Bibliographies thématiques / Cerebrospinal fluid, amyotrophic lateral sclerosis, microrna / Articles de revues

Articles de revues sur le sujet « Cerebrospinal fluid, amyotrophic lateral sclerosis, microrna »

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Auteur : Grafiati
Publié le 10 mars 2023

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1

Ricci, Claudia, Carlotta Marzocchi et Stefania Battistini. « MicroRNAs as Biomarkers in Amyotrophic Lateral Sclerosis ». Cells 7, no 11 (20 novembre 2018) : 219. http://dx.doi.org/10.3390/cells7110219.

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Amyotrophic lateral sclerosis (ALS) is an incurable and fatal disorder characterized by the progressive loss of motor neurons in the cerebral cortex, brain stem, and spinal cord. Sporadic ALS form accounts for the majority of patients, but in 1–13.5% of cases the disease is inherited. The diagnosis of ALS is mainly based on clinical assessment and electrophysiological examinations with a history of symptom progression and is then made with a significant delay from symptom onset. Thus, the identification of biomarkers specific for ALS could be of a fundamental importance in the clinical practice. An ideal biomarker should display high specificity and sensitivity for discriminating ALS from control subjects and from ALS-mimics and other neurological diseases, and should then monitor disease progression within individual patients. microRNAs (miRNAs) are considered promising biomarkers for neurodegenerative diseases, since they are remarkably stable in human body fluids and can reflect physiological and pathological processes relevant for ALS. Here, we review the state of the art of miRNA biomarker identification for ALS in cerebrospinal fluid (CSF), blood and muscle tissue; we discuss advantages and disadvantages of different approaches, and underline the limits but also the great potential of this research for future practical applications.
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Gentile, Giulia, Giovanna Morello, Valentina La Cognata, Maria Guarnaccia, Francesca Luisa Conforti et Sebastiano Cavallaro. « Dysregulated miRNAs as Biomarkers and Therapeutical Targets in Neurodegenerative Diseases ». Journal of Personalized Medicine 12, no 5 (10 mai 2022) : 770. http://dx.doi.org/10.3390/jpm12050770.

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Alzheimer’s disease (AD), Parkinson’s disease (PD), and Amyotrophic Lateral Sclerosis (ALS) are representative neurodegenerative diseases (NDs) characterized by degeneration of selective neurons, as well as the lack of effective biomarkers and therapeutic treatments. In the last decade, microRNAs (miRNAs) have gained considerable interest in diagnostics and therapy of NDs, owing to their aberrant expression and their ability to target multiple molecules and pathways. Here, we provide an overview of dysregulated miRNAs in fluids (blood or cerebrospinal fluid) and nervous tissue of AD, PD, and ALS patients. By emphasizing those that are commonly dysregulated in these NDs, we highlight their potential role as biomarkers or therapeutical targets and describe the use of antisense oligonucleotides as miRNA therapies.
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Eyileten, Ceren, Lucia Sharif, Zofia Wicik, Daniel Jakubik, Joanna Jarosz-Popek, Aleksandra Soplinska, Marek Postula, Anna Czlonkowska, Agnieszka Kaplon-Cieslicka et Dagmara Mirowska-Guzel. « The Relation of the Brain-Derived Neurotrophic Factor with MicroRNAs in Neurodegenerative Diseases and Ischemic Stroke ». Molecular Neurobiology 58, no 1 (17 septembre 2020) : 329–47. http://dx.doi.org/10.1007/s12035-020-02101-2.

