Insights on Natural Products Against Amyotrophic Lateral Sclerosis (ALS)


Cite item

Full Text

Abstract

Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease that causes the death of motor neurons and consequent muscle paralysis. Despite many efforts to address it, current therapy targeting ALS remains limited, increasing the interest in complementary therapies. Over the years, several herbal preparations and medicinal plants have been studied to prevent and treat this disease, which has received remarkable attention due to their blood-brain barrier penetration properties and low toxicity. Thus, this review presents the therapeutic potential of a variety of medicinal herbs and their relationship with ALS and their physiopathological pathways.

About the authors

Kadja Luana Monteiro

Research Group on Therapeutic Strategies - GPET, Laboratory of Synthesis and Research in Medicinal Chemistry - LSPMED, Institute of Chemistry and Biotechnology, Federal University of Alagoas

Email: info@benthamscience.net

Marcone dos Santos Alcântara

Research Group on Therapeutic Strategies - GPET, Laboratory of Synthesis and Research in Medicinal Chemistry - LSPMED, Institute of Chemistry and Biotechnology, Federal University of Alagoas,

Email: info@benthamscience.net

Thiago de Aquino

Research Group on Therapeutic Strategies - GPET, Laboratory of Synthesis and Research in Medicinal Chemistry - LSPMED, Institute of Chemistry and Biotechnology, Federal University of Alagoas,

