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A systematic review of salivary biomarkers in Parkinson's disease

Neural Regeneration Research 2024年第12期19卷 2613-2625页

作者： Maria Ilenia De Bartolo Daniele Belvisi Romina Mancinelli Matteo Costanzo Claudia Caturano Giorgio Leodori Alfredo Berardelli Giovanni Fabbrini Giorgio Vivacqua IRCCS Neuromed PozzilliItaly Department of Human Neurosciences Sapienza University of RomeRomeItaly Department of Anatomical HistologicalForensic Medicine and Orthopedics SciencesSapienza University of RomeRomeItaly Department of Experimental Morphology and Microscopy-Integrated Research Center(PRAAB)-Campus Biomedico University of Rome RomeItaly

The search fo r reliable and easily accessible biomarkers in Parkinson's disease is receiving a growing emphasis,to detect neurodegeneration from the prodromal phase and to enforce disease-modifying therapies.Despite the need for non-invasively accessible biomarke rs,the majo rity of the studies have pointed to cerebrospinal fluid or peripheral biopsies biomarkers,which require invasive collection procedures.Saliva represents an easily accessible biofluid and an incredibly wide source of molecular biomarkers.In the present study,after presenting the morphological and biological bases for looking at saliva in the search of biomarkers for Parkinson's disease,we systematically reviewed the results achieved so far in the saliva of different cohorts of Parkinson's disease patients.A comprehensive literature search on PubMed and SCOPUS led to the discovery of 289articles.After screening and exclusion,34 relevant articles were derived fo r systematic review.alpha-synuclein,the histopathological hallmark of Parkinson's disease,has been the most investigated Parkinson's disease biomarker in saliva,with oligomeric alphasynuclein consistently found increased in Parkinson's disease patients in comparison to healthy controls,while conflicting results have been reported regarding the levels of total alpha-synuclein and phosphorylated alpha-synuclein,and few studies described an increased oligomeric alpha-synuclein/total alpha-synuclein ratio in Parkinson's disease.Beyond alpha-synuclein,other biomarkers to rgeting diffe rent molecular pathways have been explored in the saliva of Parkinson's disease patients:total tau,phosphorylated tau,amyloid-β1-42(pathological protein aggregation biomarkers);DJ-1,heme-oxygenase-l,metabolites(alte red energy homeostasis biomarkers);MAPLC-3beta(aberrant proteostasis biomarker);cortisol,tumor necrosis factor-alpha(inflammation biomarkers);DNA methylation,miRNA(DNA/RNA defects biomarkers);acetylcholinesterase activity(synaptic and neuronal network dysfunction biomarkers);Raman spectra,proteome,a

关键词： alpha-synuclein amyloid-beta autophagy DJ-1 neurodegeneration neuroinflammation Parkinson's disease salivary biomarkers tau

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Pathological and physiological functional cross-talks ofα-synuclein and tau in the central nervous system

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Neural Regeneration Research 2024年第4期19卷 855-862页

作者： Mingyue Jin Shengming Wang Xiaodie Gao Zhenyou Zou Shinji Hirotsune Liyuan Sun Guangxi Key Laboratory of Brain and Cognitive Neuroscience Guilin Medical University Department of Genetic Disease Research Osaka Metropolitan University Graduate School of Medicine Department of Scientific Research Brain Hospital of Guangxi Zhuang Autonomous Region

α-synuclein and tau are abundant multifunctional brain proteins that are mainly expressed in the presynaptic and axonal compartments of neurons,respectively.Previous works have revealed that intracellular deposition ofα-synuclein and/or tau causes many neurodegenerative disorders,including Alzheimer’s disease and Parkinson’s disease.Despite intense investigation,the normal physiological functions and roles ofα-synuclein and tau are still unclear,owing to the fact that mice with knockout of either of these proteins do not present apparent phenotypes.Interestingly,the co-occurrence ofα-synuclein and tau aggregates was found in post-mortem brains with synucleinopathies and tauopathies,some of which share similarities in clinical manifestations.Furthermore,the direct interaction ofα-synuclein with tau is considered to promote the fibrillization of each of the proteins in vitro and in vivo.On the other hand,our recent findings have revealed thatα-synuclein and tau are cooperatively involved in brain development in a stage-dependent manner.These findings indicate strong cross-talk between the two proteins in physiology and pathology.In this review,we provide a summary of the recent findings on the functional roles ofα-synuclein and tau in the physiological conditions and pathogenesis of neurodegenerative diseases.A deep understanding of the interplay betweenα-synuclein and tau in physiological and pathological conditions might provide novel targets for clinical diagnosis and therapeutic strategies to treat neurodegenerative diseases.

