Longitudinal changes in CSF alpha-synuclein species reflect Parkinson's disease progression
ABSTRACT Background Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease‐modifying therapies. In this article, we investiga...
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| Published in | Movement disorders Vol. 31; no. 10; pp. 1535 - 1542 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Blackwell Publishing Ltd
01.10.2016
Wiley Subscription Services, Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0885-3185 1531-8257 1531-8257 |
| DOI | 10.1002/mds.26754 |
Cover
| Abstract | ABSTRACT
Background
Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease‐modifying therapies. In this article, we investigated the longitudinal changes of CSF α‐synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression.
Methods
We used our newly developed enzyme‐linked immunosorbent assay systems for measuring different forms of α‐synuclein, such as oligomeric‐α‐synuclein, phosphorylated‐α‐synuclein at serine 129, or total‐α‐synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total‐tau, phosphorylated‐tau, Aβ40, and Aβ42) were also measured for this cohort.
Results
Interestingly, total‐α‐synuclein and oligomeric‐α‐synuclein levels significantly increased during the 2‐year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow‐up period, whereas phosphorylated‐α‐synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric‐α‐synuclein/total‐α‐synuclein ratio and a worsening of motor signs, in particular in the postural‐instability and gait‐difficulty dominant PD group. A strong positive correlation between the changes in CSF total‐α‐synuclein and oligomeric‐α‐synuclein during the 2‐year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P < .001).
Conclusion
Our data show that CSF α‐synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society |
|---|---|
| AbstractList | ABSTRACT
Background
Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease‐modifying therapies. In this article, we investigated the longitudinal changes of CSF α‐synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression.
Methods
We used our newly developed enzyme‐linked immunosorbent assay systems for measuring different forms of α‐synuclein, such as oligomeric‐α‐synuclein, phosphorylated‐α‐synuclein at serine 129, or total‐α‐synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total‐tau, phosphorylated‐tau, Aβ40, and Aβ42) were also measured for this cohort.
Results
Interestingly, total‐α‐synuclein and oligomeric‐α‐synuclein levels significantly increased during the 2‐year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow‐up period, whereas phosphorylated‐α‐synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric‐α‐synuclein/total‐α‐synuclein ratio and a worsening of motor signs, in particular in the postural‐instability and gait‐difficulty dominant PD group. A strong positive correlation between the changes in CSF total‐α‐synuclein and oligomeric‐α‐synuclein during the 2‐year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P < .001).
Conclusion
Our data show that CSF α‐synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF α-synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression. We used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of α-synuclein, such as oligomeric-α-synuclein, phosphorylated-α-synuclein at serine 129, or total-α-synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, Aβ , and Aβ ) were also measured for this cohort. Interestingly, total-α-synuclein and oligomeric-α-synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated-α-synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric-α-synuclein/total-α-synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total-α-synuclein and oligomeric-α-synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P < .001). Our data show that CSF α-synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society. Background: Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF α-synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression. Methods: We used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of α-synuclein, such as oligomeric-α-synuclein, phosphorylated-α-synuclein at serine 129, or total-α-synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, Aβ40, and Aβ42) were also measured for this cohort. Results: Interestingly, total-α-synuclein and