Email: info@benthamscience.net

Edeildo da Silva-Júnior

Institute of Chemistry and Biotechnology,, Federal University of Alagoas

Author for correspondence.
Email: info@benthamscience.net

References

  1. Taylor, J.P.; Brown, R.H., Jr; Cleveland, D.W. Decoding ALS: From genes to mechanism. Nature, 2016, 539(7628), 197-206. doi: 10.1038/nature20413 PMID: 27830784
  2. Zarei, S.; Carr, K.; Reiley, L.; Diaz, K.; Guerra, O.; Altamirano, P.; Pagani, W.; Lodin, D.; Orozco, G.; Chinea, A. A comprehensive review of amyotrophic lateral sclerosis. Surg. Neurol. Int., 2015, 6(1), 171. doi: 10.4103/2152-7806.169561 PMID: 26629397
  3. Gil, J.; Funalot, B.; Verschueren, A.; Danel-Brunaud, V.; Camu, W.; Vandenberghe, N.; Desnuelle, C.; Guy, N.; Camdessanche, J.P.; Cintas, P.; Carluer, L.; Pittion, S.; Nicolas, G.; Corcia, P.; Fleury, M.C.; Maugras, C.; Besson, G.; Le Masson, G.; Couratier, P. Causes of death amongst French patients with amyotrophic lateral sclerosis: A prospective study. Eur. J. Neurol., 2008, 15(11), 1245-1251. doi: 10.1111/j.1468-1331.2008.02307.x PMID: 18973614
  4. Spataro, R.; Lo Re, M.; Piccoli, T.; Piccoli, F.; La Bella, V. Causes and place of death in Italian patients with amyotrophic lateral sclerosis. Acta Neurol. Scand., 2010, 122(3), 217-223. doi: 10.1111/j.1600-0404.2009.01290.x PMID: 20078446
  5. Turner, M.R.; Hardiman, O.; Benatar, M.; Brooks, B.R.; Chio, A.; de Carvalho, M.; Ince, P.G.; Lin, C.; Miller, R.G.; Mitsumoto, H.; Nicholson, G.; Ravits, J.; Shaw, P.J.; Swash, M.; Talbot, K.; Traynor, B.J.; Van den Berg, L.H.; Veldink, J.H.; Vucic, S.; Kiernan, M.C. Controversies and priorities in amyotrophic lateral sclerosis. Lancet Neurol., 2013, 12(3), 310-322. doi: 10.1016/S1474-4422(13)70036-X PMID: 23415570
  6. Mejzini, R.; Flynn, L.L.; Pitout, I.L.; Fletcher, S.; Wilton, S.D.; Akkari, P.A. ALS genetics, mechanisms, and therapeutics: Where are we now? Front. Neurosci., 2019, 13, 1310. doi: 10.3389/fnins.2019.01310 PMID: 31866818
  7. Torquato, H.; Goettert, M.; Justo, G.; Paredes-Gamero, E. Anti-cancer phytometabolites targeting cancer stem cells. Curr. Genomics, 2017, 18(2), 156-174. doi: 10.2174/1389202917666160803162309 PMID: 28367074
  8. Kim, J.; Lee, H.J.; Lee, K.W. Naturally occurring phytochemicals for the prevention of Alzheimer’s disease. J. Neurochem., 2010, 112(6), 1415-1430. doi: 10.1111/j.1471-4159.2009.06562.x PMID: 20050972
  9. Lahlou, M. The success of natural products in drug discovery. Pharmacol. & Pharm., 2013, 04, 17-31.
  10. Henkel, T.; Brunne, R.M.; Müller, H.; Reichel, F. Statistical investigation into the structural complementarity of natural products and synthetic compounds. Angew. Chem. Int. Ed., 1999, 38(5), 643-647. doi: 10.1002/(SICI)1521-3773(19990301)38:53.0.CO;2-G PMID: 29711552
  11. Lee, M.L.; Schneider, G. Scaffold architecture and pharmacophoric properties of natural products and trade drugs: Application in the design of natural product-based combinatorial libraries. J. Comb. Chem., 2001, 3(3), 284-289. doi: 10.1021/cc000097l PMID: 11350252
  12. Jin, X.; Liu, M.Y.; Zhang, D.F.; Zhong, X.; Du, K.; Qian, P.; Gao, H.; Wei, M.J. Natural products as a potential modulator of microglial polarization in neurodegenerative diseases. Pharmacol. Res., 2019, 145, 104253. doi: 10.1016/j.phrs.2019.104253 PMID: 31059788
  13. Liu, Z.; Ran, Y.; Huang, S.; Wen, S.; Zhang, W.; Liu, X.; Ji, Z.; Geng, X.; Ji, X.; Du, H.; Leak, R.K.; Hu, X. Curcumin protects against ischemic stroke by titrating microglia/macrophage polarization. Front. Aging Neurosci., 2017, 9, 233. doi: 10.3389/fnagi.2017.00233 PMID: 28785217
  14. Di Paolo, M.; Papi, L.; Gori, F.; Turillazzi, E. Natural products in neurodegenerative diseases: A great promise but an ethical challenge. Int. J. Mol. Sci., 2019, 20(20), 5170. doi: 10.3390/ijms20205170 PMID: 31635296
  15. Silva, J.M.; Nobre, M.S.C.; Albino, S.L.; Lócio, L.L.; Nascimento, A.P.S.; Scotti, L.; Scotti, M.T.; Oshiro-Junior, J.A.; Lima, M.C.A.; Mendonça-Junior, F.J.B.; Moura, R.O. Secondary metabolites with antioxidant activities for the putative treatment of amyotrophic lateral sclerosis (ALS): "Experimental evidences. Oxid. Med. Cell. Longev., 2020, 2020, 1-22. doi: 10.1155/2020/5642029 PMID: 33299526
  16. Shao, J.W.; Jiang, J.L.; Zou, J.J.; Yang, M.Y.; Chen, F.M.; Zhang, Y.J.; Jia, L. Therapeutic potential of ginsenosides on diabetes: From hypoglycemic mechanism to clinical trials. J. Funct. Foods, 2020, 64, 103630. doi: 10.1016/j.jff.2019.103630
  17. Pizzino, G.; Irrera, N.; Cucinotta, M.; Pallio, G.; Mannino, F.; Arcoraci, V.; Squadrito, F.; Altavilla, D.; Bitto, A. Oxidative stress: Harms and benefits for human health. Oxid. Med. Cell. Longev., 2017, 2017, 1-13. doi: 10.1155/2017/8416763 PMID: 28819546
  18. Cenini, G.; Lloret, A.; Cascella, R. Oxidative stress in neurodegenerative diseases: From a mitochondrial point of view. Oxid. Med. Cell. Longev., 2019, 2019, 1-18. doi: 10.1155/2019/2105607 PMID: 31210837
  19. Dirnagl, U.; Meisel, A. Endogenous neuroprotection: Mitochondria as gateways to cerebral preconditioning? Neuropharmacology, 2008, 55(3), 334-344. doi: 10.1016/j.neuropharm.2008.02.017 PMID: 18402985
  20. Dirnagl, U.; Becker, K.; Meisel, A. Preconditioning and tolerance against cerebral ischaemia: From experimental strategies to clinical use. Lancet Neurol., 2009, 8(4), 398-412. doi: 10.1016/S1474-4422(09)70054-7 PMID: 19296922
  21. Calabrese, V.; Cornelius, C.; Dinkova-Kostova, A.T.; Calabrese, E.J.; Mattson, M.P. Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders. Antioxid. Redox Signal., 2010, 13(11), 1763-1811. doi: 10.1089/ars.2009.3074 PMID: 20446769
  22. Calabrese, V.; Cornelius, C.; Dinkova-Kostova, A.T.; Calabrese, E.J. Vitagenes, cellular stress response, and acetylcarnitine: Relevance to hormesis. Biofactors, 2009, 35(2), 146-160. doi: 10.1002/biof.22 PMID: 19449442
  23. Calabrese, E.J.; Iavicoli, I.; Calabrese, V. Hormesis: Why it is important to biogerontologists. Biogerontology, 2012, 13(3), 215-235. doi: 10.1007/s10522-012-9374-7 PMID: 22270337
  24. Sies, H.; Belousov, V.V.; Chandel, N.S.; Davies, M.J.; Jones, D.P.; Mann, G.E.; Murphy, M.P.; Yamamoto, M.; Winterbourn, C. Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology. Nat. Rev. Mol. Cell Biol., 2022, 23(7), 499-515. doi: 10.1038/s41580-022-00456-z PMID: 35190722
  25. Sies, H.; Jones, D.P. Reactive oxygen species (ROS) as pleiotropic physiological signalling agents. Nat. Rev. Mol. Cell Biol., 2020, 21(7), 363-383. doi: 10.1038/s41580-020-0230-3 PMID: 32231263
  26. Van Houten, B.; Woshner, V.; Santos, J.H. Role of mitochondrial DNA in toxic responses to oxidative stress. DNA Repair, 2006, 5(2), 145-152. doi: 10.1016/j.dnarep.2005.03.002 PMID: 15878696
  27. Selvaraji, S.; Poh, L.; Natarajan, V.; Mallilankaraman, K.; Arumugam, T.V. Negative conditioning of mitochondrial dysfunction in age-related neurodegenerative diseases. Cond. Med., 2019, 2(1), 30-39. PMID: 31058265
  28. Wang, Y.; Xu, E.; Musich, P.R.; Lin, F. Mitochondrial dysfunction in neurodegenerative diseases and the potential countermeasure. CNS Neurosci. Ther., 2019, 25(7), 816-824. doi: 10.1111/cns.13116 PMID: 30889315
  29. Hemerková, P.; Vališ, M. Role of oxidative stress in the pathogenesis of amyotrophic lateral sclerosis: Antioxidant metalloenzymes and therapeutic strategies. Biomolecules, 2021, 11(3), 437. doi: 10.3390/biom11030437 PMID: 33809730
  30. Golenia, A.; Leśkiewicz, M.; Regulska, M.; Budziszewska, B.; Szczęsny, E.; Jagiełła, J.; Wnuk, M.; Ostrowska, M.; Lasoń, W.; Basta-Kaim, A.; Słowik, A. Catalase activity in blood fractions of patients with sporadic ALS. Pharmacol. Rep., 2014, 66(4), 704-707. doi: 10.1016/j.pharep.2014.02.021 PMID: 24948075
  31. Tabrizi, S. Neurodegenerative diseases neurobiology pathogenesis and therapeutics. J. Neurol. Neurosurg. Psychiatry, 2006, 77(2), 284-284. doi: 10.1136/jnnp.2005.072710
  32. Angelova, P.R.; Abramov, A.Y. Role of mitochondrial ROS in the brain: From physiology to neurodegeneration. FEBS Lett., 2018, 592(5), 692-702. doi: 10.1002/1873-3468.12964 PMID: 29292494
  33. Pehar, M.; Beeson, G.; Beeson, C.C.; Johnson, J.A.; Vargas, M.R. Mitochondria-targeted catalase reverts the neurotoxicity of hSOD1G⁹³A astrocytes without extending the survival of ALS-linked mutant hSOD1 mice. PLoS One, 2014, 9(7), e103438. doi: 10.1371/journal.pone.0103438 PMID: 25054289
  34. Richardson, K.; Allen, S.P.; Mortiboys, H.; Grierson, A.J.; Wharton, S.B.; Ince, P.G.; Shaw, P.J.; Heath, P.R. The effect of SOD1 mutation on cellular bioenergetic profile and viability in response to oxidative stress and influence of mutation-type. PLoS One, 2013, 8(6), e68256. doi: 10.1371/journal.pone.0068256 PMID: 23840839
