The aqueous extract of Glycyrrhiza inflata can upregulate unfolded protein response-mediated chaperones to reduce tau misfolding in cell models of Alzheimer’s disease

Drug Design, Development and Therapy

Volumn 10, Issue , 2016, Pages 885-896

  Chang, Kuo Hsuan ^a   Chen, I Cheng ^a   Lin, Hsuan Yuan ^b   Chen, Hsuan Chiang ^b   Lin, Chih Hsin ^a   Lin, Te Hsien ^b   Weng, Yu Ting ^a   Chao, Chih Ying ^a   Wu, Yih Ru ^a   Lin, Jung Yaw ^b   Lee Chen, Guey Jen ^b   Chen, Chiung Mei ^a  

^a CHANG GUNG UNIVERSITY COLLEGE OF MEDICINE   (Taiwan)

^b NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

Author keywords

Alzheimer s disease; G. inflata; Tau misfolding; Tauopathy; TCM extracts; UPR mediated chaperones

Indexed keywords

CHAPERONE; HERBACEOUS AGENT; MAPT PROTEIN, HUMAN; PLANT EXTRACT; TAU PROTEIN; WATER;

ALZHEIMER DISEASE; BIOLOGICAL MODEL; CELL PROLIFERATION; CHEMISTRY; CHINESE MEDICINE; DOSE RESPONSE; DRUG EFFECTS; GLYCYRRHIZA; HEK293 CELL LINE; HUMAN; METABOLISM; NERVE CELL; PATHOLOGY; PHYSIOLOGY; PROTEIN UNFOLDING; STRUCTURE ACTIVITY RELATION; TUMOR CELL LINE; UNFOLDED PROTEIN RESPONSE; UPREGULATION;

ALZHEIMER DISEASE; CELL LINE, TUMOR; CELL PROLIFERATION; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUGS, CHINESE HERBAL; GLYCYRRHIZA; HEK293 CELLS; HUMANS; MEDICINE, CHINESE TRADITIONAL; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; NEURONS; PLANT EXTRACTS; PROTEIN UNFOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; TAU PROTEINS; UNFOLDED PROTEIN RESPONSE; UP-REGULATION; WATER;

EID: 84959568117     PISSN: None     EISSN: 11778881     Source Type: Journal    
DOI: 10.2147/DDDT.S96454     Document Type: Article

References (44)