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AbstractBrain-derived neurotrophic factor (BDNF) is a member of the neurotrophin family of growth factors that plays a crucial role in the development of the nervous system while supporting the survival of existing neurons and instigating neurogenesis. Altered levels of BDNF, both in the circulation and in the central nervous system (CNS), have been reported to be involved in the pathogenesis of neurodegenerative diseases, including Alzheimer’s disease (AD), Parkinson’s disease (PD), amyotrophic lateral sclerosis (ALS), Huntington’s disease (HD), multiple sclerosis (MS), and ischemic stroke. MicroRNAs (miRNAs) are a class of non-coding RNAs found in body fluids such as peripheral blood and cerebrospinal fluid. Several different miRNAs, and their target genes, are recognized to be involved in the pathophysiology of neurodegenerative and neurovascular diseases. Thus, they present as promising biomarkers and a novel treatment approach for CNS disorders. Currently, limited studies provide viable evidence of miRNA-mediated post-transcriptional regulation of BDNF. The aim of this review is to provide a comprehensive assessment of the current knowledge regarding the potential diagnostic and prognostic values of miRNAs affecting BDNF expression and its role as a CNS disorders and neurovascular disease biomarker. Moreover, a novel therapeutic approach in neurodegenerative diseases and ischemic stroke targeting miRNAs associated with BDNF will be discussed.
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Geekiyanage, Hirosha, Shima Rayatpisheh, James A. Wohlschlegel, Robert Brown et Victor Ambros. « Extracellular microRNAs in human circulation are associated with miRISC complexes that are accessible to anti-AGO2 antibody and can bind target mimic oligonucleotides ». Proceedings of the National Academy of Sciences 117, no 39 (14 septembre 2020) : 24213–23. http://dx.doi.org/10.1073/pnas.2008323117.

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MicroRNAs (miRNAs) function cell-intrinsically to regulate gene expression by base-pairing to complementary mRNA targets while in association with Argonaute, the effector protein of the miRNA-mediated silencing complex (miRISC). A relatively dilute population of miRNAs can be found extracellularly in body fluids such as human blood plasma and cerebrospinal fluid (CSF). The remarkable stability of circulating miRNAs in such harsh extracellular environments can be attributed to their association with protective macromolecular complexes, including extracellular vesicles (EVs), proteins such as Argonaut 2 (AGO2), or high-density lipoproteins. The precise origins and the potential biological significance of various forms of miRNA-containing extracellular complexes are poorly understood. It is also not known whether extracellular miRNAs in their native state may retain the capacity for miRISC-mediated target RNA binding. To explore the potential functionality of circulating extracellular miRNAs, we comprehensively investigated the association between circulating miRNAs and the miRISC Argonaute AGO2. Using AGO2 immunoprecipitation (IP) followed by small-RNA sequencing, we find that miRNAs in circulation are primarily associated with antibody-accessible miRISC/AGO2 complexes. Moreover, we show that circulating miRNAs can base-pair with a target mimic in a seed-based manner, and that the target-bound AGO2 can be recovered from blood plasma in an ∼1:1 ratio with the respective miRNA. Our findings suggest that miRNAs in circulation are largely contained in functional miRISC/AGO2 complexes under normal physiological conditions. However, we find that, in human CSF, the assortment of certain extracellular miRNAs into free miRISC/AGO2 complexes can be affected by pathological conditions such as amyotrophic lateral sclerosis.
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Nakayama, Yui, Satoru Morimoto, Misao Yoneda, Shigeki Kuzuhara et Yasumasa Kokubo. « Cerebrospinal Fluid Biomarkers for Kii Amyotrophic Lateral Sclerosis/Parkinsonism-Dementia Complex ». Journal of Neurodegenerative Diseases 2013 (27 mars 2013) : 1–4. http://dx.doi.org/10.1155/2013/679089.

