There are a variety of types of amyotrophic lateral sclerosis (ALS). Most patients with ALS (90%) are classified into the sporadic type (SALS) without heredity. 5% of SALS and 3%of familial type (FALS) are caused by mutations in the 43-kDa trans-activating response region DNA-binding protein (TDP-43). 20%of FALS are caused by the mutation of Cu, Zn superoxide dismutase (SOD1). Superoxide dismutases (SODs) catalyze the dismutation which reaction breaks down harmful radicals into non-reactive molecules in the cells. Mutated SOD1 leads to the production of ROS that causes neuronal death. Recently, a number of new causal factors have been found to link to the pathogenesis of ALS. Characteristic pathological mechanism of ALS is the function of cytosolic protein aggregates. Normal cell functions are disturbed in the cytosol and lead to abnormal cellular processes such as oxidative stress, excitotoxicity, mitochondrial dysfunction. Matrix metalloproteinases (MMPs) and Tissue inhibitors of metalloproteinases (TIMPs) process physiological tissue remodeling and pathological conditions, both of which include vascular and fibrotic regenerations, angiogenesis and destructive diseases such as ALS and cancers. The Receptor for Advanced Glycation End Products (RAGE) plays an important role in ALS causing inflammation oxidative stress and cellular dysfunction. RAGE is also expressed in neurons, vascular cells, microglia, and astrocytes in the central nervous system (CNS). β-N-methylamino-L-alanine (BMAA) is a potential environmental factor in ALS, which is derived from the cycad plant synthesized by cyanobacteria. BMAA is consumed mainly as cycad flour. Dysfunction of these factors are closely associated with nuclear factor-κB (NF-κB) and activator protein-1 (AP-1) The drugs that suppress activated NF-κB are currently thalidomide, celecoxib and valproic acid. These drugs might slow down the exacerbation of ALS as they are effective for cancers.
| Published in | American Journal of Biomedical and Life Sciences (Volume 10, Issue 5) |
| DOI | 10.11648/j.ajbls.20221005.13 |
| Page(s) | 146-154 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2022. Published by Science Publishing Group |
Amyotrophic Lateral Sclerosis, Thalidomide, Celecoxib, Valproic Acid, Probiotics
| [1] | Younus H. Therapeutic potentials of superoxide dismutase. Int J Health Sci (Qassim). 2018; 12 (3): 88-93. |
| [2] | Frakes AE, Ferraiuolo L, Haidet-Phillips AM. Microglia induce motor neuron death via the classical NF-κB pathway in amyotrophic lateral sclerosis. Neuron. 2014; 81 (5): 1009-1023. |
| [3] | Redler RL, Dokholyan NV. The complex molecular biology of amyotrophic lateral sclerosis (ALS). Prog Mol Biol Transl Sci. 2012; 107: 215-262. |
| [4] | Philips T, Robberecht W. Neuroinflammation in amyotrophic lateral sclerosis: role of glial activation in motor neuron disease. Lancet Neurol. 2011 Mar; 10 (3): 253-63. |
| [5] | Small CD, Crawford BD. Matrix metalloproteinases in neural development: a phylogenetically diverse perspective. Neural Regen Res. 2016 Mar; 11 (3): 357-62. |
| [6] | Łukaszewicz-Zając M, Mroczko B, Słowik A. Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in amyotrophic lateral sclerosis (ALS). J Neural Transm (Vienna). 2014 Nov; 121 (11): 1387-97. |