  35. Ahtoniemi, T.; Jaronen, M.; Keksa-Goldsteine, V.; Goldsteins, G.; Koistinaho, J. Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane. Neurobiol. Dis., 2008, 32(3), 479-485. doi: 10.1016/j.nbd.2008.08.010 PMID: 18817872
  36. Xiao, Y.; Karam, C.; Yi, J.; Zhang, L.; Li, X.; Yoon, D.; Wang, H.; Dhakal, K.; Ramlow, P.; Yu, T.; Mo, Z.; Ma, J.; Zhou, J. ROS-related mitochondrial dysfunction in skeletal muscle of an ALS mouse model during the disease progression. Pharmacol. Res., 2018, 138, 25-36. doi: 10.1016/j.phrs.2018.09.008 PMID: 30236524
  37. Bruijn, L.I.; Miller, T.M.; Cleveland, D.W. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu. Rev. Neurosci., 2004, 27(1), 723-749. doi: 10.1146/annurev.neuro.27.070203.144244 PMID: 15217349
  38. Vijayvergiya, C.; Beal, M.F.; Buck, J.; Manfredi, G. Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci., 2005, 25(10), 2463-2470. doi: 10.1523/JNEUROSCI.4385-04.2005 PMID: 15758154
  39. Babu, G.N.; Kumar, A.; Chandra, R.; Puri, S.K.; Singh, R.L.; Kalita, J.; Misra, U.K. Oxidant-antioxidant imbalance in the erythrocytes of sporadic amyotrophic lateral sclerosis patients correlates with the progression of disease. Neurochem. Int., 2008, 52(6), 1284-1289. doi: 10.1016/j.neuint.2008.01.009 PMID: 18308427
  40. Ikawa, M.; Okazawa, H.; Tsujikawa, T.; Matsunaga, A.; Yamamura, O.; Mori, T.; Hamano, T.; Kiyono, Y.; Nakamoto, Y.; Yoneda, M. Increased oxidative stress is related to disease severity in the ALS motor cortex: A PET study. Neurology, 2015, 84(20), 2033-2039. doi: 10.1212/WNL.0000000000001588 PMID: 25904686
  41. Ehrhart, J.; Smith, A.J.; Kuzmin-Nichols, N.; Zesiewicz, T.A.; Jahan, I.; Shytle, R.D.; Kim, S.H.; Sanberg, C.D.; Vu, T.H.; Gooch, C.L.; Sanberg, P.R.; Garbuzova-Davis, S. Humoral factors in ALS patients during disease progression. J. Neuroinflammation, 2015, 12(1), 127. doi: 10.1186/s12974-015-0350-4 PMID: 26126965
  42. Pollari, E.; Goldsteins, G.; Bart, G.; Koistinaho, J.; Giniatullin, R. The role of oxidative stress in degeneration of the neuromuscular junction in amyotrophic lateral sclerosis. Front. Cell. Neurosci., 2014, 8, 131. doi: 10.3389/fncel.2014.00131 PMID: 24860432
  43. Tan, W.; Pasinelli, P.; Trotti, D. Role of mitochondria in mutant SOD1 linked amyotrophic lateral sclerosis. Biochim. Biophys. Acta Mol. Basis Dis., 2014, 1842(8), 1295-1301. doi: 10.1016/j.bbadis.2014.02.009 PMID: 24568860
  44. LoGerfo, A.; Chico, L.; Borgia, L.; Petrozzi, L.; Rocchi, A.; D’Amelio, A.; Carlesi, C.; Ienco, E.; Mancuso, M.; Siciliano, G. Lack of association between nuclear factor erythroid-derived 2-like 2 promoter gene polymorphisms and oxidative stress biomarkers in amyotrophic lateral sclerosis patients. Oxid. Med. Cell. Longev., 2014, 2014, 1-9. doi: 10.1155/2014/432626 PMID: 24672634
  45. Calabrese, V.; Mancuso, C.; Calvani, M.; Rizzarelli, E.; Butterfield, D.A.; Giuffrida Stella, A.M. Nitric oxide in the central nervous system: Neuroprotection versus neurotoxicity. Nat. Rev. Neurosci., 2007, 8(10), 766-775. doi: 10.1038/nrn2214 PMID: 17882254
  46. Mancuso, C.; Pani, G.; Calabrese, V. Bilirubin: An endogenous scavenger of nitric oxide and reactive nitrogen species. Redox Rep., 2006, 11(5), 207-213. doi: 10.1179/135100006X154978 PMID: 17132269
  47. Drake, J.; Sultana, R.; Aksenova, M.; Calabrese, V.; Butterfield, D.A. Elevation of mitochondrial glutathione by? -glutamylcysteine ethyl ester protects mitochondria against peroxynitrite-induced oxidative stress. J. Neurosci. Res., 2003, 74(6), 917-927. doi: 10.1002/jnr.10810 PMID: 14648597
  48. Siracusa, R.; Scuto, M.; Fusco, R.; Trovato, A.; Ontario, M.L.; Crea, R.; Di Paola, R.; Cuzzocrea, S.; Calabrese, V. Anti-inflammatory and anti-oxidant activity of hidrox® in rotenone-induced parkinson’s disease in mice. Antioxidants, 2020, 9(9), 824. doi: 10.3390/antiox9090824 PMID: 32899274
  49. Forni, C.; Facchiano, F.; Bartoli, M.; Pieretti, S.; Facchiano, A.; D’Arcangelo, D.; Norelli, S.; Valle, G.; Nisini, R.; Beninati, S.; Tabolacci, C.; Jadeja, R.N. Beneficial role of phytochemicals on oxidative stress and age-related diseases. BioMed Res. Int., 2019, 2019, 1-16. doi: 10.1155/2019/8748253 PMID: 31080832
  50. Chico, L.; Ienco, E.C.; Bisordi, C.; Lo Gerfo, A.; Petrozzi, L.; Petrucci, A.; Mancuso, M.; Siciliano, G. Amyotrophic lateral sclerosis and oxidative stress: A double-blind therapeutic trial after curcumin supplementation. CNS Neurol. Disord. Drug Targets, 2018, 17(10), 767-779. doi: 10.2174/1871527317666180720162029 PMID: 30033879
  51. Kim, D.S.; Kim, J.Y.; Han, Y. Curcuminoids in neurodegenerative diseases. Recent Patents CNS Drug Discov., 2012, 7(3), 184-204. doi: 10.2174/157488912803252032 PMID: 22742420
  52. Darvesh, A.S.; Carroll, R.T.; Bishayee, A.; Novotny, N.A.; Geldenhuys, W.J.; Van der Schyf, C.J. Curcumin and neurodegenerative diseases: A perspective. Expert Opin. Investig. Drugs, 2012, 21(8), 1123-1140. doi: 10.1517/13543784.2012.693479 PMID: 22668065
  53. Jiang, H.; Tian, X.; Guo, Y.; Duan, W.; Bu, H.; Li, C. Activation of nuclear factor erythroid 2-related factor 2 cytoprotective signaling by curcumin protect primary spinal cord astrocytes against oxidative toxicity. Biol. Pharm. Bull., 2011, 34(8), 1194-1197. doi: 10.1248/bpb.34.1194 PMID: 21804205
  54. Dong, H.; Xu, L.; Wu, L.; Wang, X.; Duan, W.; Li, H.; Li, C. Curcumin abolishes mutant TDP-43 induced excitability in a motoneuron-like cellular model of ALS. Neuroscience, 2014, 272, 141-153. doi: 10.1016/j.neuroscience.2014.04.032 PMID: 24785678
  55. Janssens, J.; Kleinberger, G.; Wils, H.; Van Broeckhoven, C. The role of mutant TAR DNA-binding protein 43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Biochem. Soc. Trans., 2011, 39(4), 954-959. doi: 10.1042/BST0390954 PMID: 21787329
  56. Mackenzie, I.R.A.; Rademakers, R. The role of transactive response DNA-binding protein-43 in amyotrophic lateral sclerosis and frontotemporal dementia. Curr. Opin. Neurol., 2008, 21(6), 693-700. doi: 10.1097/WCO.0b013e3283168d1d PMID: 18989115
  57. Lu, J.; Duan, W.; Guo, Y.; Jiang, H.; Li, Z.; Huang, J.; Hong, K.; Li, C. Mitochondrial dysfunction in human TDP-43 transfected NSC34 cell lines and the protective effect of dimethoxy curcumin. Brain Res. Bull., 2012, 89(5-6), 185-190. doi: 10.1016/j.brainresbull.2012.09.005 PMID: 22986236
  58. Bhatia, N.K.; Srivastava, A.; Katyal, N.; Jain, N.; Khan, M.A.I.; Kundu, B.; Deep, S. Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity. Biochim. Biophys. Acta. Proteins Proteomics, 2015, 1854(5), 426-436. doi: 10.1016/j.bbapap.2015.01.014 PMID: 25666897
  59. Strong, R.; Miller, R.A.; Astle, C.M.; Baur, J.A.; de Cabo, R.; Fernandez, E.; Guo, W.; Javors, M.; Kirkland, J.L.; Nelson, J.F.; Sinclair, D.A.; Teter, B.; Williams, D.; Zaveri, N.; Nadon, N.L.; Harrison, D.E. Evaluation of resveratrol, green tea extract, curcumin, oxaloacetic acid, and medium-chain triglyceride oil on life span of genetically heterogeneous mice. J. Gerontol. A Biol. Sci. Med. Sci., 2013, 68(1), 6-16. doi: 10.1093/gerona/gls070 PMID: 22451473
  60. Anand, P.; Kunnumakkara, A.B.; Newman, R.A.; Aggarwal, B.B. Bioavailability of curcumin: Problems and promises. Mol. Pharm., 2007, 4(6), 807-818. doi: 10.1021/mp700113r PMID: 17999464
  61. Liu, W.; Zhai, Y.; Heng, X.; Che, F.Y.; Chen, W.; Sun, D.; Zhai, G. Oral bioavailability of curcumin: Problems and advancements. J. Drug Target., 2016, 24(8), 694-702. doi: 10.3109/1061186X.2016.1157883 PMID: 26942997
  62. Tripodo, G.; Chlapanidas, T.; Perteghella, S.; Vigani, B.; Mandracchia, D.; Trapani, A.; Galuzzi, M.; Tosca, M.C.; Antonioli, B.; Gaetani, P.; Marazzi, M.; Torre, M.L. Mesenchymal stromal cells loading curcumin-INVITE-micelles: A drug delivery system for neurodegenerative diseases. Colloids Surf. B Biointerfaces, 2015, 125, 300-308. doi: 10.1016/j.colsurfb.2014.11.034 PMID: 25524221
  63. Wu, A.; Ying, Z.; Gomez-Pinilla, F. Dietary curcumin counteracts the outcome of traumatic brain injury on oxidative stress, synaptic plasticity, and cognition. Exp. Neurol., 2006, 197(2), 309-317. doi: 10.1016/j.expneurol.2005.09.004 PMID: 16364299
  64. Ullah, F.; Liang, A.; Rangel, A.; Gyengesi, E.; Niedermayer, G.; Münch, G. High bioavailability curcumin: An anti-inflammatory and neurosupportive bioactive nutrient for neurodegenerative diseases characterized by chronic neuroinflammation. Arch. Toxicol., 2017, 91(4), 1623-1634. doi: 10.1007/s00204-017-1939-4 PMID: 28204864
  65. Rakotoarisoa, M.; Angelova, A. Amphiphilic nanocarrier systems for curcumin delivery in neurodegenerative disorders. Medicines, 2018, 5(4), 126. doi: 10.3390/medicines5040126 PMID: 30477087