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Objective. Amyotrophic lateral sclerosis/parkinsonism-dementia complex is classified as one of the tauopathies. Methods. The total tau, phosphorylated tau, and amyloid β42 levels were assayed in cerebrospinal fluid from patients with Kii amyotrophic lateral sclerosis/parkinsonism-dementia complex (), Alzheimer’s disease (), Parkinson’s disease (), amyotrophic lateral sclerosis (), and controls () using specific enzyme-linked immunosorbent assay methods. Results. Total tau and phosphorylated tau did not increase and amyloid β42 was relatively reduced in Kii amyotrophic lateral sclerosis/parkinsonism-dementia complex. Relatively reduced amyloid β42 might discriminate Kii amyotrophic lateral sclerosis/parkinsonism-dementia complex from amyotrophic lateral sclerosis and Parkinson’s disease, and the ratios of phosphorylated-tau to amyloid β42 could discriminate Kii amyotrophic lateral sclerosis/parkinsonism-dementia complex from Alzheimer’s disease. Conclusions. Cerebrospinal fluid analysis may be useful to differentiate amyotrophic lateral sclerosis/parkinsonism-dementia complex from Alzheimer’s disease, amyotrophic lateral sclerosis, and Parkinson’s disease.
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Matías-Guiu, J., L. Galán, R. García-Ramos, J. A. Barcia et A. Guerrero. « Cerebrospinal fluid cytotoxicity in lateral amyotrophic sclerosis ». Neurología (English Edition) 25, no 6 (2010) : 364–73. http://dx.doi.org/10.1016/s2173-5808(10)70068-7.

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7

Finsterer, Josef, et Bruno Mamoli. « Cerebrospinal fluid filtration in amyotrophic lateral sclerosis ». European Journal of Neurology 6, no 5 (septembre 1999) : 597–600. http://dx.doi.org/10.1046/j.1468-1331.1999.650597.x.

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Brettschneider, Johannes, Karin Widl, Dagmar Schattauer, Albert C. Ludolph et Hayrettin Tumani. « Cerebrospinal fluid erythropoietin (EPO) in amyotrophic lateral sclerosis ». Neuroscience Letters 416, no 3 (avril 2007) : 257–60. http://dx.doi.org/10.1016/j.neulet.2007.02.002.

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Kornhuber, Malte E., et Johannes Kornhuber. « Cerebrospinal fluid amino acids in amyotrophic lateral sclerosis ». Annals of Neurology 31, no 4 (avril 1992) : 449. http://dx.doi.org/10.1002/ana.410310418.

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10

Thompson, Alexander G., Elizabeth Gray, Marie-Laëtitia Thézénas, Philip D. Charles, Samuel Evetts, Michele T. Hu, Kevin Talbot, Roman Fischer, Benedikt M. Kessler et Martin R. Turner. « Cerebrospinal fluid macrophage biomarkers in amyotrophic lateral sclerosis ». Annals of Neurology 83, no 2 (février 2018) : 258–68. http://dx.doi.org/10.1002/ana.25143.

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11

Costa, Júlia, Marta Gromicho, Ana Pronto-Laborinho, Conceição Almeida, Ricardo A. Gomes, Ana C. L. Guerreiro, Abel Oliva, Susana Pinto et Mamede de Carvalho. « Cerebrospinal Fluid Chitinases as Biomarkers for Amyotrophic Lateral Sclerosis ». Diagnostics 11, no 7 (5 juillet 2021) : 1210. http://dx.doi.org/10.3390/diagnostics11071210.

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Amyotrophic lateral sclerosis (ALS) is a neurodegenerative neuromuscular disease that affects motor neurons controlling voluntary muscles. Survival is usually 2–5 years after onset, and death occurs due to respiratory failure. The identification of biomarkers would be very useful to help in disease diagnosis and for patient stratification based on, e.g., progression rate, with implications in therapeutic trials. Neurofilaments constitute already-promising markers for ALS and, recently, chitinases have emerged as novel marker targets for the disease. Here, we investigated cerebrospinal fluid (CSF) chitinases as potential markers for ALS. Chitotriosidase (CHIT1), chitinase-3-like protein 1 (CHI3L1), chitinase-3-like protein 2 (CHI3L2) and the benchmark marker phosphoneurofilament heavy chain (pNFH) were quantified by an enzyme-linked immunosorbent assay (ELISA) from the CSF of 34 ALS patients and 24 control patients with other neurological diseases. CSF was also analyzed by UHPLC-mass spectrometry. All three chitinases, as well as pNFH, were found to correlate with disease progression rate. Furthermore, CHIT1 was elevated in ALS patients with high diagnostic performance, as was pNFH. On the other hand, CHIT1 correlated with forced vital capacity (FVC). The three chitinases correlated with pNFH, indicating a relation between degeneration and neuroinflammation. In conclusion, our results supported the value of CHIT1 as a diagnostic and progression rate biomarker, and its potential as respiratory function marker. The results opened novel perspectives to explore chitinases as biomarkers and their functional relevance in ALS.
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Krieger, Charles, Thomas L. Perry et Hermann J. Ziltener. « Amyotrophic Lateral Sclerosis : Interleukin-6 Levels in Cerebrospinal Fluid ». Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 19, no 3 (août 1992) : 357–59. http://dx.doi.org/10.1017/s0317167100041998.