| [7] | Pinet K, McLaughlin KA. Mechanisms of physiological tissue remodeling in animals: Manipulating tissue, organ, and organism morphology. Dev Biol. 2019 Jul 15; 451 (2): 134-145. |
| [8] | Singh D, Srivastava SK, Chaudhuri TK. Multifaceted role of matrix metalloproteinases (MMPs). Front Mol Biosci. 2015 May 13; 2: 19. |
| [9] | Yabluchanskiy A, Ma Y, Iyer RP, Hall ME. Matrix metalloproteinase-9: Many shades of function in cardiovascular disease. Physiology (Bethesda). 2013 Nov; 28 (6): 391-403. |
| [10] | Cui N, Hu M, Khalil RA. Biochemical and Biological Attributes of Matrix Metalloproteinases. Prog Mol Biol Transl Sci. 2017; 147: 1-73. |
| [11] | Chang C, Werb Z. The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol. 2001 Nov; 11 (11): S37-43. |
| [12] | Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci. 2002 Oct 1; 115 (Pt 19): 3719-27. |
| [13] | Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 2003 May 2; 92 (8): 827-39. |
| [14] | Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta. 2010 Jan; 1803 (1): 55-71. |
| [15] | Halade GV, Jin YF, Lindsey ML. Matrix metalloproteinase (MMP)-9: a proximal biomarker for cardiac remodeling and a distal biomarker for inflammation. Pharmacol Ther. 2013 Jul; 139 (1): 32-40. |
| [16] | Jorge Luis Sánchez-Torres, Petra Yescas-Gómez, Julio Torres-Romero, et al, Matrix metalloproteinases deregulation in amyotrophic lateral sclerosis, Journal of the Neurological Sciences, Vol. 419, 2020, 117175. |
| [17] | Wang T, Jin X, Liao Y,. Association of NF-κB and AP-1 with MMP-9 Overexpression in 2-Chloroethanol Exposed Rat Astrocytes. Cells. 2018; 7 (8): 96. |
| [18] | Picca A, Fanelli F, Calvani R, Mulè G, Pesce V, Sisto A, Pantanelli C, Bernabei R, Landi F, Marzetti E. Gut Dysbiosis and Muscle Aging: Searching for Novel Targets against Sarcopenia. Mediators Inflamm. 2018 Jan 30; 2018: 7026198. |
| [19] | Dhillon RJ, Hasni S. Pathogenesis and Management of Sarcopenia. Clin Geriatr Med. 2017; 33 (1): 17-26. |
| [20] | DeFronzo RA, Tripathy D. Skeletal muscle insulin resistance is the primary defect in type 2 diabetes. Diabetes Care. 2009 Nov; 32 Suppl 2 (Suppl 2): S157-63. |
| [21] | Singh R, Barden A, Mori T, Beilin L. Advanced glycation end-products: a review. Diabetologia. 2001 Feb; 44 (2): 129-46. |
| [22] | Ahmed N. Advanced glycation endproducts--role in pathology of diabetic complications. Diabetes Res Clin Pract. 2005 Jan; 67 (1): 3-21. |
| [23] | Goldin A, Beckman JA, Schmidt AM, Creager MA. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation. 2006 Aug 8; 114 (6): 597-605. |
| [24] | In: Lakowicz J. R. (eds) (2006) Protein Fluorescence. Principles of Fluorescence Spectroscopy. Springer, Boston, MA. 45-50. |
| [25] | Mori H, Kuroda A, Ishizu M. Association of accumulated advanced glycation end-products with a high prevalence of sarcopenia and dynapenia in patients with type 2 diabetes. J Diabetes Investig. 2019 Sep; 10 (5): 1332-1340. |
| [26] | Sun K, Semba RD, Fried LP, Schaumberg DA, Ferrucci L, Varadhan R. Elevated Serum Carboxymethyl-Lysine, an Advanced Glycation End Product, Predicts Severe Walking Disability in Older Women: The Women's Health and Aging Study I. J Aging Res. 2012; 2012: 586385. |
| [27] | Snedeker JG, Gautieri A. The role of collagen crosslinks in ageing and diabetes - the good, the bad, and the ugly. Muscles Ligaments Tendons J. 2014; 4 (3): 303-308. |