  66. Ahmadi, M.; Agah, E.; Nafissi, S.; Jaafari, M.R.; Harirchian, M.H.; Sarraf, P.; Faghihi-Kashani, S.; Hosseini, S.J.; Ghoreishi, A.; Aghamollaii, V.; Hosseini, M.; Tafakhori, A. Safety and efficacy of nanocurcumin as add-on therapy to riluzole in patients with amyotrophic lateral sclerosis: A pilot randomized clinical trial. Neurotherapeutics, 2018, 15(2), 430-438. doi: 10.1007/s13311-018-0606-7 PMID: 29352425
  67. Ghasemi, F.; Bagheri, H.; Barreto, G.E.; Read, M.I.; Sahebkar, A. Effects of curcumin on microglial cells. Neurotox. Res., 2019, 36(1), 12-26. doi: 10.1007/s12640-019-00030-0 PMID: 30949950
  68. Handique, J.G.; Baruah, J.B. Polyphenolic compounds: An overview. React. Funct. Polym., 2002, 52(3), 163-188. doi: 10.1016/S1381-5148(02)00091-3
  69. Wang, J.; Zhang, Y.; Tang, L.; Zhang, N.; Fan, D. Protective effects of resveratrol through the up-regulation of SIRT1 expression in the mutant hSOD1-G93A-bearing motor neuron-like cell culture model of amyotrophic lateral sclerosis. Neurosci. Lett., 2011, 503(3), 250-255. doi: 10.1016/j.neulet.2011.08.047 PMID: 21896316
  70. Barber, S.C.; Higginbottom, A.; Mead, R.J.; Barber, S.; Shaw, P.J. An in vitro screening cascade to identify neuroprotective antioxidants in ALS. Free Radic. Biol. Med., 2009, 46(8), 1127-1138. doi: 10.1016/j.freeradbiomed.2009.01.019 PMID: 19439221
  71. Mancuso, R.; del Valle, J.; Modol, L.; Martinez, A.; Granado-Serrano, A.B.; Ramirez-Núñez, O.; Pallás, M.; Portero-Otin, M.; Osta, R.; Navarro, X. Resveratrol improves motoneuron function and extends survival in SOD1(G93A) ALS mice. Neurotherapeutics, 2014, 11(2), 419-432. PMID: 24414863
  72. Song, L.; Chen, L.; Zhang, X.; Li, J.; Le, W. Resveratrol ameliorates motor neuron degeneration and improves survival in SOD1(G93A) mouse model of amyotrophic lateral sclerosis. BioMed Res. Int., 2014, 2014, 1-10. doi: 10.1155/2014/483501 PMID: 25057490
  73. Mancuso, R.; del Valle, J.; Morell, M.; Pallás, M.; Osta, R.; Navarro, X. Lack of synergistic effect of resveratrol and sigma-1 receptor agonist (PRE-084) in SOD1G93A ALS mice: Overlapping effects or limited therapeutic opportunity? Orphanet J. Rare Dis., 2014, 9(1), 78. doi: 10.1186/1750-1172-9-78 PMID: 24885036
  74. Srinivasan, E.; Rajasekaran, R. Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein. J. Comput. Aided Mol. Des., 2018, 32(12), 1347-1361. doi: 10.1007/s10822-018-0175-1 PMID: 30368622
  75. Yun, Y.C.; Jeong, S.; Kim, S.H.; Cho, G. Reduced sirtuin 1/adenosine monophosphate-activated protein kinase in amyotrophic lateral sclerosis patient-derived mesenchymal stem cells can be restored by resveratrol. J. Tissue Eng. Regen. Med., 2018, 13(1), 110-115.
  76. Laudati, G.; Mascolo, L.; Guida, N.; Sirabella, R.; Pizzorusso, V.; Bruzzaniti, S.; Serani, A.; Di Renzo, G.; Canzoniero, L.M.T.; Formisano, L. Resveratrol treatment reduces the vulnerability of SH-SY5Y cells and cortical neurons overexpressing SOD1-G93A to Thimerosal toxicity through SIRT1/DREAM/PDYN pathway. Neurotoxicology, 2019, 71, 6-15. doi: 10.1016/j.neuro.2018.11.009 PMID: 30503815
  77. Caplliure-Llopis, J.; Peralta-Chamba, T.; Carrera-Juliá, S.; Cuerda-Ballester, M.; Drehmer-Rieger, E.; López-Rodriguez, M.M.; Rubia Ortí, J.E. Therapeutic alternative of the ketogenic Mediterranean diet to improve mitochondrial activity in Amyotrophic Lateral Sclerosis (ALS): A Comprehensive Review. Food Sci. Nutr., 2020, 8(1), 23-35. doi: 10.1002/fsn3.1324 PMID: 31993129
  78. Hu, T.; He, X.W.; Jiang, J.G.; Xu, X.L. Hydroxytyrosol and its potential therapeutic effects. J. Agric. Food Chem., 2014, 62(7), 1449-1455. doi: 10.1021/jf405820v PMID: 24479643
  79. de Pablos, R.M.; Espinosa-Oliva, A.M.; Hornedo-Ortega, R.; Cano, M.; Arguelles, S. Hydroxytyrosol protects from aging process via AMPK and autophagy; a review of its effects on cancer, metabolic syndrome, osteoporosis, immune-mediated and neurodegenerative diseases. Pharmacol. Res., 2019, 143, 58-72. doi: 10.1016/j.phrs.2019.03.005 PMID: 30853597
  80. Oliván, S.; Martínez-Beamonte, R.; Calvo, A.C.; Surra, J.C.; Manzano, R.; Arnal, C.; Osta, R.; Osada, J. Extra virgin olive oil intake delays the development of amyotrophic lateral sclerosis associated with reduced reticulum stress and autophagy in muscle of SOD1G93A mice. J. Nutr. Biochem., 2014, 25(8), 885-892. doi: 10.1016/j.jnutbio.2014.04.005 PMID: 24917047
  81. Kalaiselvan, I.; Samuthirapandi, M.; Govindaraju, A.; Sheeja Malar, D.; Kasi, P.D. Olive oil and its phenolic compounds (hydroxytyrosol and tyrosol) ameliorated TCDD-induced heptotoxicity in rats via inhibition of oxidative stress and apoptosis. Pharm. Biol., 2016, 54(2), 338-346. doi: 10.3109/13880209.2015.1042980 PMID: 25955957
  82. Rajabian, A.; Sadeghnia, H.; Fanoudi, S.; Hosseini, A. Genus Boswellia as a new candidate for neurodegenerative disorders. Iran. J. Basic Med. Sci., 2020, 23(3), 277-286. PMID: 32440312
  83. Ammon, H. Boswellic acids in chronic inflammatory diseases. Planta Med., 2006, 72(12), 1100-1116. doi: 10.1055/s-2006-947227 PMID: 17024588
  84. Siddiqui, A.; Shah, Z.; Jahan, R.N.; Othman, I.; Kumari, Y. Mechanistic role of boswellic acids in Alzheimer’s disease: Emphasis on anti-inflammatory properties. Biomed. Pharmacother., 2021, 144, 112250. doi: 10.1016/j.biopha.2021.112250 PMID: 34607104
  85. Minj, E.; Upadhayay, S.; Mehan, S. Nrf2/HO-1 signaling activator acetyl-11-keto-beta boswellic acid (AKBA)-mediated neuroprotection in methyl mercury-induced experimental model of ALS. Neurochem. Res., 2021, 46(11), 2867-2884. doi: 10.1007/s11064-021-03366-2 PMID: 34075522
  86. Landis-Piwowar, K.R.; Huo, C.; Chen, D.; Milacic, V.; Shi, G.; Chan, T.H.; Dou, Q.P. A novel prodrug of the green tea polyphenol (-)-epigallocatechin-3-gallate as a potential anticancer agent. Cancer Res., 2007, 67(9), 4303-4310. doi: 10.1158/0008-5472.CAN-06-4699 PMID: 17483343
  87. Bedlack, R.S.; Joyce, N.; Carter, G.T.; Paganoni, S.; Karam, C. Complementary and alternative therapies in amyotrophic lateral sclerosis. Neurol. Clin., 2015, 33(4), 909-936. doi: 10.1016/j.ncl.2015.07.008 PMID: 26515629
  88. Hockenbery, D.M.; Oltvai, Z.N.; Yin, X.M.; Milliman, C.L.; Korsmeyer, S.J. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell, 1993, 75(2), 241-251. doi: 10.1016/0092-8674(93)80066-N PMID: 7503812
  89. Terao, J.; Piskula, M.; Yao, Q. Protective effect of epicatechin, epicatechin gallate, and quercetin on lipid peroxidation in phospholipid bilayers. Arch. Biochem. Biophys., 1994, 308(1), 278-284. doi: 10.1006/abbi.1994.1039 PMID: 8311465
  90. Levites, Y.; Amit, T.; Youdim, M.B.H.; Mandel, S. Involvement of protein kinase C activation and cell survival/cell cycle genes in green tea polyphenol (-)-epigallocatechin 3-gallate neuroprotective action. J. Biol. Chem., 2002, 277(34), 30574-30580. doi: 10.1074/jbc.M202832200 PMID: 12058035
  91. Mandel, S.A.; Avramovich-Tirosh, Y.; Reznichenko, L.; Zheng, H.; Weinreb, O.; Amit, T.; Youdim, M.B.H. Multifunctional activities of green tea catechins in neuroprotection. Modulation of cell survival genes, iron-dependent oxidative stress and PKC signaling pathway. Neurosignals, 2005, 14(1-2), 46-60. doi: 10.1159/000085385 PMID: 15956814
  92. Nie, G.; Cao, Y.; Zhao, B. Protective effects of green tea polyphenols and their major component, (-)-epigallocatechin-3-gallate (EGCG), on 6-hydroxydopamine-induced apoptosis in PC12 cells. Redox Rep., 2002, 7(3), 171-177. doi: 10.1179/135100002125000424 PMID: 12189048
  93. Reznichenko, L.; Amit, T.; Youdim, M.B.H.; Mandel, S. Green tea polyphenol (-)-epigallocatechin-3-gallate induces neurorescue of long-term serum-deprived PC12 cells and promotes neurite outgrowth. J. Neurochem., 2005, 93(5), 1157-1167. doi: 10.1111/j.1471-4159.2005.03085.x PMID: 15934936
  94. Mandel, S.; Weinreb, O.; Amit, T.; Youdim, M.B.H. Cell signaling pathways in the neuroprotective actions of the green tea polyphenol (-)-epigallocatechin-3-gallate: Implications for neurodegenerative diseases. J. Neurochem., 2004, 88(6), 1555-1569. doi: 10.1046/j.1471-4159.2003.02291.x PMID: 15009657
  95. Panickar, K.S.; Polansky, M.M.; Anderson, R.A. Green tea polyphenols attenuate glial swelling and mitochondrial dysfunction following oxygen-glucose deprivation in cultures. Nutr. Neurosci., 2009, 12(3), 105-113. doi: 10.1179/147683009X423300 PMID: 19356313
  96. Koh, S.; Kwon, H.; Kim, K.S.; Kim, J.; Kim, M.H.; Yu, H.J.; Kim, M.; Lee, K.W.; Do, B.R.; Jung, H.K.; Yang, K.W.; Appel, S.H.; Kim, S.H. Epigallocatechin gallate prevents oxidative-stress-induced death of mutant Cu/Zn-superoxide dismutase (G93A) motoneuron cells by alteration of cell survival and death signals. Toxicology, 2004, 202(3), 213-225. doi: 10.1016/j.tox.2004.05.008 PMID: 15337584