1. Iqbal K, del C, Alonso A, et al. Tau pathology in Alzheimer disease and other tauopathies. Biochim Biophys Acta. 2005;1739(2–3):198–210.
2. Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev. 2000;33(1):95–130.
3. Weingarten MD, Lockwood AH, Hwo SY, Kirschner MW. A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A. 1975;72(5):1858–1862.
4. Miyata Y, Hoshi M, Nishida E, Minami Y, Sakai H. Binding of microtubule-associated protein 2 and tau to the intermediate filament reassembled from neurofilament 70-kDa subunit protein. Its regulation by calmodulin. J Biol Chem. 1986;261(28):13026–13030.
5. Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Eikelenboom P, Scheper W. The unfolded protein response is activated in pretangle neurons in Alzheimer’s disease hippocampus. Am J Pathol. 2009;174(4):1241–1251.
6. Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334(6059):1081–1086.
7. Abisambra JF, Jinwal UK, Blair LJ, et al. Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation. J Neurosci. 2013;33(22):9498–9507.
8. Goedert M, Spillantini MG, Potier MC, Ulrich J, Crowther RA. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. EMBO J. 1989;8(2):393–399.
9. D’Souza I, Poorkaj P, Hong M, et al. Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc Natl Acad Sci U S A. 1999;96(10):5598–5603.
10. Momeni P, Pittman A, Lashley T, et al. Clinical and pathological features of an Alzheimer’s disease patient with the MAPT ΔK280 mutation. Neurobiol Aging. 2009;30(3):388–393.
11. Khlistunova I, Biernat J, Wang Y, et al. Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J Biol Chem. 2006;281(2):1205–1214.
12. Pickhardt M, Biernat J, Khlistunova I, et al. N-phenylamine derivatives as aggregation inhibitors in cell models of tauopathy. Curr Alzheimer Res. 2007;4(4):397–402.
13. Pickhardt M, Gazova Z, von Bergen M, et al. Anthraquinones inhibit tau aggregation and dissolve Alzheimer’s paired helical filaments in vitro and in cells. J Biol Chem. 2005;280(5):3628–3635.
14. Park CH, Choi SH, Koo JW, et al. Novel cognitive improving and neuroprotective activities of Polygala tenuifolia Willdenow extract, BT-11. J Neurosci Res. 2002;70(3):484–492.
15. Fujiwara H, Iwasaki K, Furukawa K, et al. Uncaria rhynchophylla, a Chinese medicinal herb, has potent antiaggregation effects on Alzheimer’s β-amyloid proteins. J Neurosci Res. 2006;84(2):427–433.
16. Jiang H, Luo X, Bai D. Progress in clinical, pharmacological, chemical and structural biological studies of huperzine A: a drug of traditional Chinese medicine origin for the treatment of Alzheimer’s disease. Curr Med Chem. 2003;10(21):2231–2252.
17. Wischik CM, Edwards PC, Lai RY, Roth M, Harrington CR. Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines. Proc Natl Acad Sci U S A. 1996;93(20):11213–11218.
18. Wischik CM, Staff RT, Wischik DJ, et al. Tau aggregation inhibitor therapy: an exploratory phase 2 study in mild or moderate Alzheimer’s disease. J Alzheimers Dis. 2015;44(2):705–720.
19. Lee LC, Chen CM, Wang PR, Su MT, Lee-Chen GJ, Chang CY. Role of high mobility group box 1 (HMGB1) in SCA17 pathogenesis. PLoS One. 2014;9(12):e115809.
20. Friedhoff P, Schneider A, Mandelkow EM, Mandelkow E. Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry. 1998;37(28):10223–10230.
21. Shaw G, Morse S, Ararat M, Graham FL. Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J. 2002;16(8):869–871.
22. Bandyopadhyay B, Li G, Yin H, Kuret J. Tau aggregation and toxicity in a cell culture model of tauopathy. J Biol Chem. 2007;282(22):16454–16464.
23. Chang E, Honson NS, Bandyopadhyay B, et al. Modulation and detection of tau aggregation with small-molecule ligands. Curr Alzheimer Res. 2009;6(5):409–414.
24. Nakashima H, Ishihara T, Yokota O, et al. Effects of α-tocopherol on an animal model of tauopathies. Free Radic Biol Med. 2004;37(2):176–186.
25. Agholme L, Lindstrom T, Kagedal K, Marcusson J, Hallbeck M. An in vitro model for neuroscience: differentiation of SH-SY5Y cells into cells with morphological and biochemical characteristics of mature neurons. J Alzheimers Dis. 2010;20(4):1069–1082.
26. Cheung YT, Lau WK, Yu MS, et al. Effects of all-trans-retinoic acid on human SH-SY5Y neuroblastoma as in vitro model in neurotoxicity research. Neurotoxicology. 2009;30(1):127–135.
27. Cheung TS, Song TH, Ng TB, et al. Therapeutic effects of herbal chemicals in traditional Chinese medicine on Alzheimer’s disease. Curr Med Chem. 2015;22(19):2392–2403.
28. Mei Z, Zhang F, Tao L, et al. Cryptotanshinone, a compound from Salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates β-amyloid deposition through upregulating α-secretase in vivo and in vitro. Neurosci Lett. 2009;452(2):90–95.
29. Yang F, Lim GP, Begum AN, et al. Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem. 2005;280(7):5892–5901.
30. 25-35-induced oxidative stress and apoptosis in primary cultured hippocampal neurons. Chem Biol Interact. 2015;239:12–18.
31. Kuang P, Wu W, Zhu K. Evidence for amelioration of cellular damage in ischemic rat brain by radix salviae miltiorrhizae treatment – immunocytochemistry and histopathology studies. J Tradit Chin Med. 1993;13(1):38–41.
32. Lee MK, Kim SR, Sung SH, et al. Asiatic acid derivatives protect cultured cortical neurons from glutamate-induced excitotoxicity. Res Commun Mol Pathol Pharmacol. 2000;108(1–2):75–86.
33. Ved HS, Koenig ML, Dave JR, Doctor BP. Huperzine A, a potential therapeutic agent for dementia, reduces neuronal cell death caused by glutamate. Neuroreport. 1997;8(4):963–968.
34. Wang BS, Wang H, Wei ZH, Song YY, Zhang L, Chen HZ. Efficacy and safety of natural acetylcholinesterase inhibitor huperzine A in the treatment of Alzheimer’s disease: an updated meta-analysis. J Neural Transm. 2009;116(4):457–465.
35. Asl MN, Hosseinzadeh H. Review of pharmacological effects of Glycyrrhiza sp. and its bioactive compounds. Phytother Res. 2008;22(6):709–724.
36. Chen CM, Weng YT, Chen WL, et al. Aqueous extract of Glycyrrhiza inflata inhibits aggregation by upregulating PPARGC1A and NFE2L2-ARE pathways in cell models of spinocerebellar ataxia 3. Free Radic Biol Med. 2014;71:339–350.
37. Yim SB, Park SE, Lee CS. Protective effect of glycyrrhizin on 1-methyl-4-phenylpyridinium-induced mitochondrial damage and cell death in differentiated PC12 cells. J Pharmacol Exp Ther. 2007;321(2):816–822.
38. Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 1998;17(19):5708–5717.
39. Iwawaki T, Hosoda A, Okuda T, et al. Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress. Nat Cell Biol. 2001;3(2):158–164.
40. Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, Mikoshiba K. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell. 2005;120(1):85–98.
41. Synofzik M, Haack TB, Kopajtich R, et al. Absence of BiP co-chaperone DNAJC3 causes diabetes mellitus and multisystemic neurodegeneration. Am J Hum Genet. 2014;95(6):689–697.
42. Faria D, Lentze N, Almaca J, et al. Regulation of ENaC biogenesis by the stress response protein SERP1. Pflugers Arch. 2012;463(6):819–827.
43. Yamaguchi A, Hori O, Stern DM, Hartmann E, Ogawa S, Tohyama M. Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. J Cell Biol. 1999;147(6):1195–1204.
44. Hori O, Miyazaki M, Tamatani T, et al. Deletion of SERP1/RAMP4, a component of the endoplasmic reticulum (ER) translocation sites, leads to ER stress. Mol Cell Biol. 2006;26(11):4257–4267.