Gangliosides determine the amyloid pathology of Alzheimer's disease

NeuroReport

Volumn 20, Issue 12, 2009, Pages 1043-1046

  Oikawa, Naoto ^a   Yamaguchi, Haruyasu ^b   Ogino, Koichi ^c   Taki, Takao ^c   Yuyama, Kohei ^a   Yamamoto, Naoki ^a,f   Shin, Ryong Woon ^d   Furukawa, Koichi ^e   Yanagisawa, Katsuhiko ^a  

^a NATIONAL CENTER FOR GERIATRICS AND GERONTOLOGY   (Japan)

^b GUNMA UNIVERSITY   (Japan)

^c OTSUKA PHARMACEUTICAL CO LTD   (Japan)

^d TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^e NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^f RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

Alzheimer's disease; Amyloid; Amyloid protein; Amyloid angiopathy; Ganglioside; Senile plaque

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; GANGLIOSIDE; GANGLIOSIDE GM1; GANGLIOSIDE GM3; SYNTHETASE;

ALZHEIMER DISEASE; ANIMAL TISSUE; ARTICLE; BLOOD VESSEL; BRAIN; CONTROLLED STUDY; IMMUNOHISTOCHEMISTRY; MOUSE; NONHUMAN; PARENCHYMA; PRIORITY JOURNAL; PROTEIN EXPRESSION; TRANSGENIC MOUSE; VASCULAR AMYLOIDOSIS; VASCULAR TISSUE;

AGING; ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; BLOOD VESSELS; BLOTTING, WESTERN; BRAIN; CEREBRAL AMYLOID ANGIOPATHY; G(M1) GANGLIOSIDE; G(M3) GANGLIOSIDE; HUMANS; IMMUNOHISTOCHEMISTRY; MICE; MICE, TRANSGENIC; MUTATION; N-ACETYLGALACTOSAMINYLTRANSFERASES; RECEPTORS, CELL SURFACE;

EID: 68249128437     PISSN: 09594965     EISSN: None     Source Type: Journal    
DOI: 10.1097/WNR.0b013e32832e4b9d     Document Type: Article

References (22)

1. Yanagisawa K, Odaka A, Suzuki N, Ihara Y. GM1 ganglioside-bound amyloid b-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat Med 1995; 1:1062-1066.
2. Yanagisawa K, Ihara Y. GM1 ganglioside-bound amyloid β-protein in Alzheimer's disease brain. Neurobiol Aging 1998; 19:S65-S67. (Pubitemid 28178941)
3. Hayashi H, Kimura N, Yamaguchi H, Hasegawa K, Yokoseki T, Shibata M, et al. A seed for Alzheimer amyloid in the brain. J Neurosci 2004; 24:4894-4902.
4. Yamamoto N, Matsubara E, Maeda S, Minagawa H, Takashima A, Maruyama W, et al. A ganglioside-induced toxic soluble Aβ assembly. Its enhanced formation from Aβ bearing the Arctic mutation. J Biol Chem 2007; 282:2646-2655. (Pubitemid 47076773)
5. Matsuzaki K. Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim Biophys Acta 2007; 1768:1935-1942 (Pubitemid 47135568)
6. Yanagisawa K. Role of gangliosides in Alzheimer's disease. Biochim Biophys Acta 2007; 1768:1943-1951
7. Ariga T, McDonald MP, Yu RK. Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease - a review. J Lipid Res 2008; 49:1157-1175.
8. Shin RW, Ogino K, Shimabuku A, Taki T, Nakashima H, Ishihara T, et al. Amyloid precursor protein cytoplasmic domain with phospho-Thr668 accumulates in Alzheimer's disease and its transgenic models: a role to mediate interaction of Aβ and tau. Acta Neuropathol 2007; 113:627-636. (Pubitemid 46863899)
9. Takamiya K, Yamamoto A, Furukawa K, Yamashiro S, Shin M, Okada M, et al. Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system. Proc Natl Acad Sci U S A 1996; 93:10662-10667. (Pubitemid 26333045)
10. Yamamoto N, Hirabayashi Y, Amari M, Yamaguchi H, Romanov G, Van Nostrand WE, et al. Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides. FEBS Lett 2005; 579:2185-2190. (Pubitemid 40469690)
11. Yamamoto N, Igbabvoa U, Shimada Y, Ohno-Iwashita Y, Kobayashi M, Wood WG, et al. Accelerated Aβ aggregation in the presence of GM1-ganglioside- accumulated synaptosomes of aged apoE4-knock-in mouse brain. FEBS Lett 2004; 569:135-139. (Pubitemid 38844606)
12. Yamamoto N, Fukata Y, Fukata M, Yanagisawa K. GM1-ganglioside-induced Aβ assembly on synaptic membranes of cultured neurons. Biochim Biophys Acta 2007; 1768:1128-1137. (Pubitemid 46550354)
13. Weller RO, Massey A, Newman TA, Hutchings M, Kuo YM, Roher AE. Cerebral amyloid angiopathy: amyloid β accumulates in putative interstitial fluid drainage pathways in Alzheimer's disease. Am J Pathol 1998; 153:725-733. (Pubitemid 28419027)
14. Ida N, Hartmann T, Pantel J, Schröder J, Zerfass R, Förstl H, et al. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J Biol Chem 1996; 271:22908-22914. (Pubitemid 26304742)
15. Levy E, Carman MD, Fernandez-Madrid IJ, Power MD, Lieberburg I, van Duinen SG, et al. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 1990; 248:1124-1126. (Pubitemid 20189869)
16. Rozemuller AJ, Roos RA, Bots GT, Kamphorst W, Eikelenboom P, Van Nostrand WE. Distribution of β/A4 protein and amyloid precursor protein in hereditary cerebral hemorrhage with amyloidosis-Dutch type and Alzheimer's disease. Am J Pathol 1993; 142:1449-1457 (Pubitemid 24058132)
17. Gorbenko GP, Kinnunen PK. The role of lipid-protein interactions in amyloid-type protein fibril formation. Chem Phys Lipids 2006; 141:72-82.
18. Kurganov B, Doh M, Arispe N. Aggregation of liposomes induced by the toxic peptides Alzheimer's Aβ s, human amylin and prion (106-126): facilitation by membrane-bound GM1 ganglioside. Peptides 2004; 25:217-232.
19. Gellermann GP, Appel TR, Tannert A, Radestock A, Hortschansky P, Schroeckh V, et al. Raft lipids as common components of human extracellular amyloid fibrils. Proc Natl Acad Sci U S A 2005; 102:6297-6302. (Pubitemid 40617437)
20. Wang SS, Good TA, Rymer DL. The influence of phospholipid membranes on bovine calcitonin peptide's secondary structure and induced neurotoxic effects. Int J Biochem Cell Biol 2005; 37:1656-1669. (Pubitemid 40719645)
21. Miura T, Yoda M, Takaku N, Hirose T, Takeuchi H. Clustered negative charges on the lipid membrane surface induce β-sheet formation of prion protein fragment 106-126. Biochemistry 2007; 46:11589-11597. (Pubitemid 47585504)
22. Choo-Smith LP, Garzon-Rodriguez W, Glabe CG, Surewicz WK. Acceleration of amyloid fibril formation by specific binding of Aβ -(1-40) peptide to ganglioside-containing membrane vesicles. J Biol Chem 1997; 272:22987-22990.