oligomeric-α-synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated-α-synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric-α-synuclein/total-α-synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total-α-synuclein and oligomeric-α-synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P <.001). Conclusion: Our data show that CSF α-synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. Background Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF [alpha]-synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression. Methods We used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of [alpha]-synuclein, such as oligomeric-[alpha]-synuclein, phosphorylated-[alpha]-synuclein at serine 129, or total-[alpha]-synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n=121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, A[beta]40, and A[beta]42) were also measured for this cohort. Results Interestingly, total-[alpha]-synuclein and oligomeric-[alpha]-synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated-[alpha]-synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric-[alpha]-synuclein/total-[alpha]-synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total-[alpha]-synuclein and oligomeric-[alpha]-synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r=0.84, P<.001). Conclusion Our data show that CSF [alpha]-synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society Background Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF alpha -synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression. Methods We used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of alpha -synuclein, such as oligomeric- alpha -synuclein, phosphorylated- alpha -synuclein at serine 129, or total- alpha -synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n=121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, A beta sub(40), and A beta sub(42)) were also measured for this cohort. Results Interestingly, total- alpha -synuclein and oligomeric- alpha -synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated- alpha -synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric- alpha -synuclein/total- alpha -synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total- alpha -synuclein and oligomeric- alpha -synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r=0.84, P<.001). Conclusion Our data show that CSF alpha -synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. copyright 2016 International Parkinson and Movement Disorder Society Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF α-synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression.BACKGROUNDParkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for disease diagnosis and progression has a key role for developing disease-modifying therapies. In this article, we investigated the longitudinal changes of CSF α-synuclein species in early PD patients and explored the potential use of these species as surrogate biomarkers for PD progression.We used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of α-synuclein, such as oligomeric-α-synuclein, phosphorylated-α-synuclein at serine 129, or total-α-synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, Aβ40 , and Aβ42 ) were also measured for this cohort.METHODSWe used our newly developed enzyme-linked immunosorbent assay systems for measuring different forms of α-synuclein, such as oligomeric-α-synuclein, phosphorylated-α-synuclein at serine 129, or total-α-synuclein in CSF from the longitudinal Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study cohort (n = 121). CSF Alzheimer's disease biomarkers (total-tau, phosphorylated-tau, Aβ40 , and Aβ42 ) were also measured for this cohort.Interestingly, total-α-synuclein and oligomeric-α-synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated-α-synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric-α-synuclein/total-α-synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total-α-synuclein and oligomeric-α-synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P < .001).RESULTSInterestingly, total-α-synuclein and oligomeric-α-synuclein levels significantly increased during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study follow-up period, whereas phosphorylated-α-synuclein at serine 129 levels showed a longitudinal decrease. We have also noted an association between a change of the