loaded with monomers of human α-syn, as well as human and mouse pre-formed fibrils (PFFs), to allow local application and slow release. The spread

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Mikalauskaite, Kamile, Mantas Ziaunys, Tomas Sneideris, and Vytautas Smirnovas. "Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity." International Journal of Molecular Sciences 21, no. 23 (2020): 8916. http://dx.doi.org/10.3390/ijms21238916.

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The formation of amyloid fibrils is linked to multiple neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. Despite years of research and countless studies on the topic of such aggregate formation, as well as their resulting structure, the current knowledge is still fairly limited. One of the main aspects prohibiting effective aggregation tracking is the environment’s effect on amyloid-specific dyes, namely thioflavin-T (ThT). Currently, there are only a few studies hinting at ionic strength being one of the factors that modulate the dye’s binding affinity and fluorescen

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Allsop, David, Jennifer Mayes, Susan Moore, Atef Masad, and Brian J. Tabner. "Metal-dependent generation of reactive oxygen species from amyloid proteins implicated in neurodegenerative disease." Biochemical Society Transactions 36, no. 6 (2008): 1293–98. http://dx.doi.org/10.1042/bst0361293.

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Using a method based on ESR spectroscopy and spin-trapping, we have shown that Aβ (amyloid β-peptide) (implicated in Alzheimer's disease), α-synuclein (implicated in Parkinson's disease), ABri (British dementia peptide) (responsible for familial British dementia), certain toxic fragments of the prion protein (implicated in the transmissible spongiform encephalopathies) and the amylin peptide (found in the pancreas in Type 2 diabetes mellitus) all have the common ability to generate H2O2in vitro. Numerous controls (reverse, scrambled and non-toxic peptides) lacked this property. We have also no

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