关键词： alpha-synuclein microtubule-associated protein neurodegenerative disease tau

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Roles of neuronal lysosomes in the etiology of Parkinson’s disease

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Neural Regeneration Research 2024年第9期19卷 1981-1983页

作者： Mattia Volta Institute for Biomedicine Eurac ResearchBolzanoItaly

Therapeutic progress in neurodegenerative conditions such as Parkinson’s disease has been hampered by a lack of detailed knowledge of its molecular etiology.The advancements in genetics and genomics have provided fundamental insights into specific protein players and the cellular processes involved in the onset of disease.In this respect,the autophagy-lysosome system has emerged in recent years as a strong point of convergence for genetics,genomics,and pathologic indications,spanning both familial and idiopathic Parkinson’s disease.Most,if not all,genes linked to familial disease are involved,in a regulatory capacity,in lysosome function(e.g.,LRRK2,alpha-synuclein,VPS35,Parkin,and PINK1).Moreover,the majority of genomic loci associated with increased risk of idiopathic Parkinson’s cluster in lysosome biology and regulation(GBA as the prime example).Lastly,neuropathologic evidence showed alterations in lysosome markers in autoptic material that,coupled to the alpha-synuclein proteinopathy that defines the disease,strongly indicate an alteration in functionality.In this Brief Review article,I present a personal perspective on the molecular and cellular involvement of lysosome biology in Parkinson’s pathogenesis,aiming at a larger vision on the events underlying the onset of the disease.The attempts at targeting autophagy for therapeutic purposes in Parkinson’s have been mostly aimed at“indiscriminately”enhancing its activity to promote the degradation and elimination of aggregate protein accumulations,such as alpha-synuclein Lewy bodies.However,this approach is based on the assumption that protein pathology is the root cause of disease,while pre-pathology and pre-degeneration dysfunctions have been largely observed in clinical and pre-clinical settings.In addition,it has been reported that unspecific boosting of autophagy can be detrimental.Thus,it is important to understand the mechanisms of specific autophagy forms and,even more,the adjustment of specific lysosome functionalities.Indeed,lysosomes exert fine signa

关键词： alpha-synuclein autophagy LRRK2 lysosome neuroprotection neurotransmission Parkinson’s disease Rit2 synapse

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Gut-microbiome-brain axis:the crosstalk between the vagus nerve,alpha-synuclein and the brain in Parkinson's disease

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Neural Regeneration Research 2023年第12期18卷 2611-2614页

作者： Júlio César Claudino dos Santos Leandro Freitas Oliveira Felipe Micelli Noleto Camilla Teixeira Pinheiro Gusmão Gerly Anne de Castro Brito Glauce Socorro de Barros Viana Christus University Center-UNICHRISTUS FortalezaCEBrazil Postgraduate Program in Morphofunctional Sciences Federal University of Ceará-UFCFortalezaCEBrazil Universidade Católica de Brasília-UCB BrasíliaDFBrasil Postgraduate Program in Physiology and Pharmacology Department of the Federal University of Ceará-UFC FortalezaCEBrazil Physiology and Pharmacology Department of the Federal University of Ceará-UFC FortalezaCEBrazil

This critical review of the literature shows that there is a close link between the microbiome,the gut,and the brain in Parkinson's disease.The vagus nerve,the main component of the parasympathetic nervous system,is involved in the regulation of immune response,digestion,heart rate,and control of mood.It can detect microbiota metabolites through its afferents,transferring this gut information to the central nervous system.Preclinical and clinical studies have shown the important role played by the gut microbiome and gut-related factors in disease development and progression,as well as treatment responses.These findings suggest that the gut microbiome may be a valuable target for new therapeutic strategies for Parkinson's disease.More studies are needed to better understand the underlying biology and how this axis can be modulated for the patient's benefit.