  97. Koh, S.H.; Lee, S.M.; Kim, H.Y.; Lee, K.Y.; Lee, Y.J.; Kim, H.T.; Kim, J.; Kim, M.H.; Hwang, M.S.; Song, C.; Yang, K.W.; Lee, K.W.; Kim, S.H.; Kim, O.H. The effect of epigallocatechin gallate on suppressing disease progression of ALS model mice. Neurosci. Lett., 2006, 395(2), 103-107. doi: 10.1016/j.neulet.2005.10.056 PMID: 16356650
  98. Xu, Z.; Chen, S.; Li, X.; Luo, G.; Li, L.; Le, W. Neuroprotective effects of (-)-epigallocatechin-3-gallate in a transgenic mouse model of amyotrophic lateral sclerosis. Neurochem. Res., 2006, 31(10), 1263-1269. doi: 10.1007/s11064-006-9166-z PMID: 17021948
  99. Srinivasan, E.; Rajasekaran, R. Probing the inhibitory activity of epigallocatechin-gallate on toxic aggregates of mutant (L84F) SOD1 protein through geometry based sampling and steered molecular dynamics. J. Mol. Graph. Model., 2017, 74, 288-295. doi: 10.1016/j.jmgm.2017.04.019 PMID: 28458007
  100. Cao, G.; Sofic, E.; Prior, R.L. Antioxidant and prooxidant behavior of flavonoids: Structure-activit relationships. Free Radic. Biol. Med., 1997, 22(5), 749-760. doi: 10.1016/S0891-5849(96)00351-6 PMID: 9119242
  101. Esposito, E.; Rotilio, D.; Dimatteo, V.; Digiulio, C.; Cacchio, M.; Algeri, S. A review of specific dietary antioxidants and the effects on biochemical mechanisms related to neurodegenerative processes. Neurobiol. Aging, 2002, 23(5), 719-735. doi: 10.1016/S0197-4580(02)00078-7 PMID: 12392777
  102. Vauzour, D.; Vafeiadou, K.; Rodriguez-Mateos, A.; Rendeiro, C.; Spencer, J.P.E. The neuroprotective potential of flavonoids: A multiplicity of effects. Genes Nutr., 2008, 3(3-4), 115-126. doi: 10.1007/s12263-008-0091-4 PMID: 18937002
  103. He, L.; He, T.; Farrar, S.; Ji, L.; Liu, T.; Ma, X. Antioxidants maintain cellular redox homeostasis by elimination of reactive oxygen species. Cell. Physiol. Biochem., 2017, 44(2), 532-553. doi: 10.1159/000485089 PMID: 29145191
  104. Kim, T.Y.; Leem, E.; Lee, J.M.; Kim, S.R. Control of reactive oxygen species for the prevention of parkinson’s disease: The possible application of flavonoids. Antioxidants, 2020, 9(7), 583. doi: 10.3390/antiox9070583 PMID: 32635299
  105. Solanki, I.; Parihar, P.; Mansuri, M.L.; Parihar, M.S. Flavonoid-based therapies in the early management of neurodegenerative diseases. Adv. Nutr., 2015, 6(1), 64-72. doi: 10.3945/an.114.007500 PMID: 25593144
  106. Mansuri, M.L.; Parihar, P.; Solanki, I.; Parihar, M.S. Flavonoids in modulation of cell survival signalling pathways. Genes Nutr., 2014, 9(3), 400. doi: 10.1007/s12263-014-0400-z PMID: 24682883
  107. Mantilla, C.B.; Ermilov, L.G. The novel TrkB receptor agonist 7,8-dihydroxyflavone enhances neuromuscular transmission. Muscle Nerve, 2012, 45(2), 274-276. doi: 10.1002/mus.22295 PMID: 22246885
  108. Korkmaz, O.T.; Aytan, N.; Carreras, I.; Choi, J.K.; Kowall, N.W.; Jenkins, B.G.; Dedeoglu, A. 7,8-Dihydroxyflavone improves motor performance and enhances lower motor neuronal survival in a mouse model of amyotrophic lateral sclerosis. Neurosci. Lett., 2014, 566, 286-291. doi: 10.1016/j.neulet.2014.02.058 PMID: 24637017
  109. Sharma, D.R.; Wani, W.Y.; Sunkaria, A.; Kandimalla, R.J.; Sharma, R.K.; Verma, D.; Bal, A.; Gill, K.D. Quercetin attenuates neuronal death against aluminum-induced neurodegeneration in the rat hippocampus. Neuroscience, 2016, 324, 163-176. doi: 10.1016/j.neuroscience.2016.02.055 PMID: 26944603
  110. Ip, P.; Sharda, P.R.; Cunningham, A.; Chakrabartty, S.; Pande, V.; Chakrabartty, A. Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant. Protein Eng. Des. Sel., 2017, 30(6), 431-440. doi: 10.1093/protein/gzx025 PMID: 28475686
  111. Wang, T.H.; Wang, S.Y.; Wang, X.D.; Jiang, H.Q.; Yang, Y.Q.; Wang, Y.; Cheng, J.L.; Zhang, C.T.; Liang, W.W.; Feng, H.L. Fisetin exerts antioxidant and neuroprotective effects in multiple mutant hsod1 models of amyotrophic lateral sclerosis by activating ERK. Neuroscience, 2018, 379, 152-166. doi: 10.1016/j.neuroscience.2018.03.008 PMID: 29559385
  112. Ye, L.; Wang, H.; Duncan, S.E.; Eigel, W.N.; O’Keefe, S.F. Antioxidant activities of Vine Tea (Ampelopsis grossedentata) extract and its major component dihydromyricetin in soybean oil and cooked ground beef. Food Chem., 2015, 172, 416-422. doi: 10.1016/j.foodchem.2014.09.090 PMID: 25442572
  113. Murakami, T.; Miyakoshi, M.; Araho, D.; Mizutani, K.; Kambara, T.; Ikeda, T.; Chou, W.H.; Inukai, M.; Takenaka, A.; Igarashi, K. Hepatoprotective activity of tocha, the stems and leaves of Ampelopsis grossedentata, and ampelopsin. Biofactors, 2004, 21(1-4), 175-178. doi: 10.1002/biof.552210136 PMID: 15630194
  114. Kou, X.; Shen, K.; An, Y.; Qi, S.; Dai, W.X.; Yin, Z. Ampelopsin inhibits H2O2-induced apoptosis by ERK and Akt signaling pathways and up-regulation of heme oxygenase-1. Phytother. Res., 2012, 26(7), 988-994. doi: 10.1002/ptr.3671 PMID: 22144097
  115. Singh, B.; Kaur, P. Gopichand; Singh, R.D.; Ahuja, P.S. Biology and chemistry of Ginkgo biloba. Fitoterapia, 2008, 79(6), 401-418. doi: 10.1016/j.fitote.2008.05.007 PMID: 18639617
  116. Ferrante, R.J.; Klein, A.M.; Dedeoglu, A.; Beal, M.F. Therapeutic efficacy of EGb761 (Gingko biloba extract) in a transgenic mouse model of amyotrophic lateral sclerosis. J. Mol. Neurosci., 2001, 17(1), 89-96. doi: 10.1385/JMN:17:1:89 PMID: 11665866
  117. Jiang, F.; DeSilva, S.; Turnbull, J. Beneficial effect of ginseng root in SOD-1 (G93A) transgenic mice. J. Neurol. Sci., 2000, 180(1-2), 52-54. doi: 10.1016/S0022-510X(00)00421-4 PMID: 11090864
  118. Trieu, V.N.; Uckun, F.M. Genistein is neuroprotective in murine models of familial amyotrophic lateral sclerosis and stroke. Biochem. Biophys. Res. Commun., 1999, 258(3), 685-688. doi: 10.1006/bbrc.1999.0577 PMID: 10329446
  119. Orrell, R.; Lane, J.; Ross, M. Antioxidant treatment for amyotrophic lateral sclerosis/motor neuron disease.In: Cochrane Database of Systematic Reviews; John Wiley & Sons, Ltd: Chichester, UK, 2004. doi: 10.1002/14651858.CD002829.pub2
  120. Gurney, M.E.; Cutting, F.B.; Zhai, P.; Doble, A.; Taylor, C.P.; Andrus, P.K.; Hall, E.D. Benefit of vitamin E, riluzole, and gababapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol., 1996, 39(2), 147-157. doi: 10.1002/ana.410390203 PMID: 8967745
  121. Desnuelle, C.; Dib, M.; Garrel, C.; Favier, A. A double-blind, placebo-controlled randomized clinical trial of α-tocopherol (vitamin E) in the treatment of amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. Other Motor Neuron Disord., 2001, 2(1), 9-18. doi: 10.1080/146608201300079364 PMID: 11465936
  122. Ascherio, A.; Weisskopf, M.G.; O’Reilly, E.J.; Jacobs, E.J.; McCullough, M.L.; Calle, E.E.; Cudkowicz, M.; Thun, M.J.; Vitamin, E. Vitamin E intake and risk of amyotrophic lateral sclerosis. Ann. Neurol., 2005, 57(1), 104-110. doi: 10.1002/ana.20316 PMID: 15529299
  123. Veldink, J.H.; Kalmijn, S.; Groeneveld, G-J.; Wunderink, W.; Koster, A.; de Vries, J.H.M.; van der Luyt, J.; Wokke, J.H.J.; Van den Berg, L.H. Intake of polyunsaturated fatty acids and vitamin E reduces the risk of developing amyotrophic lateral sclerosis. J. Neurol. Neurosurg. Psychiatry, 2006, 78(4), 367-371. doi: 10.1136/jnnp.2005.083378 PMID: 16648143
  124. Wang, H.; O’Reilly, E.J.; Weisskopf, M.G.; Logroscino, G.; McCullough, M.L.; Schatzkin, A.; Kolonel, L.N.; Ascherio, A.; Vitamin, E. Vitamin E intake and risk of amyotrophic lateral sclerosis: A pooled analysis of data from 5 prospective cohort studies. Am. J. Epidemiol., 2011, 173(6), 595-602. doi: 10.1093/aje/kwq416 PMID: 21335424
  125. Graf, M.; Ecker, D.; Horowski, R.; Kramer, B.; Riederer, P.; Gerlach, M.; Hager, C.; Ludolph, A.C.; Becker, G.; Osterhage, J.; Jost, W.H.; Schrank, B.; Stein, C.; Kostopulos, P.; Lubik, S.; Wekwerth, K.; Dengler, R.; Troeger, M.; Wuerz, A.; Hoge, A.; Schrader, C.; Schimke, N.; Krampfl, K.; Petri, S.; Zierz, S.; Eger, K.; Neudecker, S.; Traufeller, K.; Sievert, M.; Neundörfer, B.; Hecht, M. High dose vitamin E therapy in amyotrophic lateral sclerosis as add-on therapy to riluzole: Results of a placebo-controlled double-blind study. J. Neural Transm., 2005, 112(5), 649-660. doi: 10.1007/s00702-004-0220-1 PMID: 15517433
  126. Michal Freedman, D.; Kuncl, R.W.; Weinstein, S.J.; Malila, N.; Virtamo, J.; Albanes, D. Vitamin E serum levels and controlled supplementation and risk of amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. Frontotemporal Degener., 2013, 14(4), 246-251. doi: 10.3109/21678421.2012.745570 PMID: 23286756