| [28] | Gordon MK, Hahn RA. Collagens. Cell Tissue Res. 2010; 339 (1): 247-257. |
| [29] | Tanzer ML. Cross-linking of collagen. Science. 1973 May 11; 180 (4086): 561-6. |
| [30] | Juranek JK, Daffu GK, Wojtkiewicz J. Receptor for Advanced Glycation End Products and its Inflammatory Ligands are Upregulated in Amyotrophic Lateral Sclerosis. Front Cell Neurosci. 2015; 9: 485. |
| [31] | Auten RL, Davis JM. Oxygen toxicity and reactive oxygen species: the devil is in the details. Pediatr Res. 2009 Aug; 66 (2): 121-7. |
| [32] | Pizzino G, Irrera N, Cucinotta M,. Oxidative Stress: Harms and Benefits for Human Health. Oxid Med Cell Longev. 2017; 2017: 8416763. |
| [33] | Southorn PA, Powis G. Free radicals in medicine. I. Chemical nature and biologic reactions. Mayo Clin Proc. 1988 Apr; 63 (4): 381-9. |
| [34] | Bhattacharyya A, Chattopadhyay R, Mitra S, Crowe SE. Oxidative stress: an essential factor in the pathogenesis of gastrointestinal mucosal diseases. Physiol Rev. 2014; 94 (2): 329-354. |
| [35] | Atashgahi S, Shetty SA, Smidt H, de Vos WM. Flux, Impact, and Fate of Halogenated Xenobiotic Compounds in the Gut. Front Physiol. 2018 Jul 10; 9: 888. |
| [36] | Marquis RE. Oxygen metabolism, oxidative stress and acid-base physiology of dental plaque biofilms. J Ind Microbiol. 1995 Sep; 15 (3): 198-207. |
| [37] | Taniyama Y, Griendling KK. Reactive oxygen species in the vasculature: molecular and cellular mechanisms. Hypertension. 2003 Dec; 42 (6): 1075-81. |
| [38] | Rojas F, Gonzalez D, Cortes N. Reactive oxygen species trigger motoneuron death in non-cell-autonomous models of ALS through activation of c-Abl signaling. Front Cell Neurosci. 2015 Jun 9; 9: 203. |
| [39] | Kang W, Jia Z, Tang D. Fusobacterium nucleatum Facilitates Apoptosis, ROS Generation, and Inflammatory Cytokine Production by Activating AKT/MAPK and NF-κB Signaling Pathways in Human Gingival Fibroblasts. Oxid Med Cell Longev. 2019 Oct 13; 2019: 1681972. |
| [40] | Boehm, E. T., Thon, C., Kupcinskas, J. Fusobacterium nucleatum is associated with worse prognosis in Lauren’s diffuse type gastric cancer patients. Sci Rep 10, 16240 (2020). |
| [41] | Ma J, Shen H, Kapesa L, Zeng S. Lauren classification and individualized chemotherapy in gastric cancer. Oncol Lett. 2016 May; 11 (5): 2959-2964. |
| [42] | Kim, H. S., Son, J., Lee, D. Gut- and oral-dysbiosis differentially impact spinal- and bulbar-onset ALS, predicting ALS severity and potentially determining the location of disease onset. BMC Neurol 1023; 22, 62: 45-50. |
| [43] | Nardone G, Rocco A, Malfertheiner P. Review article: helicobacter pylori and molecular events in precancerous gastric lesions. Aliment Pharmacol Ther. 2004 Aug 1; 20 (3): 261-70. |
| [44] | Whisner CM, Athena Aktipis C. The Role of the Microbiome in Cancer Initiation and Progression: How Microbes and Cancer Cells Utilize Excess Energy and Promote One Another's Growth. Curr Nutr Rep. 2019 Mar; 8 (1): 42-51. |
| [45] | Ballard JWO, Towarnicki SG. Mitochondria, the gut microbiome and ROS. Cell Signal. 2020 Nov; 75: 109737. |
| [46] | Schieber M, Chandel NS. ROS function in redox signaling and oxidative stress. Curr Biol. 2014; 24 (10): R453-R462. |
| [47] | Mori K, Shibanuma M, Nose K. Invasive potential induced under long-term oxidative stress in mammary epithelial cells. Cancer Res. 2004 Oct 15; 64 (20): 7464-72. |