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ABSTRACT:Recent observations indicate that antibodies to gangliosides are found in many patients with amyotrophic lateral sclerosis (ALS). If antigen-antibody complexes occur in ALS, elevations of cytokine levels might be expected, among them the cytokine interleukin-6 (IL-6). IL-6 is secreted by activated monocytes and other cell types and is an important mediator of the inflammatory response. We have measured cerebrospinal fluid (CSF) IL-6 levels in patients with ALS and compared them with those in psychiatric and neurodegenerative disorders not believed to be due to immune disorders of the central nervous system. We found no significant differences in CSF IL-6 levels between these groups.
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13

CHEN, YAN, XIAO-HUI LIU, JIAN-JUN WU, HUI-MING REN, JIAN WANG, ZHENG-TONG DING et YU-PING JIANG. « Proteomic analysis of cerebrospinal fluid in amyotrophic lateral sclerosis ». Experimental and Therapeutic Medicine 11, no 6 (31 mars 2016) : 2095–106. http://dx.doi.org/10.3892/etm.2016.3210.

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14

IWASAKI, Y. « Decreased cerebrospinal-fluid superoxide dismutase in amyotrophic lateral sclerosis ». Lancet 342, no 8879 (octobre 1993) : 1118. http://dx.doi.org/10.1016/0140-6736(93)92104-2.

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Gray, Elizabeth, James R. Larkin, Tim D. W. Claridge, Kevin Talbot, Nicola R. Sibson et Martin R. Turner. « The longitudinal cerebrospinal fluid metabolomic profile of amyotrophic lateral sclerosis ». Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration 16, no 7-8 (29 juin 2015) : 456–63. http://dx.doi.org/10.3109/21678421.2015.1053490.

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Galán, L., J. A. Matias-Guiu, A. Guerrero-Sola et J. Matías-Guiu. « Cerebrospinal fluid cytotoxicity in amyotrophic lateral sclerosis and sample size ». Acta Neurologica Scandinavica 136, no 1 (1 juin 2017) : 79. http://dx.doi.org/10.1111/ane.12746.

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Brettschneider, Johannes, Helga Mogel, Vera Lehmensiek, Tino Ahlert, Sigurd Süssmuth, Albert C. Ludolph et Hayrettin Tumani. « Proteome Analysis of Cerebrospinal Fluid in Amyotrophic Lateral Sclerosis (ALS) ». Neurochemical Research 33, no 11 (15 mai 2008) : 2358–63. http://dx.doi.org/10.1007/s11064-008-9742-5.

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de Bustos, F., F. J. Jiménez-Jiménez, J. A. Molina, J. Esteban, A. Guerrero-Sola, M. Zurdo, M. Ortí-Pareja et al. « Cerebrospinal fluid levels of alpha-tocopherol in amyotrophic lateral sclerosis ». Journal of Neural Transmission 105, no 6-7 (9 septembre 1998) : 703–8. http://dx.doi.org/10.1007/s007020050089.

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Meier, D. H., et K. J. Schott. « Free amino acid pattern of cerebrospinal fluid in amyotrophic lateral sclerosis ». Acta Neurologica Scandinavica 77, no 1 (mars 1988) : 50–53. http://dx.doi.org/10.1111/j.1600-0404.1988.tb06973.x.

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Galán, L., J. Matías-Guiu, J. A. Matias-Guiu, M. Yáñez, V. Pytel, A. Guerrero-Sola, A. Vela-Souto, J. A. Arranz-Tagarro, U. Gómez-Pinedo et A. G. García. « Cerebrospinal fluid cytotoxicity does not affect survival in amyotrophic lateral sclerosis ». Acta Neurologica Scandinavica 136, no 3 (29 décembre 2016) : 212–16. http://dx.doi.org/10.1111/ane.12717.