关键词： alpha-synuclein enteric microbiota gastrointestinal tract Parkinson's disease vagus nerve

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alpha-synuclein seeding shows a wide heterogeneity in multiple system atrophy

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Translational Neurodegeneration 2022年第1期11卷 845-858页

作者： Ivan Martinez-Valbuena Naomi P.Visanji Ain Kim Heather H.C.Lau Raphaella W.L.So Sohaila Alshimemeri Andrew Gao Michael A.Seidman Maria R.Luquin Joel C.Watts Anthony E.Lang Gabor G.Kovacs Tanz Centre for Research in Neurodegenerative Diseases University of TorontoTorontoONCanada Edmond J.Safra Program in PD and the Morton and Gloria Shulman Movement Disorders Clinic Toronto Western HospitalTorontoONCanada Department of Laboratory Medicine and Pathobiology University of TorontoTorontoONCanada Krembil Brain Institute University Health NetworkTorontoONCanada Department of Biochemistry University of TorontoTorontoONCanada Laboratory Medicine Program University Health NetworkTorontoONCanada Department of Neurology Clinica Universidad de NavarraPamplonaNavarraSpain Division of Neurology Department of MedicineKing Saud UniversityRiyadhSaudi Arabia.

Background: Multiple system atrophy (MSA) is a neurodegenerative condition characterized by variable combinations of parkinsonism, autonomic failure, cerebellar ataxia and pyramidal features. Although the distribution of synucleinopathy correlates with the predominant clinical features, the burden of pathology does not fully explain observed differences in clinical presentation and rate of disease progression. We hypothesized that the clinical heterogeneity in MSA is a consequence of variability in the seeding activity of α-synuclein both between different patients and between different brain regions. Methods: The reliable detection of α-synuclein seeding activity derived from MSA using cell-free amplification assays remains challenging. Therefore, we conducted a systematic evaluation of 168 different reaction buffers, using an array of pH and salts, seeded with fully characterized brain homogenates from one MSA and one PD patient. We then validated the two conditions that conferred the optimal ability to discriminate between PD- and MSA-derived samples in a larger cohort of 40 neuropathologically confirmed cases, including 15 MSA. Finally, in a subset of brains, we conducted the first multi-region analysis of seeding behaviour in MSA. Results: Using our novel buffer conditions, we show that the physicochemical factors that govern the in vitro amplification of α-synuclein can be tailored to generate strain-specific reaction buffers that can be used to reliably study the seeding capacity from MSA-derived α-synuclein. Using this novel approach, we were able to sub-categorize the 15 MSA brains into 3 groups: high, intermediate and low seeders. To further demonstrate heterogeneity in α-synuclein seeding in MSA, we conducted a comprehensive multi-regional evaluation of α-synuclein seeding in 13 different regions from 2 high seeders, 2 intermediate seeders and 2 low seeders. Conclusions: We have identified unexpected differences in seed-competent α-synuclein across a cohort of neuropathologically comparable MSA brains.

关键词： alpha-synuclein Multiple system atrophy RT-QuIC Seeding behavior

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Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation

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Neural Regeneration Research 2020年第3期15卷 407-415页

作者： Heather R.Lucas Ricardo D.Fernández Department of Chemistry Virginia Commonwealth University

N-acetylatedα-synuclein(αSyn)has long been established as an intrinsically disordered protein associated with a dysfunctional role in Parkinson’s disease.In recent years,a physiologically relevant,higher order conformation has been identified as a helical tetramer that is tailored by buried hydrophobic interactions and is distinctively aggregation resistant.The canonical mechanism by which the tetramer assembles remains elusive.As novel biochemical approaches,computational methods,pioneering purification platforms,and powerful imaging techniques continue to develop,puzzling information that once sparked debate as to the veracity of the tetramer has now shed light upon this new counterpart inαSyn neurobiology.Nuclear magnetic resonance and computational studies on multimericαSyn structure have revealed that the protein folding propensity is controlled by small energy barriers that enable large scale reconfiguration.Alternatively,familial mutations ablate tetramerization and reconfigure polymorphic fibrillization.In this review,we will discuss the dynamic landscape ofαSyn quaternary structure with a focus on the tetrameric conformation.