| [48] | Gasche Y, Copin JC, Sugawara T. Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia. J Cereb Blood Flow Metab. 2001 Dec; 21 (12): 1393-400. |
| [49] | Spronk E, Sykes G, Falcione S. Hemorrhagic Transformation in Ischemic Stroke and the Role of Inflammation. Front Neurol. 2021; 12: 66-70. |
| [50] | Morisaki Y, Niikura M, Watanabe M. back to 50 Selective Expression of Osteopontin in ALS-resistant Motor Neurons is a Critical Determinant of Late Phase Neurodegeneration Mediated by Matrix Metalloproteinase-9. Sci Rep. 2016 Jun 6; 6: 27354. |
| [51] | Singh M, Foster CR, Dalal S. Osteopontin: role in extracellular matrix deposition and myocardial remodeling post-MI. J Mol Cell Cardiol. 2010 Mar; 48 (3): 538-43. |
| [52] | Kaplan A, Spiller KJ, Towne C. Neuronal matrix metalloproteinase-9 is a determinant of selective neurodegeneration. Neuron. 2014 Jan 22; 81 (2): 333-48. |
| [53] | Guarneri C, Bevelacqua V, Polesel J. NF-κB inhibition is associated with OPN/MMP-9 downregulation in cutaneous melanoma. Oncol Rep. 2017 Feb; 37 (2): 737-746. |
| [54] | Lazăr L, Loghin A, Bud ES. Cyclooxygenase-2 and matrix metalloproteinase-9 expressions correlate with tissue inflammation degree in periodontal disease. Rom J Morphol Embryol. 2015; 56 (4): 1441-6. |
| [55] | Komine O, Yamanaka K. Neuroinflammation in motor neuron disease. Nagoya J Med Sci. 2015 Nov; 77 (4): 537-49. |
| [56] | Simpson DSA, Oliver PL. ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease. Antioxidants (Basel). 2020 Aug 13; 9 (8): 743. |
| [57] | Smith JA, Das A, Ray SK. Role of pro-inflammatory cytokines released from microglia in neurodegenerative diseases. Brain Res Bull. 2012 Jan 4; 87 (1): 10-20. |
| [58] | Dutta K, Thammisetty SS, Boutej H. Mitigation of ALS Pathology by Neuron-Specific Inhibition of Nuclear Factor Kappa B Signaling. J Neurosci. 2020 Jun 24; 40 (26): 5137-5154. |
| [59] | Ting Liu, Lingyun Zhang, Donghyun Joo. NF-κB signaling in inflammation Signal Transduct Target Ther. 2017; 2: 17023. |
| [60] | Beinke S, Ley SC. Functions of NF-kappaB1 and NF-kappaB2 in immune cell biology. Biochem J. 2004; 382 (Pt 2): 393-409. |
| [61] | Liu T, Zhang L, Joo D. NF-κB signaling in inflammation. Signal Transduct Target Ther. 2017; 2: 17023. |
| [62] | Sun SC. Non-canonical NF-κB signaling pathway. back to 60 Cell Res. 2011; 21 (1): 71-85. |
| [63] | Källstig E, McCabe BD, Schneider BL. The Links between ALS and NF-κB. Int J Mol Sci. 2021 Apr 8; 22 (8): 3875. |
| [64] | Dresselhaus EC, Meffert MK. Cellular Specificity of NF-κB Function in the Nervous System. Front Immunol. 2019 May 9; 10: 1043. |
| [65] | Zhou Y, Ji X, Chen J, Fu Y, Huang J Short-chain fatty acid butyrate: A novel shield against chronic gastric ulcer. Exp Ther Med. 2021 Apr; 21 (4): 329. |
| [66] | Zhu H, Hart CA, Sales D. Bacterial killing in gastric juice--effect of pH and pepsin on Escherichia coli and Helicobacter pylori. J Med Microbiol. 2006 Sep; 55 (Pt 9): 1265-1270. |
| [67] | Sung J, Kim N, Lee J. Associations among Gastric Juice pH, Atrophic Gastritis, Intestinal Metaplasia and Helicobacter pylori Infection. Gut Liver. 2018; 12 (2): 158-164. |
| [68] | Martinsen TC, Fossmark R, Waldum HL. The Phylogeny and Biological Function of Gastric Juice-Microbiological Consequences of Removing Gastric Acid. Int J Mol Sci. 2019; 20 (23): 6031. Published 2019 Nov 29. |
