Role of gangliosides in Alzheimer's disease

Biochimica et Biophysica Acta - Biomembranes

Volumn 1768, Issue 8, 2007, Pages 1943-1951

  Yanagisawa, Katsuhiko ^a  

^a NATIONAL CENTER FOR GERIATRICS AND GERONTOLOGY   (Japan)

Author keywords

Alzheimer's disease; Amyloid protein; Cholesterol; Ganglioside; Seed

Indexed keywords

AMYLOID BETA PROTEIN; APOLIPOPROTEIN E4; CHOLESTEROL; GANGLIOSIDE; GANGLIOSIDE GM1;

ALZHEIMER DISEASE; CONFORMATIONAL TRANSITION; FACILITATION; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN METABOLISM; REVIEW;

AGE FACTORS; ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; ANIMALS; APOLIPOPROTEIN E4; BRAIN; CELL MEMBRANE; G(M1) GANGLIOSIDE; HUMANS; NEURONS; PROTEIN BINDING; RISK FACTORS;

EID: 34547152918     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.01.018     Document Type: Review

References (28)

1. Shoji M., Golde T.E., Ghiso J., Cheung T.T., Estus S., Shaffer L.M., Cai X.-D., McKay D.M., Tintner R., Frangione B., and Younkin S.G. Production of the Alzheimer amyloid β-protein by normal proteolytic processing. Science 258 (1992) 126-129
2. Haass C., Schlossmacher M.G., Hung A.Y., Vigo-Pelfrey C., Mellon A., Ostaszewski B.L., Lieberburg I., Koo E.H., Schenk D., Teplow D.B., and Selkoe D.J. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359 (1992) 322-325
3. Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., Sinha S., Sclossmacher M., Whaley J., Swindlehurst C., McCormack R., Wolfert R., Selkoe D.J., Lieberburg I., and Schenk D. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359 (1992) 325-327
4. Selkoe D.J. Alzheimer's disease: genotypes, phenotypes, and treatments. Science 275 (1997) 630-631
5. Levy E., Carman M.D., Fernandez-Madrid I.J., Power M.D., Lieberburg I., van Duinen S.G., Bots G.T., Luyendijk W., and Frangione B. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248 (1990) 1124-1126
6. Hendriks L., van Duijn C.M., Cras P., Cruts M., Van Hul W., van Harskamp F., Warren A., McInnis M.G., Antonarakis S.E., Martin J.J., et al. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β-amyloid precursor protein gene. Nat. Genet. 1 (1992) 218-221
7. Nilsberth C., Westlind-Danielsson A., Eckman C.B., Condron M.M., Axelman K., Forsell C., Stenh C., Luthman J., Teplow D.B., Younkin S.G., Naslund J., and Lannfelt L. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nat. Neurosci. 4 (2001) 887-893
8. Yanagisawa K., McLaurin J., Michikawa M., Chakrabartty A., and Ihara Y. Amyloid β-protein (Aβ) associated with lipid molecules: immunoreactivity distinct from that of soluble Aβ. FEBS Lett. 420 (1997) 43-46
9. McLaurin J., and Chakrabartty A. Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity. J. Biol. Chem. 271 (1996) 26482-26489
10. Choo-Smith L.P., and Surewicz W.K. The interaction between Alzheimer amyloid β (1-40) peptide and ganglioside GM1-containing membranes. FEBS Lett. 402 (1997) 95-98
11. Choo-Smith L.P., Garzon-Rodriguez W., Glabe C.G., and Surewicz W.K. Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles. J. Biol. Chem. 272 (1997) 22987-22990
12. McLaurin J., Franklin T., Fraser P.E., and Chakrabartty A. Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides. J. Biol. Chem. 273 (1998) 4506-4515
13. Matsuzaki K., and Horikiri C. Interactions of amyloid β-peptide (1-40) with ganglioside-containing membranes. Biochemistry 38 (1999) 4137-4142
14. Ariga T., Kobayashi K., Hasegawa A., Kiso M., Ishida H., and Miyatake T. Characterization of high-affinity binding between gangliosides and amyloid β-protein. Arch. Biochem. Biophys. 388 (2001) 225-230
15. Kakio A., Nishimoto S.I., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276 (2001) 24985-24990
16. Kakio A., Nishimoto S., Yanagisawa K., Kozutsumi Y., and Matsuzaki K. Interactions of amyloid β-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 41 (2002) 7385-7390
17. Naiki H., and Gejyo F. Kinetic analysis of amyloid fibril formation. Methods Enzymol. 309 (1999) 305-318
18. Hayashi H., Kimura N., Yamaguchi H., Hasegawa K., Yokoseki T., Shibata M., Yamamoto N., Michikawa M., Yoshikawa Y., Terao K., Matsuzaki K., Lemere C.A., Selkoe D.J., Naiki H., and Yanagisawa K. A seed for Alzheimer amyloid in the brain. J. Neurosci. 24 (2004) 4894-4902
19. Yanagisawa K., Odaka A., Suzuki N., and Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat. Med. 1 (1995) 1062-1066
20. Igbavboa U., Avdulov N.A., Schroeder F., and Wood W.G. Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice. J. Neurochem. 66 (1996) 1717-1725
21. Yamamoto N., Igbabvoa U., Shimada Y., Ohno-Iwashita Y., Kobayashi M., Wood W.G., Fujita S.C., and Yanagisawa K. Accelerated Aβ aggregation in the presence of GM1-ganglioside-accumulated synaptosomes of aged apoE4-knock-in mouse brain. FEBS Lett. 569 (2004) 135-139
22. Molander-Melin M., Blennow K., Bogdanovic N., Dellheden B., Mansson J.E., and Fredman P. Structural membrane alterations in Alzheimer brains found to be associated with regional disease development: increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains. J. Neurochem. 92 (2005) 171-182
23. Gylys K.H., Fein J.A., Yang F., Miller C.A., and Cole G.M. Increased cholesterol in Aβ-positive nerve terminal form Alzheimer's disease cortex. Neurobiol. Aging 28 (2007) 8-17
24. Rozemuller A.J., Roos R.A., Bots G.T., Kamphorst W., Eikelenboom P., and Van Nostrand W.E. Distribution of β/A4 protein and amyloid precursor protein in hereditary cerebral hemorrhage with amyloidosis-Dutch type and Alzheimer's disease. Am. J. Pathol. 142 (1993) 1449-1457
25. Melchor J.P., McVoy L., and Van Nostr W.E. Charge alterations of E22 enhance the pathogenic properties of the amyloid β-protein. J. Neurochem. 74 (2000) 2209-2212
26. Grabowski T.J., Cho H.S., Vonsattel J.P., Rebeck G.W., and Greenberg S.M. Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Ann. Neurol. 49 (2001) 697-705
27. Kumar-Singh S., Cras P., Wang R., Kros J.M., van Swieten J., Lubke U., Ceuterick C., Serneels S., Vennekens K., Timmermans J.P., Van Marck E., Martin J.J., van Duijn C.M., and Van Broeckhoven C. Dense-core senile plaques in the Flemish variant of Alzheimer's disease are vasocentric. Am. J. Pathol. 161 (2002) 507-520
28. Yamamoto N., Hirabayashi Y., Amari M., Yamaguchi H., Romanov G., Van Nostrand W.E., and Yanagisawa K. Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides. FEBS Lett. 579 (2005) 2185-2190