关键词： alpha-synuclein amyloid fibrils intrinsically disordered protein multimer N-acetylation oligomer Parkinson’s disease protein folding protein structure tetramer

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Implications of alpha-synuclein nitration at tyrosine 39 in methamphetamine-induced neurotoxicity in vitro and in vivo

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Neural Regeneration Research 2019年第2期14卷 319-327页

作者： Hong-Hua Qiao Lin-Nan Zhu Yue Wang Jia-Liang Hui Wei-Bing Xie Chao Liu Ling Chen Ping-Ming Qiu School of Forensic Medicine Southern Medical University Kingmed Institute for Forensic Science First Clinical Medicine College Southern Medical University Guangzhou Forensic Science Institute Guangdong Province Key Laboratory of Forensic Genetics

Methamphetamine is an amphetamine-type psychostimulant that can damage dopaminergic neurons and cause characteristic pathological changes similar to neurodegenerative diseases such as Parkinson's disease. However, its specific mechanism of action is still unclear. In the present study, we established a Parkinson's disease pathology model by exposing SH-SY5 Y cells and C57 BL/6 J mice to methamphetamine. In vitro experiments were performed with 0, 0.5, 1.0, 1.5, 2.0 or 2.5 mM methamphetamine for 24 hours or 2.0 mM methamphetamine for 0-, 2-, 4-, 8-, 16-, and 24-hour culture of SH-SY5 Y cells. Additional experimental groups of SH-SY5 Y cells were administered a nitric oxide inhibitor, 0.1 mM N-nitro-L-arginine, 1 hour before exposure to 2.0 mM methamphetamine for 24 hours. In vivo experiments: C57 BL/6 J mice were intraperitoneally injected with N-nitro-L-arginine(8 mg/kg), eight times, at intervals of 12 hours. Methamphetamine 15 mg/kg was intraperitoneally injected eight times, at intervals of 12 hours, but 0.5-hour after each N-nitro-L-arginine injection in the combined group. Western blot assay was used to determine the expression of nitric oxide synthase, α-synuclein(α-Syn), 5 G4, nitrated α-synuclein at the residue Tyr39(nT39 α-Syn), cleaved caspase-3, and cleaved poly ADP-ribose polymerase(PARP) in cells and mouse brain tissue. Immunofluorescence staining was conducted to measure the positive reaction of NeuN, nT39 α-Syn and 5 G4. Enzyme linked immunosorbent assay was performed to determine the dopamine levels in the mouse brain. After methamphetamine exposure, α-Syn expression increased; the aggregation of α-Syn 5 G4 increased; nT39 α-Syn, nitric oxide synthase, cleaved caspase-3, and cleaved PARP expression increased in the cultures of SH-SY5 Y cells and in the brains of C57 BL/6 J mice; and dopamine levels were reduced in the mouse brain. These changes were markedly reduced when N-nitro-L-arginine was administered with methamphetamine in both SH-SY5 Y cells and C57 BL/6 J mice. These results suggest that

关键词： nerve regeneration alpha-synuclein nitrated α-synuclein Parkinson's disease methamphetamine N-nitro-L-arginine alpha-synuclein aggregation apoptosis neurotoxicity neural regeneration

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Nanomolar concentration of alpha-synuclein enhances dopaminergic neuronal survival via Akt pathway

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Neural Regeneration Research 2013年第35期8卷 3269-3274页

作者： Ji-Young Kim Beom Seok Jeon Han-Joon Kim Tae-Beom Ahn Department of Neurology Inje University Seoul Paik Hospital Department of Neurology College of Medicine Seoul National University Hospital Department of Neurology Kyung Hee University Medical Center