| [69] | Afroze S, Meng F, Jensen K. The physiological roles of secretin and its receptor. Ann Transl Med. 2013; 1 (3): 29. |
| [70] | Silva, D. F., Candeias, E., Esteves, A. R. Microbial BMAA elicits mitochondrial dysfunction, innate immunity activation, and Alzheimer’s disease features in cortical neurons. J Neuroinflammation 2020-17, 332-334. |
| [71] | Okamoto, S., Esumi, S., Hamaguchi-Hamada, K. β-N-methylamino-L-alanine (BMAA) suppresses cell cycle progression of non-neuronal cells. Sci Rep 2018; 8: 17-20. |
| [72] | Banack SA, Caller TA, Stommel EW. The cyanobacteria derived toxin Beta-N-methylamino-L-alanine and amyotrophic lateral sclerosis. Toxins (Basel). 2010; 2 (12): 2837-2850. |
| [73] | Nunes-Costa D, Magalhães JD, G-Fernandes M. Microbial BMAA and the Pathway for Parkinson's Disease Neurodegeneration. Front Aging Neurosci. 2020; 12: 26. |
| [74] | Vega AE, Cortiñas TI, Mattana CM. Growth of Helicobacter pylori in medium supplemented with cyanobacterial extract. J Clin Microbiol. 2003 Dec; 41 (12): 5384-8. |
| [75] | Thomas RM, Jobin C. The Microbiome and Cancer: Is the 'Oncobiome' Mirage Real? Trends Cancer. 2015; 1 (1): 24-35. |
| [76] | Gorlé N, Bauwens E, Haesebrouck F. Helicobacter and the Potential Role in Neurological Disorders: There Is More Than Helicobacter pylori. Front Immunol. 2021; 11: 58-60. 4165. |
| [77] | Alvarez-Arellano L, Maldonado-Bernal C. Helicobacter pylori and neurological diseases: Married by the laws of inflammation. World J Gastrointest Pathophysiol. 2014; 5 (4): 400-404. |
| [78] | Saxena A, Mukhopadhyay AK, Nandi SP. Helicobacter pylori: Perturbation and restoration of gut microbiome. J Biosci. 2020; 45 (1): 110. |
| [79] | Vale FF, Oleastro M. Overview of the phytomedicine approaches against Helicobacter pylori. World J Gastroenterol. 2014; 20 (19): 5594-609. |
| [80] | Belov Kirdajova D, Kriska J, Tureckova J. Ischemia-Triggered Glutamate Excitotoxicity From the Perspective of Glial Cells. Front Cell Neurosci. 2020 Mar 19; 14: 51. |
| [81] | Wang JP, Kurt-Jones EA, Shin OS. Varicella-zoster virus activates inflammatory cytokines in human monocytes and macrophages via Toll-like receptor 2. J Virol. 2005; 79 (20): 12658-12666. |
| [82] | Pandya RS, Zhu H, Li W. Therapeutic neuroprotective agents for amyotrophic lateral sclerosis. Cell Mol Life Sci. 2013 Dec; 70 (24): 4729-45. |
| [83] | Xia, Q., Hu, Q., Wang, H. Induction of COX-2-PGE2 synthesis by activation of the MAPK/ERK pathway contributes to neuronal death triggered by TDP-43-depleted microglia. Cell Death Dis, 2015; 11: 17-19. |
| [84] | Drachman DB, Frank K, Dykes-Hoberg M. Cyclooxygenase 2 inhibition protects motor neurons and prolongs survival in a transgenic mouse model of ALS. Ann Neurol. 2002 Dec; 52 (6): 771-8. |
| [85] | Sugai F, Yamamoto Y, Miyaguchi K, et al. Benefit of valproic acid in suppressing disease progression of ALS model mice. Eur J Neurosci. 2004 Dec; 20 (11): 3179-83. |
| [86] | Piepers S, Veldink JH, de Jong SW. Randomized sequential trial of valproic acid in amyotrophic lateral sclerosis. Ann Neurol. 2009 Aug; 66 (2): 227-34. |
| [87] | Coppede F. Targeting the epigenome to treat neurodegenerative diseases or delay their onset: a perspective. Neural Regen Res. 2022 Aug; 17 (8): 1745-1747. |