oligomeric-α-synuclein/total-α-synuclein ratio and a worsening of motor signs, in particular in the postural-instability and gait-difficulty dominant PD group. A strong positive correlation between the changes in CSF total-α-synuclein and oligomeric-α-synuclein during the 2-year Deprenyl and Tocopherol Antioxidative Therapy for Parkinsonism study was also noted (r = 0.84, P < .001).Our data show that CSF α-synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society.CONCLUSIONOur data show that CSF α-synuclein species have a dynamic pattern along the course of the disease, supporting their possible role as progression biomarkers for PD and their link with PD clinical phenotypes. © 2016 International Parkinson and Movement Disorder Society. |
| Author | Ardah, Mustafa Calabresi, Paolo El-Agnaf, Omar M.A. Tokuda, Takahiko Eusebi, Paolo Chiasserini, Davide Parnetti, Lucilla Vaikath, Nishant N. Varghese, Shiji Haque, M. Emdadul Majbour, Nour K. Auinger, Peggy |
| Author_xml | – sequence: 1 givenname: Nour K. surname: Majbour fullname: Majbour, Nour K. organization: Neurological Disorders Research Center, Qatar Biomedical Research Institute (QBRI), Hamad Bin Khalifa University (HBKU), Qatar Foundation, PO Box 5825, Doha, Qatar – sequence: 2 givenname: Nishant N. surname: Vaikath fullname: Vaikath, Nishant N. organization: Neurological Disorders Research Center, Qatar Biomedical Research Institute (QBRI), Hamad Bin Khalifa University (HBKU), Qatar Foundation, PO Box 5825, Doha, Qatar – sequence: 3 givenname: Paolo surname: Eusebi fullname: Eusebi, Paolo organization: Dipartimento di Medicina, Sezione di Neurologia, Università degli Studi di Perugia, Perugia, Italy – sequence: 4 givenname: Davide surname: Chiasserini fullname: Chiasserini, Davide organization: Dipartimento di Medicina, Sezione di Neurologia, Università degli Studi di Perugia, Perugia, Italy – sequence: 5 givenname: Mustafa surname: Ardah fullname: Ardah, Mustafa organization: Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates – sequence: 6 givenname: Shiji surname: Varghese fullname: Varghese, Shiji organization: Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates – sequence: 7 givenname: M. Emdadul surname: Haque fullname: Haque, M. Emdadul organization: Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates – sequence: 8 givenname: Takahiko surname: Tokuda fullname: Tokuda, Takahiko organization: Department of Neurology, Research Institute for Geriatrics, Kyoto Prefectural University of Medicine, Kyoto, Japan – sequence: 9 givenname: Peggy surname: Auinger fullname: Auinger, Peggy organization: Department of Neurology, Center for Human Experimental Therapeutics, University of Rochester School of Medicine and Dentistry, New York, Rochester, USA – sequence: 10 givenname: Paolo surname: Calabresi fullname: Calabresi, Paolo organization: Dipartimento di Medicina, Sezione di Neurologia, Università degli Studi di Perugia, Perugia, Italy – sequence: 11 givenname: Lucilla surname: Parnetti fullname: Parnetti, Lucilla organization: Dipartimento di Medicina, Sezione di Neurologia, Università degli Studi di Perugia, Perugia, Italy – sequence: 12 givenname: Omar M.A. surname: El-Agnaf fullname: El-Agnaf, Omar M.A. email: oelagnaf@qf.org.qa, oelagnaf@qf.org.qa organization: Neurological Disorders Research Center, Qatar Biomedical Research Institute (QBRI), Hamad Bin Khalifa University (HBKU), Qatar Foundation, PO Box 5825, Doha, Qatar |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27548849$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | 2016 International Parkinson and Movement Disorder Society 2016 International Parkinson and Movement Disorder Society. |
| Copyright_xml | – notice: 2016 International Parkinson and Movement Disorder Society – notice: 2016 International Parkinson and Movement Disorder Society. |
| CorporateAuthor | MultiPark: Multidisciplinary research focused on Parkinson's disease Lunds universitet Institutionen för experimentell medicinsk vetenskap Profile areas and other strong research environments Lund University Neural plasticitet och reparation Strategiska forskningsområden (SFO) Department of Experimental Medical Science Faculty of Medicine Strategic research areas (SRA) Medicinska fakulteten Neural Plasticity and Repair Profilområden och andra starka forskningsmiljöer |
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| ISSN | 0885-3185 1531-8257 |