Although alpha-synuclein is generally thought to have a pathological role in Parkinson＇s disease, accumulative evidence exists that alpha-synuclein has a neuroprotective effect. The aim of this study was to evaluate the effect of extracellular alpha-synuclein on dopaminergic cell survival. We assessed cell viability using the 3-（4,5-dimethyt-thiazol-2-yt）-2,5-diphenyltertazolium bromide （MTT） assay both in undifferentiated SH-SY5Y （SHSY） cells and neuronally-differentiated SH-SY5Y （ndSHSY） cells after 24 hour treatment with monomeric alpha-synuclein at various concentrations （0 [control], 50, 100 nmol/L, 1 IJmol/L）. To determine whether cell viability assessed by MTT assay was affected by cell proliferation, 5-bromo-2＇-deoxyuridine （BrdU） incorporation assay was per- formed. Level of both Akt and phosphorylated Akt was measured using western blot method in ndSHSY cells with or without 24 hour alpha-synuclein treatment. Cell viability was increased in ndSHSY cells at the nanomolar concentration of alpha-synuclein, but not in SHSY cells. Proportion of BrdU-positive ndSHSY cells was decreased in alpha-synuclein-treated group compared with control group. Level of phosphorylated Akt in alpha-synuclein-treated group was higher compared with the control group. Our study shows that extracellular alpha-synuclein at nanomolar concentra- tion benefits dopaminergic cell survival via Akt pathway.

关键词： neural regeneration alpha-synuclein neuronal survival nanomolar extracellular phosphorylatedAkt SH-SY5Y cell neuronal differentiation proliferation dopaminergic 5-bromo-2＇-deoxyuridine grants-supported paper neuroregeneration

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Dihydromyricetin and Salvianolic acid B inhibit alpha-synuclein aggregation and enhance chaperone-mediated autophagy

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Translational Neurodegeneration 2019年第1期8卷 215-229页

作者： Jia-Zhen Wu Mustafa Ardah Caroline Haikal Alexander Svanbergsson Meike Diepenbroek Nishant N.Vaikath Wen Li Zhan-You Wang Tiago F.Outeiro Omar M.El-Agnaf Jia-Yi Li Institute of Neuroscience College of Life and Health SciencesNortheastern UniversityShenyangLiaoningChina Department of Biochemistry College of Medicine and Health SciencesUnited Arab Emirates UniversityPO Box 17666Al-AinUnited Arab Emirates Neural Plasticity and Repair Unit Wallenberg Neuroscience CenterDepartment of Experimental Medical ScienceBMC A1022184 LundSweden Neurological Disorders Research Center Qatar Biomedical Research Institute(QBRI)Hamad Bin Khalifa University(HBKU)Education CityQatar FoundationP.O.Box 5825DohaQatar Institute of Heath Sciences China Medical University110112 ShenyangPeople’s Republic of China Key Laboratory of Maternal-Fetal Medicine of Liaoning Province and Key Laboratory of Obstetrics and Gynecology of Higher Education of Liaoning Province Shengjing Hospital of China Medical UniversityShenyangChina Department of Experimental Neurodegeneration Center for Nanoscale Microscopy and Molecular Physiology of the BrainCenter for Biostructural Imaging of NeurodegenerationUniversity Medical Center Göttingen37073 GöttingenGermany Max Planck Institute for Experimental Medicine GöttingenGermany