| [88] | Sibertin-Blanc C, Ciccolini J, Norguet E Monoclonal antibodies for treating gastric cancer: promises and pitfalls. Expert Opin Biol Ther. 2016 Jun; 16 (6): 759-69. |
| [89] | Valera E, Mante M, Anderson S. Lenalidomide reduces microglial activation and behavioral deficits in a transgenic model of Parkinson's disease. J Neuroinflammation. 2015 May 14; 12: 93. |
| [90] | Glass CK, Saijo K, Winner B, et al. Mechanisms underlying inflammation in neurodegeneration. Cell. 2010 Mar 19; 140 (6): 918-34. |
| [91] | Nicholson K, Bjornevik K, Abu-Ali G, et al. The human gut microbiota in people with amyotrophic lateral sclerosis. Amyotroph Lateral Scler Frontotemporal Degener. 2021 May; 22 (3-4): 186-194. |
| [92] | Zhang YG, Wu S, Yi J. Target Intestinal Microbiota to Alleviate Disease Progression in Amyotrophic Lateral Sclerosis. Clin Ther. 2017; 39 (2): 322-336. |
| [93] | Geller LT, Barzily-Rokni M, Danino T Potential role of intratumor bacteria in mediating tumor resistance to the chemotherapeutic drug gemcitabine. Science. 2017 Sep 15; 357 (6356): 1156-1160. |
| [94] | Coutzac, C., Jouniaux, JM., Paci, A. et al. Systemic short chain fatty acids limit antitumor effect of CTLA-4 blockade in hosts with cancer. Nat Commun 11, 2168 (2020). |
| [95] | Silva YP, Bernardi A, Frozza RL. The Role of Short-Chain Fatty Acids From Gut Microbiota in Gut-Brain Communication. Front Endocrinol (Lausanne). 2020; 11: 25. |
| [96] | Chew J, Zilm PS, Fuss JM, et al. A proteomic investigation of Fusobacterium nucleatum alkaline-induced biofilms. BMC Microbiol. 2012 Sep 3; 12: 189. |
| [97] | Jones EM, Cochrane CA, Percival SL. The Effect of pH on the Extracellular Matrix and Biofilms. Adv Wound Care (New Rochelle). 2015; 4 (7): 431-439. |
| [98] | O'May GA, Reynolds N, Smith AR. Effect of pH and antibiotics on microbial overgrowth in the stomachs and duodena of patients undergoing percutaneous endoscopic gastrostomy feeding. J Clin Microbiol. 2005; 43 (7): 3059-3065. |
| [99] | Zou K, Li Z1, Zhang Y, et al Advances in the study of berberine and its derivatives: a focus on anti-inflammatory and anti-tumor effects in the digestive system. Acta Pharmacol Sin. 2017 Feb; 38 (2): 157-167. |
| [100] | Wang H, Zhu C, Ying Y. Metformin and berberine, two versatile drugs in treatment of common metabolic diseases. Oncotarget. 2017 Sep 11; 9 (11): 10135-10146. |
| [101] | QiangZhanga, XiaobingWangb, ShijieCaoc Berberine represses human gastric cancer cell growth in vitro and in vivo by inducing cytostatic autophagy via inhibition of MAPK/mTOR/p70S6K and Akt signaling pathways Biomedicine & Pharmacotherapy 2020; 128: 115-120. |
| [102] | Rusmini P, Cristofani R, Tedesco B, et al. Enhanced Clearance of Neurotoxic Misfolded Proteins by the Natural Compound Berberine and Its Derivatives. Int J Mol Sci. 2020 May 13; 21 (10): 3443. |
| [103] | Cicardi ME, Cristofani R, Crippa V. Autophagic and Proteasomal Mediated Removal of Mutant Androgen Receptor in Muscle Models of Spinal and Bulbar Muscular Atrophy. Front Endocrinol (Lausanne). 2019 Aug 20; 10: 569. |
| [104] | Giorgetti E, Lieberman AP. Polyglutamine androgen receptor-mediated neuromuscular disease. Cell Mol Life Sci. 2016 Nov; 73 (21): 3991-9. |
| [105] | Lin JP, Yang JS, Wu CC, et al. Berberine induced down-regulation of matrix metalloproteinase-1, -2 and -9 in human gastric cancer cells (SNU-5) in vitro. In Vivo. 2008 Mar-Apr; 22 (2): 223-30. |
