Amelioration of Alzheimer’s disease by neuroprotective effect of sulforaphane in animal model

References

• Markesbery WR. Oxidative stress hypothesis in Alzheimer's disease. Free Radical Bio Med 1997;23:134–47
   PubMed Web of Science ®Google Scholar
• Frank B, Gupta S. A review of antioxidants and Alzheimer's disease. Ann Clin Psychiatry 2005;17:269–86
   PubMedGoogle Scholar
• Kim Y, Lee JH, Ryu J, Kim DJ. Multivalent & multifunctional ligands to beta-amyloid. Curr Pharm Des 2009;15:637–58
   PubMedGoogle Scholar
• Butterfield DA. Amyloid beta-peptide (1–42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic Res 2002;36:1307–13
   PubMed Web of Science ®Google Scholar
• Choi SJ, Kim MJ, Heo HJ, Hong B, Cho HY, Kim YJ, Kim HK, et al. Ameliorating effect of Gardenia jasminoides extract on amyloid beta peptide-induced neuronal cell deficit. Mol Cell 2007;24:113–8
   Google Scholar
• LaFerla FM, Green KN, Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 2007;8:499–509
   PubMed Web of Science ®Google Scholar
• Sondag CM, Dhawan G, Combs CK. Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia. J Neuroinflammation 2009;6:1
   PubMed Web of Science ®Google Scholar
• Klein WL, Krafft GA, Finch CE. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 2001;24:219–24
   PubMed Web of Science ®Google Scholar
• Lue LF, Kuo YM, Roher AE, Brachova L, Shen Y, Sue L, Beach T, et al. Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol 1999;155:853–62
   PubMed Web of Science ®Google Scholar
• Butterfield DA, Drake J, Pocernich C, Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol Med 2001;7:548–54
   PubMed Web of Science ®Google Scholar
• Tabner BJ, Turnbull S, El-Agnaf O, Allsop D. Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases. Curr Top Med Chem 2001;1:507–17
   PubMedGoogle Scholar
• Wruck CJ, Gotz ME, Herdegen T, Varoga D, Brandenburg LO, Pufe T. Kavalactones protect neural cells against amyloid beta peptide-induced neurotoxicity via extracellular signal-regulated kinase 1/2-dependent nuclear factor erythroid 2-related factor 2 activation. Mol Pharmacol 2008;73:1785–95
   PubMed Web of Science ®Google Scholar
• Varadarajan S, Yatin S, Aksenova M, Butterfield DA. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 2000;130:184–208
   PubMed Web of Science ®Google Scholar
• Zhou CC, Poulton EJ, Grun F, Bammler TK, Blumberg B, Thummel KE, Eaton DL. The dietary isothiocyanate sulforaphane is an antagonist of the human steroid and xenobiotic nuclear receptor. Mol Pharmacol 2007;71:220–9
   PubMed Web of Science ®Google Scholar
• Balasubramanian S, Chew YC, Eckert RL. Sulforaphane suppresses polycomb group protein level via a proteasome-dependent mechanism in skin cancer cells. Mol Pharmacol 2011;80:870–8
   Google Scholar
• Scott O, Galicia-Connolly E, Adams D, Surette S, Vohra S, Yager JY. The safety of cruciferous plants in humans: a systematic review. J Biomed Biotechnol 2012;2012:503241
   Google Scholar
• Park HM, Kim JA, Kwak MK. Protection against amyloid beta cytotoxicity by sulforaphane: role of the proteasome. Arch Pharm Res 2009;32:109–15
   PubMed Web of Science ®Google Scholar
• Elbarbry F, Elrody N. Potential health benefits of sulforaphane: a review of the experimental, clinical and epidemiological evidences and underlying mechanisms. J Med Plants Res 2011;5:473–84
   Google Scholar
• Fahey JW, Talalay P. Antioxidant functions of sulforaphane: a potent inducer of phase II detoxication enzymes. Food Chem Toxicol 1999;37:973–79
   PubMed Web of Science ®Google Scholar