  127. Galbussera, A.; Tremolizzo, L.; Brighina, L.; Testa, D.; Lovati, R.; Ferrarese, C.; Cavaletti, G.; Filippini, G. Vitamin E intake and quality of life in amyotrophic lateral sclerosis patients: A follow-up case series study. Neurol. Sci., 2006, 27(3), 190-193. doi: 10.1007/s10072-006-0668-x PMID: 16897634
  128. Longnecker, M.P.; Kamel, F.; Umbach, D.M.; Munsat, T.L.; Shefner, J.M.; Lansdell, L.W.; Sandler, D.P. Dietary intake of calcium, magnesium and antioxidants in relation to risk of amyotrophic lateral sclerosis. Neuroepidemiology, 2000, 19(4), 210-216. doi: 10.1159/000026258 PMID: 10859501
  129. Nieves, J.W.; Gennings, C.; Factor-Litvak, P.; Hupf, J.; Singleton, J.; Sharf, V.; Oskarsson, B.; Fernandes Filho, J.A.M.; Sorenson, E.J.; D’Amico, E.; Goetz, R.; Mitsumoto, H. Association between dietary intake and function in amyotrophic lateral sclerosis. JAMA Neurol., 2016, 73(12), 1425-1432. doi: 10.1001/jamaneurol.2016.3401 PMID: 27775751
  130. Fitzgerald, K.C.; O’Reilly, É.J.; Fondell, E.; Falcone, G.J.; McCullough, M.L.; Park, Y.; Kolonel, L.N.; Ascherio, A. Intakes of vitamin C and carotenoids and risk of amyotrophic lateral sclerosis: Pooled results from 5 cohort studies. Ann. Neurol., 2013, 73(2), 236-245. doi: 10.1002/ana.23820 PMID: 23362045
  131. Okamoto, K.; Kihira, T.; Kobashi, G.; Washio, M.; Sasaki, S.; Yokoyama, T.; Miyake, Y.; Sakamoto, N.; Inaba, Y.; Nagai, M. Fruit and vegetable intake and risk of amyotrophic lateral sclerosis in Japan. Neuroepidemiology, 2009, 32(4), 251-256. doi: 10.1159/000201563 PMID: 19209004
  132. Ma, Z.; Yang, Z. Scavenging effects of Astragalus and Gynostemma pentaphyllum with its product on O2-. and. OH. Zhong Yao Cai, 1999, 22(6), 303-306. PMID: 12575069
  133. Shahzad, M.; Shabbir, A.; Wojcikowski, K.; Wohlmuth, H.; Gobe, G.C. The antioxidant effects of radix astragali (Astragalus membranaceus and related species) in protecting tissues from injury and disease. Curr. Drug Targets, 2016, 17(12), 1331-1340. doi: 10.2174/1389450116666150907104742 PMID: 26343107
  134. Rong, J.; Cheung, C.; Lau, A.; Shen, J.; Tam, P.; Cheng, Y.C. Induction of heme oxygenase-1 by traditional Chinese medicine formulation ISF-1 and its ingredients as a cytoprotective mechanism against oxidative stress. Int. J. Mol. Med., 2008, 21(4), 405-411. doi: 10.3892/ijmm.21.4.405 PMID: 18360685
  135. Hu, J.Y.; Han, J.; Chu, Z.G.; Song, H.P.; Zhang, D.X.; Zhang, Q.; Huang, Y.S. Astragaloside IV attenuates hypoxia-induced cardiomyocyte damage in rats by upregulating superoxide dismutase-1 levels. Clin. Exp. Pharmacol. Physiol., 2009, 36(4), 351-357. doi: 10.1111/j.1440-1681.2008.05059.x PMID: 18986331
  136. Liu, X.; Zhang, J.; Wang, S.; Qiu, J.; Yu, C.; Astragaloside, I.V. Astragaloside IV attenuates the H2O2-induced apoptosis of neuronal cells by inhibiting α-synuclein expression via the p38 MAPK pathway. Int. J. Mol. Med., 2017, 40(6), 1772-1780. doi: 10.3892/ijmm.2017.3157 PMID: 29039448
  137. Yu, J.; Guo, M.; Li, Y.; Zhang, H.; Chai, Z.; Wang, Q.; Yan, Y.; Yu, J.; Liu, C.; Zhang, G.; Cungen, M. Astragaloside IV protects neurons from microglia-mediated cell damage through promoting microglia polarization. Folia Neuropathol., 2019, 57(2), 170-181. doi: 10.5114/fn.2019.86299 PMID: 31556576
  138. Liu, Y. Therapeutic potential of madecassoside in transgenic mice of amyotrophic lateral sclerosis. Chin. Tradit. Herbal Drugs, 2006, 37, 718-720.
  139. Bai, J-R.; Liu, Y-J.; Song, Y. The mechanism of interfere effects of madecassoside (MC) on neurodegeneration in mice. Zhongguo Laonianxue Zazhi, 2008, 28, 2297-2300.
  140. Sasmita, A.O.; Ling, A.P.K.; Voon, K.G.L.; Koh, R.Y.; Wong, Y.P. Madecassoside activates anti neuroinflammatory mechanisms by inhibiting lipopolysaccharide induced microglial inflammation. Int. J. Mol. Med., 2018, 41(5), 3033-3040. doi: 10.3892/ijmm.2018.3479 PMID: 29436598
  141. Liu, S.; Li, G.; Tang, H.; Pan, R.; Wang, H.; Jin, F.; Yan, X.; Xing, Y.; Chen, G.; Fu, Y.; Dong, J. Madecassoside ameliorates lipopolysaccharide-induced neurotoxicity in rats by activating the Nrf2-HO-1 pathway. Neurosci. Lett., 2019, 709, 134386. doi: 10.1016/j.neulet.2019.134386 PMID: 31330225
  142. Lee, K.; Choi, J.; Choi, B.K.; Gu, Y.M.; Ryu, H.W.; Oh, S.R.; Lee, H.J.; Picroside, I.I.; Picroside, II. Isolated from Pseudolysimachion rotundum var. subintegrum inhibits glucocorticoid refractory serum amyloid A (SAA) Expression and SAA-induced IL-33 secretion. Molecules, 2019, 24(10), 2020. doi: 10.3390/molecules24102020 PMID: 31137813
  143. Li, B.; Lei, S.; Xiong, S.; Chen, S.; Zhang, Z. Pharmacokinetics and pharmacodynamics of morroniside: A review. Nat. Prod. Commun., 2019, 2019. doi: 10.1177/1934578X19856526
  144. Wang, W.; Huang, W.; Li, L.; Ai, H.; Sun, F.; Liu, C.; An, Y. Morroniside prevents peroxide-induced apoptosis by induction of endogenous glutathione in human neuroblastoma cells. Cell. Mol. Neurobiol., 2008, 28(2), 293-305. doi: 10.1007/s10571-007-9168-7 PMID: 17647102
  145. Wang, W.; Sun, F.; An, Y.; Ai, H.; Zhang, L.; Huang, W.; Li, L. Morroniside protects human neuroblastoma SH-SY5Y cells against hydrogen peroxide-induced cytotoxicity. Eur. J. Pharmacol., 2009, 613(1-3), 19-23. doi: 10.1016/j.ejphar.2009.04.013 PMID: 19379729
  146. Wang, W.; Xu, J.; Li, L.; Wang, P.; Ji, X.; Ai, H.; Zhang, L.; Li, L. Neuroprotective effect of morroniside on focal cerebral ischemia in rats. Brain Res. Bull., 2010, 83(5), 196-201. doi: 10.1016/j.brainresbull.2010.07.003 PMID: 20637265
  147. Zhang, J.X.; Wang, R.; Xi, J.; Shen, L.; Zhu, A.Y.; Qi, Q.; Wang, Q.Y.; Zhang, L.J.; Wang, F.C.; Lü, H.Z.; Hu, J.G. Morroniside protects SK-N-SH human neuroblastoma cells against H2O2-induced damage. Int. J. Mol. Med., 2017, 39(3), 603-612. doi: 10.3892/ijmm.2017.2882 PMID: 28204825
  148. Li, P.; Matsunaga, K.; Ohizumi, Y. Nerve growth factor-potentiating compounds from Picrorhizae Rhizoma. Biol. Pharm. Bull., 2000, 23(7), 890-892. doi: 10.1248/bpb.23.890 PMID: 10919373
  149. Cao, Y.; Liu, J.W.; Yu, Y.J.; Zheng, P.Y.; Zhang, X.D.; Li, T.; Guo, M.C. Synergistic protective effect of picroside II and NGF on PC12 cells against oxidative stress induced by H2O2. Pharmacol. Rep., 2007, 59(5), 573-579. PMID: 18048958
  150. Guo, N.; Jin, C.; Shen, L.; Wu, F.; Lin, X.; Feng, Y. Chemical components, pharmacological actions, and clinical applications of Rhizoma picrorhizae. Phytother. Res., 2020, 34(5), 1071-1082. doi: 10.1002/ptr.6591 PMID: 31880854
  151. Li, T.; Liu, J.W.; Zhang, X.D.; Guo, M.C.; Ji, G. The neuroprotective effect of picroside II from hu-huang-lian against oxidative stress. Am. J. Chin. Med., 2007, 35(4), 681-691. doi: 10.1142/S0192415X0700517X PMID: 17708634
  152. Gong, X.; Su, X.; Liu, H. Diallyl trisulfide, the antifungal component of garlic essential oil and the bioactivity of its nanoemulsions formed by spontaneous emulsification. Molecules, 2021, 26(23), 7186. doi: 10.3390/molecules26237186 PMID: 34885768
  153. Calò, L.A.; Fusaro, M.; Davis, P.A. HO-1 attenuates hypertension-induced inflammation/oxidative stress: Support from Bartter’s/Gitelman’s patients. Am. J. Hypertens., 2010, 23(9), 936-936. doi: 10.1038/ajh.2010.130 PMID: 20733571
  154. Sun, M.M.; Bu, H.; Li, B.; Yu, J.X.; Guo, Y.S.; Li, C.Y. Neuroprotective potential of phase II enzyme inducer diallyl trisulfide. Neurol. Res., 2009, 31(1), 23-27. doi: 10.1179/174313208X332959 PMID: 18768114
  155. Guo, Y.; Zhang, K.; Wang, Q.; Li, Z.; Yin, Y.; Xu, Q.; Duan, W.; Li, C. Neuroprotective effects of diallyl trisulfide in SOD1-G93A transgenic mouse model of amyotrophic lateral sclerosis. Brain Res., 2011, 1374, 110-115. doi: 10.1016/j.brainres.2010.12.014 PMID: 21147075
  156. Liu, C.; Leng, B.; Li, Y.; Jiang, H.; Duan, W.; Guo, Y.; Li, C.; Hong, K. Diallyl trisulfide protects motor neurons from the neurotoxic protein TDP-43 via activating lysosomal degradation and the antioxidant response. Neurochem. Res., 2018, 43(12), 2304-2312. doi: 10.1007/s11064-018-2651-3 PMID: 30317421
  157. Silva-Islas, C.A.; Chánez-Cárdenas, M.E.; Barrera-Oviedo, D.; Ortiz-Plata, A.; Pedraza-Chaverri, J.; Maldonado, P.D. Diallyl trisulfide protects rat brain tissue against the damage induced by ischemia-reperfusion through the Nrf2 pathway. Antioxidants, 2019, 8(9), 410. doi: 10.3390/antiox8090410 PMID: 31540440
  158. Zhu, J.; Shen, L.; Lin, X.; Hong, Y.; Feng, Y. Clinical research on traditional chinese medicine compounds and their preparations for amyotrophic lateral sclerosis. Biomed. Pharmacother., 2017, 96, 854-864. doi: 10.1016/j.biopha.2017.09.135 PMID: 29078263