| [106] | Münch C, O'Brien J, Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci U S A. 2011 Mar 1; 108 (9): 3548-53. |
| [107] | Kim HJ, Yim GW, Nam EJ, et al Synergistic Effect of COX-2 Inhibitor on Paclitaxel-Induced Apoptosis in the Human Ovarian Cancer Cell Line OVCAR-3. Cancer Res Treat. 2014 Jan; 46 (1): 81-92. |
| [108] | Jung YJ, Tweedie D, Scerba MT, et al. Neuroinflammation as a Factor of Neurodegenerative Disease: Thalidomide Analogs as Treatments. Front Cell Dev Biol. 2019 Dec 4; 7: 313. |
| [109] | Yasojima K, Tourtellotte WW, McGeer EG. Marked increase in cyclooxygenase-2 in ALS spinal cord: implications for therapy. Neurology. 2001; 57 (6): 952-6. |
| [110] | Fushida S, Kinoshita J, Kaji M, et al Paclitaxel plus valproic acid versus paclitaxel alone as second- or third-line therapy for advanced gastric cancer: a randomized Phase II trial. Drug Des Devel Ther. 2016 Jul 25; 10: 2353-8. |
| [111] | Lee JY, Lee JD, Phipps S. Absence of toll-like receptor 4 (TLR4) extends survival in the hSOD1 G93A mouse model of amyotrophic lateral sclerosis. J Neuroinflammation. 2015; 12: 90. |
APA Style
Masato Hada, Muhammad Akram. (2022). Prevention with Synbiosis and Treatment with Thalidomide and Celecoxib for Amyotrophic Lateral Sclerosis. American Journal of Biomedical and Life Sciences, 10(5), 146-154. https://doi.org/10.11648/j.ajbls.20221005.13
ACS Style
Masato Hada; Muhammad Akram. Prevention with Synbiosis and Treatment with Thalidomide and Celecoxib for Amyotrophic Lateral Sclerosis. Am. J. Biomed. Life Sci. 2022, 10(5), 146-154. doi: 10.11648/j.ajbls.20221005.13
Share This Article
Twitter
Linked In
Facebook
Copy
Download@article{10.11648/j.ajbls.20221005.13,
author = {Masato Hada and Muhammad Akram},
title = {Prevention with Synbiosis and Treatment with Thalidomide and Celecoxib for Amyotrophic Lateral Sclerosis},
journal = {American Journal of Biomedical and Life Sciences},
volume = {10},
number = {5},
pages = {146-154},
doi = {10.11648/j.ajbls.20221005.13},
url = {https://doi.org/10.11648/j.ajbls.20221005.13},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbls.20221005.13},
abstract = {There are a variety of types of amyotrophic lateral sclerosis (ALS). Most patients with ALS (90%) are classified into the sporadic type (SALS) without heredity. 5% of SALS and 3%of familial type (FALS) are caused by mutations in the 43-kDa trans-activating response region DNA-binding protein (TDP-43). 20%of FALS are caused by the mutation of Cu, Zn superoxide dismutase (SOD1). Superoxide dismutases (SODs) catalyze the dismutation which reaction breaks down harmful radicals into non-reactive molecules in the cells. Mutated SOD1 leads to the production of ROS that causes neuronal death. Recently, a number of new causal factors have been found to link to the pathogenesis of ALS. Characteristic pathological mechanism of ALS is the function of cytosolic protein aggregates. Normal cell functions are disturbed in the cytosol and lead to abnormal cellular processes such as oxidative stress, excitotoxicity, mitochondrial dysfunction. Matrix metalloproteinases (MMPs) and Tissue inhibitors of metalloproteinases (TIMPs) process physiological tissue remodeling and pathological conditions, both of which include vascular and fibrotic regenerations, angiogenesis