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Ranganathan, Srikanth, Eric Williams, Philip Ganchev, Vanathi Gopalakrishnan, David Lacomis, Leo Urbinelli, Kristyn Newhall, Merit E. Cudkowicz, Robert H. Brown et Robert Bowser. « Proteomic profiling of cerebrospinal fluid identifies biomarkers for amyotrophic lateral sclerosis ». Journal of Neurochemistry 95, no 5 (29 septembre 2005) : 1461–71. http://dx.doi.org/10.1111/j.1471-4159.2005.03478.x.

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Zetterberg, H., J. Jacobsson, L. Rosengren, K. Blennow et P. M. Andersen. « Cerebrospinal fluid neurofilament light levels in amyotrophic lateral sclerosis : impact ofSOD1genotype ». European Journal of Neurology 14, no 12 (28 septembre 2007) : 1329–33. http://dx.doi.org/10.1111/j.1468-1331.2007.01972.x.

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Iłżecka, J. « Cerebrospinal fluid Flt3 ligand level in patients with amyotrophic lateral sclerosis ». Acta Neurologica Scandinavica 114, no 3 (septembre 2006) : 205–9. http://dx.doi.org/10.1111/j.1600-0404.2006.00704.x.

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Perry, Thomas L., Charles Krieger, Shirley Hansen et Andrew Eisen. « Amyotrophic lateral sclerosis : Amino acid levels in plasma and cerebrospinal fluid ». Annals of Neurology 28, no 1 (juillet 1990) : 12–17. http://dx.doi.org/10.1002/ana.410280105.

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Ilzecka, J. « Decreased cerebrospinal fluid cGMP levels in patients with amyotrophic lateral sclerosis ». Journal of Neural Transmission 111, no 2 (1 février 2004) : 167–72. http://dx.doi.org/10.1007/s00702-003-0086-7.

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Toczylowska, Beata, Zygmunt Jamrozik, Adam Liebert et Hubert Kwiecinski. « NMR-based Metabonomics of Cerebrospinal Fluid Applied to Amyotrophic Lateral Sclerosis ». Biocybernetics and Biomedical Engineering 33, no 1 (janvier 2013) : 21–32. http://dx.doi.org/10.1016/s0208-5216(13)70053-6.

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Trojsi, Francesca, Anna Sagnelli, Giovanni Cirillo, Giovanni Piccirillo, Cinzia Femiano, Francesco Izzo, Maria Rosaria Monsurrò et Gioacchino Tedeschi. « Amyotrophic Lateral Sclerosis and Multiple Sclerosis Overlap : A Case Report ». Case Reports in Medicine 2012 (2012) : 1–4. http://dx.doi.org/10.1155/2012/324685.

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The concurrence of amyotrophic lateral sclerosis (ALS) and multiple sclerosis (MS) is extremely rare. We reported the case of a 33-year-old woman with a past history of paresthesias at the right hand, who developed progressive quadriparesis with muscular atrophy of limbs and, finally, bulbar signs and dyspnea. Clinical and neurophysiologic investigations revealed upper and lower motor neuron signs in the bulbar region and extremities, suggesting the diagnosis of ALS. Moreover, magnetic resonance imaging (MRI) and cerebrospinal fluid (CSF) analysis demonstrated 3 periventricular and juxtacortical lesions, hyperintense in T2 and FLAIR sequences, and 3 liquoral immunoglobulin G (IgG) oligoclonal bands, consistent with diagnosis of primary progressive MS (PPMS). This unusual overlap of ALS and MS leads to the discussion of a hypothetical common pathological process of immunological dysfunction in these two disorders, although the role of immune response in ALS remains ambivalent and unclear.
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Mendonça, Deise M. F., Sheila C. S. Martins, Rafael Higashi, Marcelo N. Muscara, Vivaldo Moura Neto, Leila Chimelli et Ana Maria B. Martinez. « Neurofilament heavy subunit in cerebrospinal fluid : A biomarker of amyotrophic lateral sclerosis ? » Amyotrophic Lateral Sclerosis 12, no 2 (4 janvier 2011) : 144–47. http://dx.doi.org/10.3109/17482968.2010.542002.