• Gan N, Wu YC, Brunet M, Garrido C, Chung FL, Dai C, Mi L. Sulforaphane activates heat shock response and enhances proteasome activity through up-regulation of Hsp27. J Biol Chem 2010;285:35528–36
   PubMed Web of Science ®Google Scholar
• Heiss E, Herhaus C, Klimo K, Bartsch H, Gerhauser C. Nuclear factor kappa B is a molecular target for sulforaphane-mediated anti-inflammatory mechanisms. J Biol Chem 2001;276:32008–15
   PubMed Web of Science ®Google Scholar
• Choi JW, Kim HY, Jeon M, Kim DJ, Kim Y. Efficient access to highly pure beta-amyloid peptide by optimized solid-phase synthesis. Amyloid 2012;19:133–7
   PubMed Web of Science ®Google Scholar
• Kim YS, Moss JA, Janda KD. Biological tuning of synthetic tactics in solid-phase synthesis: application to A beta(1-42). J Org Chem 2004;69:7776–8
   PubMedGoogle Scholar
• Maurice T, Lockhart BP, Privat A. Amnesia induced in mice by centrally administered beta-amyloid peptides involves cholinergic dysfunction. Brain Res 1996;706:181–93
   PubMed Web of Science ®Google Scholar
• Kim HY, Kim Y, Han G, Kim DJ. Regulation of in vitro Abeta1-40 aggregation mediated by small molecules. J Alzheimers’ Dis 2010;22:73–85
   PubMedGoogle Scholar
• Harris JR. In vitro fibrillogenesis of the amyloid beta 1–42 peptide: cholesterol potentiation and aspirin inhibition. Micron 2002;33:609–26
   Google Scholar
• Bryan KJ, Lee H, Perry G, Smith MA, Casadesus G. Transgenic mouse models of Alzheimer's disease: behavioral testing and considerations. In: Buccafusco JJ, ed. Methods of behavior analysis in neuroscience. 2nd ed. Florida: Boca Raton; 2009:1–18
   Google Scholar
• Yan JJ, Cho JY, Kim HS, Kim KL, Jung JS, Huh SO, Suh HW, et al. Protection against beta-amyloid peptide toxicity in vivo with long-term administration of ferulic acid. Br J Pharmacol 2001;133:89–96
   PubMed Web of Science ®Google Scholar
• Ader R, Moleman P, Weijnen JAW. Retention of a passive avoidance response as a function of intensity and duration of electric shock. Psychon Sci 1972;26:125–8
   Google Scholar
• Khurana R, Coleman C, Ionescu-Zanetti C, Carter SA, Krishna V, Grover RK, Roy R, et al. Mechanism of thioflavin T binding to amyloid fibrils. J Struct Biol 2005;151:229–38
   PubMed Web of Science ®Google Scholar
• LeVine H 3rd. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 1993;2:404–10
   PubMed Web of Science ®Google Scholar
• Jin Y, Wang M, Rosen RT, Ho CT. Thermal degradation of sulforaphane in aqueous solution. J Agric Food Chem 1999;47:3121–3
   PubMed Web of Science ®Google Scholar
• Van Eylen D, Oey I, Hendrickx M, Van Loey A. Kinetics of the stability of broccoli (Brassica oleracea Cv. Italica) myrosinase and isothiocyanates in broccoli juice during pressure/temperature treatments. J Agric Food Chem 2007;55:2163–70
   PubMed Web of Science ®Google Scholar
• Selkoe DJ, Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Ann Rev Pharmacol Toxicol 2003;43:545–84
   PubMed Web of Science ®Google Scholar
• Uttara B, Singh AV, Zamboni P, Mahajan RT. Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr Neuropharmacol 2009;7:65–74
   PubMed Web of Science ®Google Scholar
• Tufekci KU, Civi Bayin E, Genc S, Genc K. The Nrf2/ARE pathway: a promising target to counteract mitochondrial dysfunction in Parkinson's disease. Parkinsons Dis 2011;2011:314082
   PubMedGoogle Scholar
• Bergstrom P, Andersson HC, Gao Y, Karlsson JO, Nodin C, Anderson MF, Nilsson M, et al. Repeated transient sulforaphane stimulation in astrocytes leads to prolonged Nrf2-mediated gene expression and protection from superoxide-induced damage. Neuropharmacology 2011;60:343–53
   PubMed Web of Science ®Google Scholar