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| Issue | 10 |
| Keywords | DATATOP Parkinson's disease alpha-synuclein biomarkers oligomers |
| Language | English |
| License | http://onlinelibrary.wiley.com/termsAndConditions#vor 2016 International Parkinson and Movement Disorder Society. |
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| Notes | istex:6CD1C7D5C8D1BD5E36EE85A2E52CBC06E402E72E Michael J. Fox Foundation for Parkinson's Research (New York) ark:/67375/WNG-68JN5LFR-6 ArticleID:MDS26754 Nothing to report. Funding agency Relevant conflicts of interests/financial disclosures This study was supported by the Michael J. Fox Foundation for Parkinson's Research (New York). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| PMID | 27548849 |
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| PublicationDate | 2016-10 October 2016 2016-10-00 2016-Oct 20161001 2016-10-01 |
| PublicationDateYYYYMMDD | 2016-10-01 |
| PublicationDate_xml | – month: 10 year: 2016 text: 2016-10 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: Hoboken |
| PublicationTitle | Movement disorders |
| PublicationTitleAlternate | Mov Disord |
| PublicationYear | 2016 |
| Publisher | Blackwell Publishing Ltd Wiley Subscription Services, Inc |
| Publisher_xml | – name: Blackwell Publishing Ltd – name: Wiley Subscription Services, Inc |
| References | el-Agnaf OM, Irvine GB, Guthrie DJ. Conformations of beta-amyloid in solution. J Neurochem 1997;68(1):437-439. Ardah MT, Paleologou KE, Lv G, et al. Ginsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils. Neurobiol Dis 2015;74:89-101. Jankovic J, McDermott M, Carter J, et al. Variable expression of Parkinson's disease: a base-line analysis of the DATATOP cohort. The Parkinson Study Group. Neurology 1990;40(10):1529-1534. Hall S, Surova Y, Öhrfelt A, Zetterberg H, Lindqvist D, Hansson O. CSF biomarkers and clinical progression of Parkinson disease. Neurology 2015;84(1):57-63. El-Agnaf OM, Jakes R, Curran MD, et al. Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett 1998;440(1-2):71-75. Stewart T, Sossi V, Aasly JO, et al. Phosphorylated α-synuclein in Parkinson's disease: correlation depends on disease severity. Acta Neuropathol Commun 2015;3:7. van Dijk KD, Bidinosti M, Weiss A, Raijmakers P, Berendse HW, van de Berg WD. Reduced α-synuclein levels in cerebrospinal fluid in Parkinson's disease are unrelated to clinical and imaging measures of disease severity. Eur J Neurol 2014;21(3):388-394. Domellöf ME, Elgh E, Forsgren L. The relation between cognition and motor dysfunction in drug-naive newly diagnosed patients with Parkinson's disease. Mov Disord 2011;26(12):2183-2189. Compta Y, Valente T, Saura J, et al. Correlates of cerebrospinal fluid levels of oligomeric- and total-α-synuclein in premotor, motor and dementia stages of Parkinson's disease. J Neurol 2015;262(2):294-306. Parnetti L, Chiasserini D, Bellomo G, et al. Cerebrospinal fluid Tau/α-synuclein ratio in Parkinson's disease and degenerative dementias. Mov Disord 2011;26(8):1428-1435. Tokuda T, Salem SA, Allsop D, et al. Decreased alpha-synuclein in cerebrospinal fluid of aged individuals and subjects with Parkinson's disease. Biochem Biophys Res Commun 2006;349(1):162-166. Parnetti L, Farotti L, Eusebi P, et al. Differential role of CSF alpha-synuclein species, tau, and Aβ42 in Parkinson's Disease. Front Aging Neurosci 2014;6:53. Kang JH, Irwin DJ, Chen-Plotkin AS, et al. Association of cerebrospinal fluid β-amyloid 1-42, T-tau, P-tau181, and α-synuclein levels with clinical features of drug-naive patients with early Parkinson disease. JAMA Neurol 2013;70(10):1277-1287. Helwig M, Klinkenberg M, Rusconi R, et al. Brain propagation of transduced α-synuclein involves non-fibrillar protein species and is enhanced in α-synuclein null mice. Brain 2016;139(Pt 3):856-870. Majbour NK, Vaikath NN, van Dijk KD, et al. Oligomeric and phosphorylated alpha-synuclein as potential CSF biomarkers for Parkinson's disease. Mol Neurodegener 2016;11(1):7. Hansson O, Hall S, Ohrfelt A, et al. 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Biochem Soc Trans 2005;33(Pt 5):1106-1110. Forloni G, Artuso V, La Vitola P, Balducci C. Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases. Mov Disord 2016;31(6):771-781. Shaw LM, Vanderstichele H, Knapik-Czajka M, et al. Qualification of the analytical and clinical performance of CSF biomarker analyses in ADNI. Acta Neuropathol 2011;121(5):597-609. Mollenhauer B, Locascio JJ, Schulz-Schaeffer W, Sixel-Döring F, Trenkwalder C, Schlossmacher MG. α-Synuclein and tau concentrations in cerebrospinal fluid of patients presenting with parkinsonism: a cohort study. Lancet Neurol 2011;10(3):230-240. Ardah MT, Paleologou KE, Lv G, et al. Structure activity relationship of phenolic acid inhibitors of α-synuclein fibril formation and toxicity. Front Aging Neurosci 2014;6:197. Prodoehl J, Planetta PJ, Kurani AS, Comella CL, Corcos DM, Vaillancourt DE. Differences in brain activation between tremor- and nontremor-dominant Parkinson disease. JAMA Neurol 2013;70(1):100-106. Parnetti L, Chiasserini D, Persichetti E, et al. Cerebrospinal fluid lysosomal enzymes and alpha-synuclein in Parkinson's disease. Mov Disord 2014;29(8):1019-1027. Barbour R, Kling K, Anderson JP, et al. Red blood cells are the major source of alpha-synuclein in blood. Neurodegener Dis 2008;5(2):55-59. Vaikath NN, Majbour NK, Paleologou KE, et al. Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology. Neurobiol Dis 2015;79:81-99. El-Agnaf OM, Walsh DM, Allsop D. Soluble oligomers for the diagnosis of neurodegenerative diseases. Lancet Neurol 2003;2(8):461-462. Stewart T, Liu C, Ginghina C, et al. Cerebrospinal fluid α-synuclein predicts cognitive decline in Parkinson disease progression in the DATATOP cohort. Am J Pathol 2014;184(4):966-975. Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M. Alpha-synuclein in Lewy bodies. Nature 1997;388(6645):839-840. Jankovic J. 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| References_xml | – reference: Barbour R, Kling K, Anderson JP, et al. Red blood cells are the major source of alpha-synuclein in blood. Neurodegener Dis 2008;5(2):55-59. – reference: Majbour NK, Vaikath NN, van Dijk KD, et al. Oligomeric and phosphorylated alpha-synuclein as potential CSF biomarkers for Parkinson's disease. Mol Neurodegener 2016;11(1):7. – reference: Stewart T, Sossi V, Aasly JO, et al. Phosphorylated α-synuclein in Parkinson's disease: correlation depends on disease severity. Acta Neuropathol Commun 2015;3:7. – reference: El-Agnaf OM, Jakes R, Curran MD, et al. Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett 1998;440(1-2):71-75. – reference: Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M. Alpha-synuclein in Lewy bodies. Nature 1997;388(6645):839-840. – reference: Prodoehl J, Planetta PJ, Kurani AS, Comella CL, Corcos DM, Vaillancourt DE. Differences in brain activation between tremor- and nontremor-dominant Parkinson disease. JAMA Neurol 2013;70(1):100-106. – reference: Tokuda T, Salem SA, Allsop D, et al. Decreased alpha-synuclein in cerebrospinal fluid of aged individuals and subjects with Parkinson's disease. Biochem Biophys Res Commun 2006;349(1):162-166. – reference: Helwig M, Klinkenberg M, Rusconi R, et al. Brain propagation of transduced α-synuclein involves non-fibrillar protein species and is enhanced in α-synuclein null mice. Brain 2016;139(Pt 3):856-870. – reference: El-Agnaf OM, Walsh DM, Allsop D. Soluble oligomers for the diagnosis of neurodegenerative diseases. Lancet Neurol 2003;2(8):461-462. – reference: Parnetti L, Chiasserini D, Persichetti E, et al. Cerebrospinal fluid lysosomal enzymes and alpha-synuclein in Parkinson's disease. Mov Disord 2014;29(8):1019-1027. – reference: Jankovic J, McDermott M, Carter J, et al. Variable expression of Parkinson's disease: a base-line analysis of the DATATOP cohort. The Parkinson Study Group. Neurology 1990;40(10):1529-1534. – reference: Ardah MT, Paleologou KE, Lv G, et al. Structure activity relationship of phenolic acid inhibitors of α-synuclein fibril formation and toxicity. Front Aging Neurosci 2014;6:197. – reference: Hall S, Surova Y, Öhrfelt A, et al. Longitudinal measurements of cerebrospinal fluid biomarkers in Parkinson's disease. Mov Disord 2016;31(6):898-905. – reference: Domellöf ME, Elgh E, Forsgren L. The relation between cognition and motor dysfunction in drug-naive newly diagnosed patients with Parkinson's disease. Mov Disord 2011;26(12):2183-2189. – reference: Parnetti L, Chiasserini D, Bellomo G, et al. Cerebrospinal fluid Tau/α-synuclein ratio in Parkinson's disease and degenerative dementias. Mov Disord 2011;26(8):1428-1435. – reference: Hall S, Surova Y, Öhrfelt A, Zetterberg H, Lindqvist D, Hansson O. CSF