Background:Progressive accumulation ofα-synuclein is a key step in the pathological development of Parkinson’s disease.Impaired protein degradation and increased levels ofα-synuclein may trigger a pathological aggregation in vitro and in vivo.The chaperone-mediated autophagy(CMA)pathway is involved in the intracellular degradation processes ofα-synuclein.Dysfunction of the CMA pathway impairsα-synuclein degradation and causes cytotoxicity.Results:In the present study,we investigated the effects on the CMA pathway andα-synuclein aggregation using bioactive ingredients(Dihydromyricetin(DHM)and Salvianolic acid B(Sal B))extracted from natural medicinal plants.In both cell-free and cellular models ofα-synuclein aggregation,after administration of DHM and Sal B,we observed significant inhibition ofα-synuclein accumulation and aggregation.Cells were co-transfected with a Cterminal modifiedα-synuclein(SynT)and synphilin-1,and then treated with DHM(10μM)and Sal B(50μM)16 hours after transfection;levels ofα-synuclein aggregation decreased significantly(68%for DHM and 75%for Sal B).Concomitantly,we detected increased levels of LAMP-1(a marker of lysosomal homeostasis)and LAMP-2A(a key marker of CMA).Immunofluorescence analyses showed increased colocalization between LAMP-1 and LAMP-2A withα-synuclein inclusions after treatment with DHM and Sal B.We also found increased levels of LAMP-1 and LAMP-2A both in vitro and in vivo,along with decreased levels ofα-synuclein.Moreover,DHM and Sal B treatments exhibited anti-inflammatory activities,preventing astroglia-and microglia-mediated neuroinflammation in BAC-α-syn-GFP transgenic mice.Conclusions:Our data indicate that DHM and Sal B are effective in modulatingα-synuclein accumulation and aggregate formation and augmenting activation of CMA,holding potential for the treatment of Parkinson’s disease.

关键词： chaperone-mediated autophagy macroautophagy alpha-synuclein protein aggregation Parkinson disease lysosomal-associated membrane protein

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Beyond the synucleinopathies:alpha synuclein as a driving force in neurodegenerative comorbidities

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Translational Neurodegeneration 2019年第1期8卷 346-358页

作者： Naomi P.Visanji Anthony E.Lang Gabor G.Kovacs Edmond J.Safra program in Parkinson’s disease and the Morton and Gloria Shulman Movement disorders clinic Toronto Western HospitalTorontoOntarioCanada Department of Laboratory Medicine and Pathobiology and Tanz Centre for Research in Neurodegenerative Disease University of TorontoTorontoOntarioCanada Laboratory Medicine Program&Krembil Brain Institute University Health NetworkTorontoOntarioCanada

The fundamental role that alpha-synuclein(aSyn)plays in the pathogenesis of neurodegenerative synucleinopathies,including Parkinson’s disease,dementia with Lewy bodies,and multiple system atrophy,is a well-accepted fact.A wealth of experimental evidence has linked this relatively small but ubiquitously expressed protein to a plethora of cytopathologic mechanisms and suggests that aSyn may be capable of seeding the progressive spread of synucleinopathy throughout the brain.Beyond the synucleinopathies,the abnormal deposition of aSyn is frequently seen in a variety of other neurodegenerative proteinopathies including Alzheimer’s disease.In spite of the fact that the frequency of concomitant aSyn pathology in these disorders is such that it can be considered the rule rather than the exception,the potential role that aSyn may have in these disorders has received relatively little attention.In this article we postulate that aSyn may in fact be a key protein in driving the pathogenic processes in neurodegenerative comorbidities.In addition to reviewing the frequency of concomitant deposition of aSyn in the neurodegenerative proteinopathies,we also consider our current understanding of the interaction of aSyn with other neurodegenerative disease-associated proteins,including tau,TDP-43,amyloid-βand prion protein,in the context of neuropathologic studies describing the anatomical sites of potential concomitant pathology.We conclude that a growing body of evidence,encompassing neuropathology studies in human brain,animal models of concomitant proteinopathies and studies employing sophisticated methods of probing protein-protein interaction,cumulatively suggest that aSyn is well positioned to exert a strong influence on the pathogenesis of the neurodegenerative comorbidities.We hope to stimulate research in this emerging field and consider that future studies exploring the contribution of aSyn to the pathogenic processes in neurodegenerative comorbidities may provide critical information pertaining to diagnosis and the dev

关键词： Amyloid-β alpha-synuclein Alzheimer’s disease Comorbidity Dementia with Lewy bodies Multiple system atrophy Neurodegeneration Parkinson’s disease Prion protein Progressive supranuclear palsy Proteinopathy Tau TDP-43

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