  159. Kumar, V.; Gupta, P.; Hassan, M.I. Mechanism and implications of traditional chinese medicine in amyotrophic lateral sclerosis therapy. J. Proteins Proteomics., 2019, 2019, 1-17. doi: 10.1007/s42485-019-00009-7
  160. Komine, O.; Yamanaka, K. Neuroinflammation in motor neuron disease. Nagoya J. Med. Sci., 2015, 77(4), 537-549. PMID: 26663933
  161. Hooten, K.G.; Beers, D.R.; Zhao, W.; Appel, S.H. Protective and toxic neuroinflammation in amyotrophic lateral sclerosis. Neurotherapeutics, 2015, 12(2), 364-375. doi: 10.1007/s13311-014-0329-3 PMID: 25567201
  162. Liu, J.; Wang, F. Role of neuroinflammation in amyotrophic lateral sclerosis: Cellular mechanisms and therapeutic implications. Front. Immunol., 2017, 8, 1005. doi: 10.3389/fimmu.2017.01005 PMID: 28871262
  163. Süssmuth, S.; Brettschneider, J.; Ludolph, A.; Tumani, H. Biochemical markers in CSF of ALS patients. Curr. Med. Chem., 2008, 15(18), 1788-1801. doi: 10.2174/092986708785133031 PMID: 18691039
  164. Philips, T.; Robberecht, W. Neuroinflammation in amyotrophic lateral sclerosis: role of glial activation in motor neuron disease. Lancet Neurol., 2011, 10(3), 253-263. doi: 10.1016/S1474-4422(11)70015-1 PMID: 21349440
  165. Peric, M.; Mitrecic, D.; Andjus, P.R. Targeting astrocytes for treatment in amyotrophic lateral sclerosis. Curr. Pharm. Des., 2018, 23(33), 23. doi: 10.2174/1381612823666170615110446 PMID: 28619002
  166. Liu, E.; Karpf, L.; Bohl, D. Neuroinflammation in amyotrophic lateral sclerosis and frontotemporal dementia and the interest of induced pluripotent stem cells to study immune cells interactions with neurons. Front. Mol. Neurosci., 2021, 14, 767041. doi: 10.3389/fnmol.2021.767041 PMID: 34970118
  167. Yang, C.; Zhang, X.; Fan, H.; Liu, Y. Curcumin upregulates transcription factor Nrf2, HO-1 expression and protects rat brains against focal ischemia. Brain Res., 2009, 1282, 133-141. doi: 10.1016/j.brainres.2009.05.009 PMID: 19445907
  168. Sikora, E.; Scapagnini, G.; Barbagallo, M. Curcumin, inflammation, ageing and age-related diseases. Immun. Ageing, 2010, 7(1), 1. doi: 10.1186/1742-4933-7-1 PMID: 20205886
  169. Chico, L.; Ienco, E.; Bisordi, C.; Gerfo, A.; Schirinzi, E.; Siciliano, G. Curcumin as an ROS scavenger in amyotrophic lateral sclerosis. React. Oxyg. Species, 2016, 2(5) doi: 10.20455/ros.2016.861
  170. Bedlack, R. ALSUntangled 44: curcumin. Amyotroph. Lateral Scler. Frontotemporal Degener., 2018, 19(7-8), 623-629. doi: 10.1080/21678421.2018.1440738 PMID: 29493344
  171. Adami, R.; Bottai, D. Curcumin and neurological diseases. Nutr. Neurosci., 2022, 25(3), 441-461. doi: 10.1080/1028415X.2020.1760531 PMID: 32441587
  172. Bi, X.L.; Yang, J.Y.; Dong, Y.X.; Wang, J.M.; Cui, Y.H.; Ikeshima, T.; Zhao, Y.Q.; Wu, C.F. Resveratrol inhibits nitric oxide and TNF-α production by lipopolysaccharide-activated microglia. Int. Immunopharmacol., 2005, 5(1), 185-193. doi: 10.1016/j.intimp.2004.08.008 PMID: 15589480
  173. Meng, X.L.; Yang, J.Y.; Chen, G.L.; Wang, L.H.; Zhang, L.J.; Wang, S.; Li, J.; Wu, C.F. Effects of resveratrol and its derivatives on lipopolysaccharide-induced microglial activation and their structure-activity relationships. Chem. Biol. Interact., 2008, 174(1), 51-59. doi: 10.1016/j.cbi.2008.04.015 PMID: 18513711
  174. Morita, T. Celastrol: A new therapeutic potential of traditional Chinese medicine. Am. J. Hypertens., 2010, 23(8), 821-821. doi: 10.1038/ajh.2010.87 PMID: 20644533
  175. Venkatesha, S.H.; Dudics, S.; Astry, B.; Moudgil, K.D. Control of autoimmune inflammation by celastrol, a natural triterpenoid. Pathog. Dis., 2016, 74(6), ftw059. doi: 10.1093/femspd/ftw059 PMID: 27405485
  176. Kiaei, M.; Kipiani, K.; Petri, S.; Chen, J.; Calingasan, N.Y.; Beal, M.F. Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis. Neurodegener. Dis., 2005, 2(5), 246-254. doi: 10.1159/000090364 PMID: 16909005
  177. Jung, H.W.; Chung, Y.S.; Kim, Y.S.; Park, Y.K. Celastrol inhibits production of nitric oxide and proinflammatory cytokines through MAPK signal transduction and NF-κB in LPS-stimulated BV-2 microglial cells. Exp. Mol. Med., 2007, 39(6), 715-721. doi: 10.1038/emm.2007.78 PMID: 18160842
  178. Zhang, R.; Zhu, Y.; Dong, X.; Liu, B.; Zhang, N.; Wang, X.; Liu, L.; Xu, C.; Huang, S.; Chen, L. Celastrol attenuates cadmium-induced neuronal apoptosis via inhibiting Ca2+-CaMKII-Dependent Akt/mTOR pathway. J. Cell. Physiol., 2017, 232(8), 2145-2157. doi: 10.1002/jcp.25703 PMID: 27891586
  179. Jin, X.; Wang, J.; Xia, Z.M.; Shang, C.H.; Chao, Q.L.; Liu, Y.R.; Fan, H.Y.; Chen, D.Q.; Qiu, F.; Zhao, F. Anti-inflammatory and anti-oxidative activities of paeonol and its metabolites through blocking MAPK/ERK/p38 signaling pathway. Inflammation, 2016, 39(1), 434-446. doi: 10.1007/s10753-015-0265-3 PMID: 26433578
  180. Wang, X.; Zhu, G.; Yang, S.; Wang, X.; Cheng, H.; Wang, F.; Li, X.; Li, Q. Paeonol prevents excitotoxicity in rat pheochromocytoma PC12 cells via downregulation of ERK activation and inhibition of apoptosis. Planta Med., 2011, 77(15), 1695-1701. doi: 10.1055/s-0030-1271033 PMID: 21509715
  181. Tseng, Y.T.; Hsu, Y.Y.; Shih, Y.T.; Lo, Y.C. Paeonol attenuates microglia-mediated inflammation and oxidative stress-induced neurotoxicity in rat primary microglia and cortical neurons. Shock, 2012, 37(3), 312-318. doi: 10.1097/SHK.0b013e31823fe939 PMID: 22089194
  182. He, L.X.; Tong, X.; Zeng, J.; Tu, Y.; Wu, S.; Li, M.; Deng, H.; Zhu, M.; Li, X.; Nie, H.; Yang, L.; Huang, F. Paeonol suppresses neuroinflammatory responses in LPS-activated microglia cells. Inflammation, 2016, 39(6), 1904-1917. doi: 10.1007/s10753-016-0426-z PMID: 27624059
  183. Vu, V.T.; Liu, X.Q.; Nguyen, M.T.; Lin, Y.L.; Kong, L.Y.; Luo, J.G. New obovatol trimeric neolignans with NO inhibitory activity from the leaves of Magnolia officinalis var. biloba. Bioorg. Chem., 2020, 96, 103586. doi: 10.1016/j.bioorg.2020.103586 PMID: 31982819
  184. Ock, J.; Han, H.S.; Hong, S.H.; Lee, S.Y.; Han, Y.M.; Kwon, B.M.; Suk, K. Obovatol attenuates microglia-mediated neuroinflammation by modulating redox regulation. Br. J. Pharmacol., 2010, 159(8), 1646-1662. doi: 10.1111/j.1476-5381.2010.00659.x PMID: 20397299
  185. Liu, J.; Su, G.; Gao, J.; Tian, Y.; Liu, X.; Zhang, Z. Effects of peroxiredoxin 2 in neurological disorders: A review of its molecular mechanisms. Neurochem. Res., 2020, 45(4), 720-730. doi: 10.1007/s11064-020-02971-x PMID: 32002772
  186. Yuan, D.; Ma, B.; Yang, J.; Xie, Y.; Wang, L.; Zhang, L.; Kano, Y.; Wu, C. Anti-inflammatory effects of rhynchophylline and isorhynchophylline in mouse N9 microglial cells and the molecular mechanism. Int. Immunopharmacol., 2009, 9(13-14), 1549-1554. doi: 10.1016/j.intimp.2009.09.010 PMID: 19781666
  187. Lee, H.; Kim, Y.O.; Kim, H.; Kim, S.Y.; Noh, H.S.; Kang, S.S.; Cho, G.J.; Choi, W.S.; Suk, K. Flavonoid wogonin from medicinal herb is neuroprotective by inhibiting inflammatory activation of microglia. FASEB J., 2003, 17(13), 1-21. doi: 10.1096/fj.03-0057fje PMID: 12897065
  188. Du, Z.Y.; Li, X.Y. Inhibitory effects of ginkgolides on nitric oxide production in neonatal rat microglia in vitro. Chung Kuo Yao Li Hsueh Pao, 1998, 19(5), 467-470. PMID: 10375812
  189. Wang, L.; Lei, Q.; Zhao, S.; Xu, W.; Dong, W.; Ran, J.; Shi, Q.; Fu, J.; Ginkgolide, B. Ginkgolide B maintains calcium homeostasis in hypoxic hippocampal neurons by inhibiting calcium influx and intracellular calcium release. Front. Cell. Neurosci., 2021, 14, 627846. doi: 10.3389/fncel.2020.627846 PMID: 33679323
  190. Huang, L.; Shi, Y.; Zhao, L.; Ginkgolide, B. Alleviates learning and memory impairment in rats with vascular dementia by reducing neuroinflammation via regulating NF-ₖB pathway. Front. Pharmacol., 2021, 12.
  191. Sun, M.; Sheng, Y.; Zhu, Y.; Ginkgolide, B. Ginkgolide B alleviates the inflammatory response and attenuates the activation of LPS induced BV2 cells in vitro and in vivo. Exp. Ther. Med., 2021, 21(6), 586. doi: 10.3892/etm.2021.10018 PMID: 33850558
  192. Briones, M.R.S.; Snyder, A.M.; Ferreira, R.C.; Neely, E.B.; Connor, J.R.; Broach, J.R. A possible role for platelet-activating factor receptor in amyotrophic lateral sclerosis treatment. Front. Neurol., 2018, 9, 39. doi: 10.3389/fneur.2018.00039 PMID: 29472887
  193. Ko, H.M.; Koppula, S.; Kim, B.W.; Kim, I.S.; Hwang, B.Y.; Suk, K.; Park, E.J.; Choi, D.K. Inflexin attenuates proinflammatory responses and nuclear factor-κB activation in LPS-treated microglia. Eur. J. Pharmacol., 2010, 633(1-3), 98-106. doi: 10.1016/j.ejphar.2010.02.011 PMID: 20159010
  194. Ha, S.K.; Moon, E.; Kim, S.Y. Chrysin suppresses LPS-stimulated proinflammatory responses by blocking NF-κB and JNK activations in microglia cells. Neurosci. Lett., 2010, 485(3), 143-147. doi: 10.1016/j.neulet.2010.08.064 PMID: 20813161