biomarkers and clinical progression of Parkinson disease. Neurology 2015;84(1):57-63. – reference: Compta Y, Valente T, Saura J, et al. Correlates of cerebrospinal fluid levels of oligomeric- and total-α-synuclein in premotor, motor and dementia stages of Parkinson's disease. J Neurol 2015;262(2):294-306. – reference: Hansson O, Hall S, Ohrfelt A, et al. Levels of cerebrospinal fluid α-synuclein oligomers are increased in Parkinson's disease with dementia and dementia with Lewy bodies compared to Alzheimer's disease. Alzheimers Res Ther 2014;6(3):25. – reference: Stewart T, Liu C, Ginghina C, et al. Cerebrospinal fluid α-synuclein predicts cognitive decline in Parkinson disease progression in the DATATOP cohort. Am J Pathol 2014;184(4):966-975. – reference: Forloni G, Artuso V, La Vitola P, Balducci C. Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases. Mov Disord 2016;31(6):771-781. – reference: el-Agnaf OM, Irvine GB, Guthrie DJ. Conformations of beta-amyloid in solution. J Neurochem 1997;68(1):437-439. – reference: DATATOP: a multicenter controlled clinical trial in early Parkinson's disease. Parkinson Study Group. Arch Neurol 1989;46(10):1052-1060. – reference: Jankovic J. Parkinson's disease: clinical features and diagnosis. J Neurol Neurosurg Psychiatry 2008;79(4):368-376. – reference: Mollenhauer B, Locascio JJ, Schulz-Schaeffer W, Sixel-Döring F, Trenkwalder C, Schlossmacher MG. α-Synuclein and tau concentrations in cerebrospinal fluid of patients presenting with parkinsonism: a cohort study. Lancet Neurol 2011;10(3):230-240. – reference: Shaw LM, Vanderstichele H, Knapik-Czajka M, et al. Qualification of the analytical and clinical performance of CSF biomarker analyses in ADNI. Acta Neuropathol 2011;121(5):597-609. – reference: Parnetti L, Castrioto A, Chiasserini D, et al. Cerebrospinal fluid biomarkers in Parkinson disease. Nat Rev Neurol 2013;9(3):131-140. – reference: Vaikath NN, Majbour NK, Paleologou KE, et al. Generation and characterization of novel conformation-specific monoclonal antibodies for α-synuclein pathology. Neurobiol Dis 2015;79:81-99. – reference: Paleologou KE, Irvine GB, El-Agnaf OM. Alpha-synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy. Biochem Soc Trans 2005;33(Pt 5):1106-1110. – reference: Kang JH, Irwin DJ, Chen-Plotkin AS, et al. Association of cerebrospinal fluid β-amyloid 1-42, T-tau, P-tau181, and α-synuclein levels with clinical features of drug-naive patients with early Parkinson disease. JAMA Neurol 2013;70(10):1277-1287. – reference: van Dijk KD, Bidinosti M, Weiss A, Raijmakers P, Berendse HW, van de Berg WD. Reduced α-synuclein levels in cerebrospinal fluid in Parkinson's disease are unrelated to clinical and imaging measures of disease severity. Eur J Neurol 2014;21(3):388-394. – reference: Ardah MT, Paleologou KE, Lv G, et al. Ginsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils. Neurobiol Dis 2015;74:89-101. – reference: Blennow K, Biscetti L, Eusebi P, Parnetti L. Cerebrospinal fluid biomarkers in Alzheimer's and Parkinson's diseases-From pathophysiology to clinical practice. Mov Disord 2016;31(6):836-847. – reference: Parnetti L, Farotti L, Eusebi P, et al. Differential role of CSF alpha-synuclein species, tau, and Aβ42 in Parkinson's Disease. 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Background
Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable... Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers for... Background Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable biomarkers... Background: Parkinson's disease (PD) diagnosis is mainly based on clinical criteria, with a high risk of misdiagnosis. The identification of reliable... |
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| SubjectTerms | Aged alpha-synuclein alpha-Synuclein - cerebrospinal fluid Antioxidants - therapeutic use Basic Medicine biomarkers Biomarkers - cerebrospinal fluid DATATOP Disease Progression Female Humans Longitudinal Studies Male Medical and Health Sciences Medicin och hälsovetenskap Medicinska och farmaceutiska grundvetenskaper Middle Aged Movement disorders Neurosciences Neurovetenskaper oligomers Parkinson Disease - cerebrospinal fluid Parkinson Disease - drug therapy Parkinson's disease |
| Title | Longitudinal changes in CSF alpha-synuclein species reflect Parkinson's disease progression |
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