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Ignjatović, Aleksandar, Zorica Stević, Dragana Lavrnić, Aleksandra Nikolić-Kokić, Duško Blagojević, Mihajlo Spasić et Ivan Spasojević. « Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients ». Amyotrophic Lateral Sclerosis 13, no 4 (16 mars 2012) : 357–62. http://dx.doi.org/10.3109/17482968.2012.665929.

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Dreger, Marie, Robert Steinbach, Markus Otto, Martin R. Turner et Julian Grosskreutz. « Cerebrospinal fluid biomarkers of disease activity and progression in amyotrophic lateral sclerosis ». Journal of Neurology, Neurosurgery & ; Psychiatry 93, no 4 (1 février 2022) : 422–35. http://dx.doi.org/10.1136/jnnp-2021-327503.

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Amyotrophic lateral sclerosis (ALS) is a relentlessly progressive neurodegenerative disease, and only modest disease-modifying strategies have been established to date. Numerous clinical trials have been conducted in the past years, but have been severely hampered by the wide-ranging heterogeneity of both the biological origins and clinical characteristics of the disease. Thus, reliable biomarkers of disease activity are urgently needed to stratify patients into homogenous groups with aligned disease trajectories to allow a more effective design of clinical trial. In this review, the most promising candidate biomarkers in the cerebrospinal fluid (CSF) of patients with ALS will be summarised. Correlations between biomarker levels and clinical outcome parameters are discussed, while highlighting potential pitfalls and intercorrelations of these clinical parameters. Several CSF molecules have shown potential as biomarkers of progression and prognosis, but large, international, multicentric and longitudinal studies are crucial for validation. A more standardised choice of clinical endpoints in these studies, as well as the application of individualised models of clinical progression, would allow the quantification of disease trajectories, thereby allowing a more accurate analysis of the clinical implications of candidate biomarkers. Additionally, a comparative analysis of several biomarkers and ideally the application of a multivariate analysis including comprehensive genotypic, phenotypic and clinical characteristics collectively contributing to biomarker levels in the CSF, could promote their verification. Thus, reliable prognostic markers and markers of disease activity may improve clinical trial design and patient management in the direction of precision medicine.
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Drannik, Anna, Joan Martin, Randy Peterson, Xiaoxing Ma, Fan Jiang et John Turnbull. « Cerebrospinal fluid from patients with amyotrophic lateral sclerosis inhibits sonic hedgehog function ». PLOS ONE 12, no 2 (7 février 2017) : e0171668. http://dx.doi.org/10.1371/journal.pone.0171668.

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Jimenez-Jimenez, F. J., A. Hernanz, S. Medina-Acebron, F. de Bustos, J. M. Zurdo, H. Alonso, I. Puertas, B. Barcenilla, Y. Sayed et F. Cabrera-Valdivia. « Tau protein concentrations in cerebrospinal fluid of patients with amyotrophic lateral sclerosis ». Acta Neurologica Scandinavica 111, no 2 (février 2005) : 114–17. http://dx.doi.org/10.1111/j.1600-0404.2005.00370.x.

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Johansson, Anders, Anders Larsson, Ingela Nygren, Kaj Blennow et Håkan Askmark. « Increased serum and cerebrospinal fluid FGF-2 levels in amyotrophic lateral sclerosis ». NeuroReport 14, no 14 (octobre 2003) : 1867–69. http://dx.doi.org/10.1097/00001756-200310060-00022.

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Watanabe, Shohei, Takashi Kimura, Koichi Suenaga, Sayoko Wada, Kenkichi Tsuda, Shuhei Kasama, Toshio Takaoka, Koji Kajiyama, Masanaka Takeda et Hiroo Yoshikawa. « Decreased chloride levels of cerebrospinal fluid in patients with amyotrophic lateral sclerosis ». Journal of the Neurological Sciences 285, no 1-2 (octobre 2009) : 146–48. http://dx.doi.org/10.1016/j.jns.2009.06.026.