and destructive diseases such as ALS and cancers. The Receptor for Advanced Glycation End Products (RAGE) plays an important role in ALS causing inflammation oxidative stress and cellular dysfunction. RAGE is also expressed in neurons, vascular cells, microglia, and astrocytes in the central nervous system (CNS). β-N-methylamino-L-alanine (BMAA) is a potential environmental factor in ALS, which is derived from the cycad plant synthesized by cyanobacteria. BMAA is consumed mainly as cycad flour. Dysfunction of these factors are closely associated with nuclear factor-κB (NF-κB) and activator protein-1 (AP-1) The drugs that suppress activated NF-κB are currently thalidomide, celecoxib and valproic acid. These drugs might slow down the exacerbation of ALS as they are effective for cancers.},
year = {2022}
}
TY - JOUR T1 - Prevention with Synbiosis and Treatment with Thalidomide and Celecoxib for Amyotrophic Lateral Sclerosis AU - Masato Hada AU - Muhammad Akram Y1 - 2022/10/28 PY - 2022 N1 - https://doi.org/10.11648/j.ajbls.20221005.13 DO - 10.11648/j.ajbls.20221005.13 T2 - American Journal of Biomedical and Life Sciences JF - American Journal of Biomedical and Life Sciences JO - American Journal of Biomedical and Life Sciences SP - 146 EP - 154 PB - Science Publishing Group SN - 2330-880X UR - https://doi.org/10.11648/j.ajbls.20221005.13 AB - There are a variety of types of amyotrophic lateral sclerosis (ALS). Most patients with ALS (90%) are classified into the sporadic type (SALS) without heredity. 5% of SALS and 3%of familial type (FALS) are caused by mutations in the 43-kDa trans-activating response region DNA-binding protein (TDP-43). 20%of FALS are caused by the mutation of Cu, Zn superoxide dismutase (SOD1). Superoxide dismutases (SODs) catalyze the dismutation which reaction breaks down harmful radicals into non-reactive molecules in the cells. Mutated SOD1 leads to the production of ROS that causes neuronal death. Recently, a number of new causal factors have been found to link to the pathogenesis of ALS. Characteristic pathological mechanism of ALS is the function of cytosolic protein aggregates. Normal cell functions are disturbed in the cytosol and lead to abnormal cellular processes such as oxidative stress, excitotoxicity, mitochondrial dysfunction. Matrix metalloproteinases (MMPs) and Tissue inhibitors of metalloproteinases (TIMPs) process physiological tissue remodeling and pathological conditions, both of which include vascular and fibrotic regenerations, angiogenesis and destructive diseases such as ALS and cancers. The Receptor for Advanced Glycation End Products (RAGE) plays an important role in ALS causing inflammation oxidative stress and cellular dysfunction. RAGE is also expressed in neurons, vascular cells, microglia, and astrocytes in the central nervous system (CNS). β-N-methylamino-L-alanine (BMAA) is a potential environmental factor in ALS, which is derived from the cycad plant synthesized by cyanobacteria. BMAA is consumed mainly as cycad flour. Dysfunction of these factors are closely associated with nuclear factor-κB (NF-κB) and activator protein-1 (AP-1) The drugs that suppress activated NF-κB are currently thalidomide, celecoxib and valproic acid. These drugs might slow down the exacerbation of ALS as they are effective for cancers. VL - 10 IS - 5 ER -
Email: