Treatment with a Ginkgo biloba extract, EGb 761, inhibits excitotoxicity in an animal model of spinocerebellar ataxia type 17

Drug Design, Development and Therapy

Volumn 10, Issue , 2016, Pages 723-731

  Huang, Ding Siang ^a   Lin, Hsuan Yuan ^a,b   Lee Chen, Guey Jen ^a   Hsieh Li, Hsiu Mei ^a   Wu, Chung Hsin ^a   Lin, Jung Yaw ^a,b  

^a NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Apoptosis; EGb 761; Excitotoxicity; PolyQ diseases; Spinocerebellar ataxia type 17

Indexed keywords

GINKGO BILOBA EXTRACT; CALCIUM; GLUTAMIC ACID; PLANT EXTRACT;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; CONTROLLED STUDY; DRUG MECHANISM; EXCITOTOXICITY; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MOTOR PERFORMANCE; MOUSE; NONHUMAN; PROTEIN EXPRESSION; PSYCHOMOTOR DISORDER; SPINOCEREBELLAR DEGENERATION; ANIMAL; APOPTOSIS; DISEASE MODEL; DRUG EFFECTS; METABOLISM; PATHOLOGY; SPINOCEREBELLAR ATAXIAS; TRANSGENIC MOUSE; TUMOR CELL LINE;

ANIMALS; APOPTOSIS; CALCIUM; CELL LINE, TUMOR; DISEASE MODELS, ANIMAL; GLUTAMIC ACID; HUMANS; MICE; MICE, TRANSGENIC; PLANT EXTRACTS; SPINOCEREBELLAR ATAXIAS;

EID: 84959457314     PISSN: None     EISSN: 11778881     Source Type: Journal    
DOI: 10.2147/DDDT.S98156     Document Type: Article

References (26)

1. Fujigasaki H, Martin JJ, DeDeyn PP, et al. CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia. Brain. 2001;124:1939–1947.
2. Nakamura K, Jeong SY, Uchihara T, et al. SCA 17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum Mol Genet. 2001;10(14):1441–1448.
3. Zühlke C, Hellenbroich Y, Dalski A, et al. Different types of repeat expansion in the TATA-binding protein gene are associated with a new form of inherited ataxia. Eur J Hum Genet. 2001;9(3):160–164.
4. Koch P, Breuer P, Peitz M, et al. Excitation-induced ataxin-3 aggregation in neurons from patients with Machado-Joseph disease. Nature. 2011;480(7378):543–546.
5. Hübener J, Weber JJ, Richter C, et al. Calpain-mediated ataxin-3 cleavage in the molecular pathogenesis of spinocerebellar ataxia type 3 (SCA3). Hum Mol Genet. 2013;22(3):508–518.
6. Simoes AT, Goncalves N, Koeppen A, et al. Calpastatin-mediated inhibition of calpains in the mouse brain prevents mutant ataxin 3 proteolysis, nuclear localization and aggregation, relieving Machado-Joseph disease. Brain. 2012;135(pt 8):2428–2439.
7. Tang TS, Tu H, Chan EY, et al. Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron. 2003;39(2):227–239.
8. Tang TS, Slow E, Lupu V, et al. Disturbed Ca2+ signaling and apoptosis of medium spiny neurons in Huntington’s disease. Proc Natl Acad Sci U S A. 2005;102(7):2602–2607.
9. Ramassamy C. Emerging role of polyphenolic compounds in the treatment of neurodegenerative diseases: a review of their intracellular targets. Eur J Pharmacol. 2006;545(1):51–64.
10. Chandrasekaran K, Mehrabian Z, Spinnewyn B, Drieu K, Fiskum G. Neuroprotective effects of bilobalide, a component of the Ginkgo biloba extract (EGb 761), in gerbil global brain ischemia. Brain Res. 2001;922(2):282–292.
11. Oyama Y, Chikahisa L, Ueha T, Kanemaru K, Noda K. Ginkgo biloba extract protects brain neurons against oxidative stress induced by hydrogen peroxide. Brain Res. 1996;712(2):349–352.
12. Bastianetto S, Ramassamy C, Doré S, Christen Y, Poirier J, Quirion R. The Ginkgo biloba extract (EGb 761) protects hippocampal neurons against cell death induced by beta-amyloid. Eur J Neurosci. 2000;12(6):1882–1890.
13. Diamond BJ, Shiflett SC, Feiwel N, et al. Ginkgo biloba extract: mechanisms and clinical indications. Arch Phys Med Rehabil. 2000;81(5):668–678.
14. Kung PJ, Tao YC, Hsu HC, et al. Indole and synthetic derivative activate chaperone expression to reduce polyQ aggregation in SCA 17 neuronal cell and slice culture models. Drug Des Devel Ther. 2014;8:1929–1939.
15. Chang YC, Lin CY, Hsu CM, et al. Neuroprotective effects of granulocyte-colony stimulating factor in a novel transgenic mouse model of SCA 17. J Neurochem. 2011;118(2):288–303.
16. Rothman SM, Olney JW. Excitotoxicity and the NMDA receptor – still lethal after eight years. Trends Neurosci. 1995;18(2):57–58.
17. Sun ZW, Zhang L, Zhu SJ, Chen WC, Mei B. Excitotoxicity effects of glutamate on human neuroblastoma SH-SY5Y cells via oxidative damage. Neurosci Bull. 2010;26(1):8–16.
18. Miao Y, Dong LD, Chen J, Hu XC, Yang XL, Wang Z. Involvement of calpain/p35-p25/Cdk5/NMDAR signaling pathway in glutamate-induced neurotoxicity in cultured rat retinal neurons. PLoS One. 2012;7(8):e42318.
19. Hardwick JM, Soane L. Multiple functions of BCL-2 family proteins. Cold Spring Harb Perspect Biol. 2013;5(2):a008722.
20. Koch E, Nöldner M, Leuschner J. Reproductive and developmental toxicity of the Ginkgo biloba special extract EGb 761 in mice. Phytomedicine. 2013;12(1):90–97.
21. Mdzinarishvili A, Sumbria R, Lang D, Klein J. Ginkgo extract EGb 761 confers neuroprotection by reduction of glutamate release in ischemic brain. J Pharm Pharm Sci. 2012;15(1):94–102.
22. Rojas P, Serrano-García N, Mares-Sámano JJ, Medina-Campos ON, Pedraza-Chaverri J, Ogren SO. EGb761 protects against nigrostriatal dopaminergic neurotoxicity in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinsonism in mice: role of oxidative stress. Eur J Neurosci. 2008;28(1):41–50.
23. Barski JJ, Hartmann J, Rose CR, et al. Calbindin in cerebellar Purkinje cells is a critical determinant of the precision of motor coordination. J Neurosci. 2003;23(8):3469–3477.
24. Whitney ER, Kemper TL, Rosene DL, Bauman ML, Blatt GJ. Calbindin-D28k is a more reliable marker of human Purkinje cells than standard Nissl stains: a stereological experiment. J Neurosci Methods. 2008;168(1):42–47.
25. Park SH, Kukushkin Y, Gupta R, et al. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell. 2013;154(1):134–145.
26. Ross C, Poirier M. Protein aggregation and neurodegenerative disease. Nat Med. 2004;10(suppl):10–17.