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Siciliano, G., S. Piazza, C. Carlesi, A. Corona, M. Franzini, A. Pompella, G. Malvaldi, M. Mancuso, A. Paolicchi et L. Murri. « Antioxidant capacity and protein oxidation in cerebrospinal fluid of amyotrophic lateral sclerosis ». Journal of Neurology 254, no 5 (11 avril 2007) : 575–80. http://dx.doi.org/10.1007/s00415-006-0301-1.

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Iłżecka, J. « Decreased cerebrospinal fluid cytochrome c levels in patients with amyotrophic lateral sclerosis ». Scandinavian Journal of Clinical and Laboratory Investigation 67, no 3 (janvier 2007) : 264–69. http://dx.doi.org/10.1080/00365510601016105.

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Yang, Biying, Yongshun Wu, Yihao Wang, Huili Yang, Baoxin Du, Wei Di, Xiaotian Xu et Xiaolei Shi. « Cerebrospinal fluid MFG-E8 as a promising biomarker of amyotrophic lateral sclerosis ». Neurological Sciences 41, no 10 (27 avril 2020) : 2915–20. http://dx.doi.org/10.1007/s10072-020-04416-3.

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Iłżecka, Joanna. « Cerebrospinal fluid vascular endothelial growth factor in patients with amyotrophic lateral sclerosis ». Clinical Neurology and Neurosurgery 106, no 4 (septembre 2004) : 289–93. http://dx.doi.org/10.1016/j.clineuro.2003.12.007.

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Greiner, A., Bernd Schmaußer, Klaus Petzold, Hans Krüger et Alexander Marx. « Neuronal targets of serum and cerebrospinal fluid autoantibodies in amyotrophic lateral sclerosis ». Acta Neuropathologica 91, no 1 (1 décembre 1995) : 67–71. http://dx.doi.org/10.1007/s004010050393.

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Tarasiuk, J., K. Kapica-Topczewska, M. Chorąży, A. Borowik-Zaręba, B. Mroczko, J. Kochanowicz et A. Kułakowska. « The comparisons of blood plasma and cerebrospinal fluid S100B protein concentrations in patients with Alzheimer`s disease, amyotrophic lateral sclerosis, and multiple sclerosis ». Progress in Health Sciences 1 (11 juin 2019) : 22–27. http://dx.doi.org/10.5604/01.3001.0013.3690.

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<b>Introduction:</b>S100 calcium-binding protein B (S100B) is a biochemical marker of astroglial damage. <br/><b>Purpose:</b> To assess the pathophysiological implications of S100B concentrations in blood plasma and cerebrospinal fluid of patients with neurodegenerative central nervous system disorders. <br/><b>Materials and Methods:</b> In this study, we determined and compare S100B concentrations in blood plasma and cerebrospinal fluid obtained from subjects diagnosed with Alzheimer's disease (n=20), amyotrophic lateral sclerosis (n=12), multiple sclerosis (n=40) and the reference group (n=20), using enzyme-linked immunosorbent assay. <br/><b>Results:</b> Concentrations of S100B in plasma collected from patients diagnosed with Alzheimer's disease (252,38±183,50 pg/mL) and multiple sclerosis (164,92±250,14 pg/mL) were above laboratory standards, but in patients with amyotrophic lateral sclerosis (53,96±56,92 pg/mL) and the reference group (2,12 pg/mL) were below laboratory norms (N>75 pg/mL). Concentrations of S100B in plasma collected from patients with Alzheimer's disease (252,38±183,50 pg/mL) were significantly higher than in patients with amyotrophic lateral sclerosis (53,96±56,92 pg/mL) (p<0,029). Concentrations of S100B in CSF collected from the reference group (546,96±236,62 pg/mL) and from patients with Alzheimer's disease (587,53±189,57 pg/mL), amyotrophic lateral sclerosis (404,41±179,56 pg/mL), multiple sclerosis (462,03±146,01 pg/mL) were very similar, and none of pairwise comparisons reached statistical significance. <br/><b>Conclusions:</b> Results of our studies indicate the importance of S100B protein concentration assessment in blood in central nervous system disorders differential diagnostics.
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Taskiran, Dilek, Ayse Sagduyu, Nur Yüceyar, Fatma Zehra Kutay et Şakire Pögün. « Increased Cerebrospinal Fluid and Serum Nitrite and Nitrate Levels in Amyotrophic Lateral Sclerosis ». International Journal of Neuroscience 101, no 1-4 (janvier 2000) : 65–72. http://dx.doi.org/10.3109/00207450008986493.

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Shi, Jiaying, Xiaohui Qin, Xueli Chang, Hong Wang, Junhong Guo et Wei Zhang. « Neurofilament markers in serum and cerebrospinal fluid of patients with amyotrophic lateral sclerosis ». Journal of Cellular and Molecular Medicine 26, no 2 (6 décembre 2021) : 583–87. http://dx.doi.org/10.1111/jcmm.17100.

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Annunziata, P., et N. Volpi. « High levels of C3c in the cerebrospinal fluid from amyotrophic lateral sclerosis patients ». Acta Neurologica Scandinavica 72, no 1 (29 janvier 2009) : 61–64. http://dx.doi.org/10.1111/j.1600-0404.1985.tb01548.x.

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Klimek, A., D. Cieślak, J. Szulc-Kuberska et H. Stepien. « Reduced lumbar cerebrospinal fluid corticotropin releasing factor (CRF) levels in amyotrophic lateral sclerosis ». Acta Neurologica Scandinavica 74, no 1 (juillet 1986) : 72–74. http://dx.doi.org/10.1111/j.1600-0404.1986.tb04629.x.

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Kokić, Aleksandra Nikolić, Zorica Stević, Srdjan Stojanović, Duško P. Blagojević, David R. Jones, Sanja Pavlović, Vesna Niketić, Slobodan Apostolski et Mihajlo B. Spasić. « Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients ». Redox Report 10, no 5 (octobre 2005) : 265–70. http://dx.doi.org/10.1179/135100005x70242.

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Zheng, Y., L. Gao, D. Wang et D. Zang. « Elevated levels of ferritin in the cerebrospinal fluid of amyotrophic lateral sclerosis patients ». Acta Neurologica Scandinavica 136, no 2 (1 novembre 2016) : 145–50. http://dx.doi.org/10.1111/ane.12708.

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Pakzad, R., et S. Safiri. « Cerebrospinal fluid cytotoxicity does not affect survival in amyotrophic lateral sclerosis ; Methodological issues ». Acta Neurologica Scandinavica 136, no 1 (1 juin 2017) : 78. http://dx.doi.org/10.1111/ane.12747.

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Grundström, Eva, Dan Lindholm, Anders Johansson, Kaj Blennow et Håkan Askmark. « GDNF but not BDNF is increased in cerebrospinal fluid in amyotrophic lateral sclerosis ». NeuroReport 11, no 8 (juin 2000) : 1781–83. http://dx.doi.org/10.1097/00001756-200006050-00037.

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Fialová, L., J. Švarcová, A. Bartos, P. Ridzoň, I. Malbohan, O. Keller et R. Rusina. « Cerebrospinal fluid and serum antibodies against neurofilaments in patients with amyotrophic lateral sclerosis ». European Journal of Neurology 17, no 4 (24 novembre 2009) : 562–66. http://dx.doi.org/10.1111/j.1468-1331.2009.02853.x.

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Iwasaki, Yasuo, Ken Ikeda, Toshiya Shiojima, Mozomu Tagaya et Masao Kinoshita. « Amyotrophic lateral sclerosis cerebrospinal fluid is not toxic to cultured spinal motor neurons ». Neurological Research 17, no 5 (octobre 1995) : 393–95. http://dx.doi.org/10.1080/01616412.1995.11740349.

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