  195. Grewer, C.; Rauen, T. Electrogenic glutamate transporters in the CNS: molecular mechanism, pre-steady-state kinetics, and their impact on synaptic signaling. J. Membr. Biol., 2005, 203(1), 1-20. doi: 10.1007/s00232-004-0731-6 PMID: 15834685
  196. Foran, E.; Trotti, D. Glutamate transporters and the excitotoxic path to motor neuron degeneration in amyotrophic lateral sclerosis. Antioxid. Redox Signal., 2009, 11(7), 1587-1602. doi: 10.1089/ars.2009.2444 PMID: 19413484
  197. Choi, D.W. Glutamate receptors and the induction of excitotoxic neuronal death. Prog. Brain Res., 1994, 100, 47-51. doi: 10.1016/S0079-6123(08)60767-0
  198. Cheah, B.C.; Vucic, S.; Krishnan, A.; Kiernan, M.C. Riluzole, neuroprotection and amyotrophic lateral sclerosis. Curr. Med. Chem., 2010, 17(18), 1942-1959. doi: 10.2174/092986710791163939 PMID: 20377511
  199. Rothstein, J.D.; Tsai, G.; Kuncl, R.W.; Clawson, L.; Cornblath, D.R.; Drachman, D.B.; Pestronk, A.; Stauch, B.L.; Coyle, J.T. Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis. Ann. Neurol., 1990, 28(1), 18-25. doi: 10.1002/ana.410280106 PMID: 2375630
  200. Plaitakis, A.; Constantakakis, E. Altered metabolism of excitatory amino acids, N-acetyl-aspartate and N-acetyl-aspartylglutamate in amyotrophic lateral sclerosis. Brain Res. Bull., 1993, 30(3-4), 381-386. doi: 10.1016/0361-9230(93)90269-H PMID: 8457887
  201. Ferrarese, C.; Sala, G.; Riva, R.; Begni, B.; Zoia, C.; Tremolizzo, L.; Galimberti, G.; Millul, A.; Bastone, A.; Mennini, T.; Balzarini, C.; Frattola, L.; Beghi, E. Decreased platelet glutamate uptake in patients with amyotrophic lateral sclerosis. Neurology, 2001, 56(2), 270-272. doi: 10.1212/WNL.56.2.270 PMID: 11160972
  202. Cho, J.; Ho Kim, Y.; Kong, J.Y.; Ha, Yang C.; Gook Park, C. Protection of cultured rat cortical neurons from excitotoxicity by asarone, a major essential oil component in the rhizomes of Acorus gramineus. Life Sci., 2002, 71(5), 591-599. doi: 10.1016/S0024-3205(02)01729-0 PMID: 12052443
  203. Chen, Y.Z.; Wang, Q.W.; Liang, Y.; Fang, Y.Q. Protective effects of beta-asarone on cultured rat cortical neurons damage induced by glutamate. Zhong Yao Cai, 2007, 30(4), 436-439. PMID: 17674798
  204. Jiang, B.; Liu, J.H.; Bao, Y.M.; An, L.J. Catalpol inhibits apoptosis in hydrogen peroxide-induced PC12 cells by preventing cytochrome c release and inactivating of caspase cascade. Toxicon, 2004, 43(1), 53-59. doi: 10.1016/j.toxicon.2003.10.017 PMID: 15037029
  205. Ved, H.S.; Koenig, M.L.; Dave, J.R.; Doctor, B.P. Huperzine A, a potential therapeutic agent for dementia, reduces neuronal cell death caused by glutamate. Neuroreport, 1997, 8(4), 963-967. doi: 10.1097/00001756-199703030-00029 PMID: 9141073
  206. Gordon, R.K.; Nigam, S.V.; Weitz, J.A.; Dave, J.R.; Doctor, B.P.; Ved, H.S. The NMDA receptor ion channel: A site for binding of huperzine A. J. Appl. Toxicol., 2001, 21(S1), S47-S51. doi: 10.1002/jat.805 PMID: 11920920
  207. Hemendinger, R.A.; Armstrong, E.J., III; Persinski, R.; Todd, J.; Mougeot, J.L.; Volvovitz, F.; Rosenfeld, J. Huperzine a provides neuroprotection against several cell death inducers using in vitro model systems of motor neuron cell death. Neurotox. Res., 2008, 13(1), 49-61. doi: 10.1007/BF03033367 PMID: 18367440
  208. Wang, C.J.; Hu, C.P.; Xu, K.P.; Yuan, Q.; Li, F.S.; Zou, H.; Tan, G.S.; Li, Y.J. Protective effect of selaginellin on glutamate-induced cytotoxicity and apoptosis in differentiated PC12 cells. Naunyn Schmiedebergs Arch. Pharmacol., 2010, 381(1), 73-81. doi: 10.1007/s00210-009-0470-4 PMID: 19936711
  209. Zhang, F.; Zheng, W.; Pi, R.; Mei, Z.; Bao, Y.; Gao, J.; Tang, W.; Chen, S.; Liu, P. Cryptotanshinone protects primary rat cortical neurons from glutamate-induced neurotoxicity via the activation of the phosphatidylinositol 3-kinase/Akt signaling pathway. Exp. Brain Res., 2009, 193(1), 109-118. doi: 10.1007/s00221-008-1600-9 PMID: 18936923
  210. Kanekura, K.; Hashimoto, Y.; Kita, Y.; Sasabe, J.; Aiso, S.; Nishimoto, I.; Matsuoka, M.A. Rac1/phosphatidylinositol 3-kinase/Akt3 anti-apoptotic pathway, triggered by AlsinLF, the product of the ALS2 gene, antagonizes Cu/Zn-superoxide dismutase (SOD1) mutant-induced motoneuronal cell death. J. Biol. Chem., 2005, 280(6), 4532-4543. doi: 10.1074/jbc.M410508200 PMID: 15579468
  211. Chang, M.X.; Xu, L.Y.; Tao, J.S.; Feng, Y. Metabolism and pharmacokinetics of ferulic acid in rats. Zhongguo Zhongyao Zazhi, 1993, 18(5), 300-302, 319. PMID: 8216807
  212. Jin, Y.; Yan, E.; Fan, Y.; Guo, X.; Zhao, Y.; Zong, Z.; Liu, Z. Neuroprotection by sodium ferulate against glutamate-induced apoptosis is mediated by ERK and PI3 kinase pathways. Acta Pharmacol. Sin., 2007, 28(12), 1881-1890. doi: 10.1111/j.1745-7254.2007.00634.x PMID: 18031600
  213. Ren, Z.; Zhang, R.; Li, Y.; Li, Y.; Yang, Z.; Yang, H. Ferulic acid exerts neuroprotective effects against cerebral ischemia/reperfusion-induced injury via antioxidant and anti-apoptotic mechanisms in vitro and in vivo. Int. J. Mol. Med., 2017, 40(5), 1444-1456. doi: 10.3892/ijmm.2017.3127 PMID: 28901374
  214. Nakayama, H.; Nakahara, M.; Matsugi, E.; Soda, M.; Hattori, T.; Hara, K.; Usami, A.; Kusumoto, C.; Higashiyama, S.; Kitaichi, K. Protective effect of ferulic acid against hydrogen peroxide induced apoptosis in PC12 cells. Molecules, 2020, 26(1), 90. doi: 10.3390/molecules26010090 PMID: 33379243
  215. Yingzhu, CHEN.; Yongjian, GU.; Shiyao, BAO. Protective effects of acanthopanax senticousus saponins on cortical neuronal ischemia-hypoxia injury. J. Clin. Neurol., 1988, 6, 84-87.
  216. Diao, H-X.; Song, S-L.; Liang, H.; Wang, Y-S.; Wang, W-L.; Ji, A-G. Protective effect of polysaccharides from sea cucumber on glu-induced neurotoxicity in PC12 cells. Zhong Yao Cai, 2009, 32(3), 398-400. PMID: 19565721
  217. Guatteo, E.; Carunchio, I.; Pieri, M.; Albo, F.; Canu, N.; Mercuri, N.B.; Zona, C. Altered calcium homeostasis in motor neurons following AMPA receptor but not voltage-dependent calcium channels’ activation in a genetic model of amyotrophic lateral sclerosis. Neurobiol. Dis., 2007, 28(1), 90-100. doi: 10.1016/j.nbd.2007.07.002 PMID: 17706428
  218. Van Den Bosch, L.; Vandenberghe, W.; Klaassen, H.; Van Houtte, E.; Robberecht, W. Ca2+-permeable AMPA receptors and selective vulnerability of motor neurons. J. Neurol. Sci., 2000, 180(1-2), 29-34. doi: 10.1016/S0022-510X(00)00414-7 PMID: 11090861
  219. Prell, T.; Lautenschläger, J.; Grosskreutz, J. Calcium-dependent protein folding in amyotrophic lateral sclerosis. Cell Calcium, 2013, 54(2), 132-143. doi: 10.1016/j.ceca.2013.05.007 PMID: 23764168
  220. Hammadi, M.; Oulidi, A.; Gackière, F.; Katsogiannou, M.; Slomianny, C.; Roudbaraki, M.; Dewailly, E.; Delcourt, P.; Lepage, G.; Lotteau, S.; Ducreux, S.; Prevarskaya, N.; Van Coppenolle, F. Modulation of ER stress and apoptosis by endoplasmic reticulum calcium leak via translocon during unfolded protein response: Involvement of GRP78. FASEB J., 2013, 27(4), 1600-1609. doi: 10.1096/fj.12-218875 PMID: 23322163
  221. Grosskreutz, J.; Van Den Bosch, L.; Keller, B.U. Calcium dysregulation in amyotrophic lateral sclerosis. Cell Calcium, 2010, 47(2), 165-174. doi: 10.1016/j.ceca.2009.12.002 PMID: 20116097
  222. Mao, Q.Q.; Zhong, X.M.; Feng, C.R.; Pan, A.J.; Li, Z.Y.; Huang, Z. Protective effects of paeoniflorin against glutamate-induced neurotoxicity in PC12 cells via antioxidant mechanisms and Ca2+ antagonism. Cell. Mol. Neurobiol., 2010, 30(7), 1059-1066. doi: 10.1007/s10571-010-9537-5 PMID: 20577899
  223. Mao, Q.Q.; Zhong, X.M.; Li, Z.Y.; Huang, Z. Paeoniflorin protects against NMDA-induced neurotoxicity in PC12 cells via Ca2+ antagonism. Phytother. Res., 2011, 25(5), 681-685. doi: 10.1002/ptr.3321 PMID: 21043034
  224. You, J.; Tan, T.; Kuang, A.; Zhong, Y.; He, S. Biodistribution and metabolism of 3h-gastrodigenin and 3H-gastrodin in mice. J. West China Univ. Med. Sci., 1994, 25, 325-328.
  225. Chen, W.D.; Lu, X.L. Effect of gastrodin on release of glutamate from cultured nerve cells induced by potassium chloride. Chin. J. Nat. Med., 2000, 2, 8-10.
  226. Sun, R.; Zhang, Z.; Huang, W.; Lv, L.; Yin, J. Protective effects and machanism of muskone on pheochromocytoma cell injure induced by glutamate. Zhongguo Zhongyao Zazhi, 2009, 34(13), 1701-1704. PMID: 19873786
  227. Shu-li, S. Effects of ligustrazine on L-type calcium current in SH-SY5Y human neuroblastoma. Chinese J. Neuroimmunol. Neurol., 2004, 11, 43-45.

Supplementary files

Supplementary Files
Action
1. JATS XML
Download

Copyright (c) 2024 Bentham Science Publishers