Effects of docosahexaenoic acid on in vitro amyloid beta peptide 25-35 fibrillation

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1791, Issue 4, 2009, Pages 289-296

  Hashimoto, Michio ^a   Shahdat, Hossain Md ^a,b   Katakura, Masanori ^a   Tanabe, Yoko ^a   Gamoh, Shuji ^a   Miwa, Koji ^a   Shimada, Toshio ^a   Shido, Osamu ^a  

^a SHIMANE UNIVERSITY FACULTY OF MEDICINE   (Japan)

^b JAHANGIRNAGAR UNIVERSITY   (Bangladesh)

Author keywords

A 25 35 fibrillation; Alzheimer's disease; Docosahexaenoic acid

Indexed keywords

AMYLOID BETA PROTEIN[25-35]; DOCOSAHEXAENOIC ACID; THIOFLAVINE;

ARTICLE; CONFOCAL MICROSCOPY; FIBER; GEL ELECTROPHORESIS; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN ANALYSIS; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID; AMYLOID BETA-PROTEIN; DOCOSAHEXAENOIC ACIDS; DOSE-RESPONSE RELATIONSHIP, DRUG; FLUORESCENT DYES; HUMANS; MICROSCOPY, CONFOCAL; NEUROFIBRILLARY TANGLES; PEPTIDE FRAGMENTS; THIAZOLES;

EID: 62249093780     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2009.01.012     Document Type: Article

References (46)

1. Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron 6 (1991) 487-498
2. Selkoe D.J. Physiological production of the β-amyloid protein and the mechanism of Alzheimers disease. Trends Neurosci. 16 (1993) 403-409
3. Jarrett J.T., Berger E.P., and Lansbury P.T. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
4. Kubo T., Nishimura S., Kumagae Y., and Kaneko I. In vivo conversion of racemized β-amyloid ([D-Ser 26]Aβ 1-40) to truncated and toxic fragments ([D-Ser 26]A 25-35/40) and fragment presence in the brains of Alzheimer's patients. J. Neurosci. Res. 70 (2002) 474-483
5. Yankner B.A., Duffy L.K., and Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250 4978 (1990) 279-282
6. Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., and Cotman C.W. Neurodegeneration induced by β-amyloid peptide in vitro: the role of peptide assembly state. J. Neurosci. 16 (1993) 1676-1687
7. Tohda C., Tamura T., and Komatsu K. Repair of amyloid β(25-35)-induced memory impairment and synaptic loss by a Kampo formula, Zokumei-to. Brain Res. 990 (2003) 141-147
8. Yamada M., Chiba T., Sasabe J., Nawa M., Tajima H., Niikura T., Terashita K., Aiso S., Kita Y., Matsuoka M., and Nishimoto I. Implanted cannula-mediated repetitive administration of Aβ25-35 into the mouse cerebral ventricle effectively impairs spatial working memory. Behav. Brain Res. 164 (2005) 139-146
9. Hashimoto M., Hossain S., Shimada T., Sugioka K., Yamasaki H., Fujii Y., Ishibashi Y., Oka J., and Shido O. Docosahexaenoic acid provides protection from impairment of learning ability in Alzheimer's disease model rats. J. Neurochem. 81 (2002) 1084-1091
10. Hashimoto M., Tanabe Y., Fujii Y., Kikuta T., Shibata H., and Shido O. Chronic administration of docosahexaenoic acid ameliorates the impairment of spatial cognition learning ability in amyloid β-infused rats. J. Nutr. 135 (2005) 549-555
11. Crawford M. The role of essential fatty acids in neural development: implications for perinatal nutrition. Am. J. Clin. Nutr. 57 (1993) 703S-710S
12. Lauritzen L., Hansen H.S., Jorgensen M.H., and Michaelsen K.F. The essentiality of long chain n-3 fatty acids in relation to development and function of the brain and retina. Prog. Lipid Res. 40 (2001) 1-94
13. Söderberg M., Edlund C., Kristensson K., and Dallner G. Fatty acid composition of brain phospholipids in aging and in Alzheimer's disease. Lipids 26 (1991) 421-425
14. Kotani S., Sakaguchi E., Warashina S., Matsukawa N., Ishikura Y., Kiso Y., Sakakibara M., Yoshimoto T., Guo J., and Yamashima T. Dietary supplementation of arachidonic and docosahexaenoic acids improves cognitive dysfunction. Neurosci. Res. 56 (2006) 159-164
15. Hashimoto M., Hossain S., Agdul H., and Shido O. Docosahexaenoic acid-induced amelioration on impairment of memory learning in amyloid β-infused rats relates to the decreases of amyloid β and cholesterol levels in detergent-insoluble membrane fractions. Biochim. Biophys. Acta 1738 (2005) 91-98
16. William M., Charles-Félix C., Nicolas F., Pascal E., Edwige A., Annette K., and Giaume C. Proinflammatory cytokines released from microglia inhibit gap junctions in astrocytes: potentiation by β-amyloid. FASEB J. 20 (2006) 494-496
17. Grace E.A., Rabiner C.A., and Busciglio J. Characterization of neuronal dystrophy induced by fibrillar amyloid β: implications for Alzheimer's disease. Neuroscience 114 (2002) 265-273
18. Li X., and Zuo P. Effects of Aβ25-35 on neurogenesis in the adult mouse subventricular zone and dentate gyrus. Neurol. Res. 27 (2005) 218-222
19. Hirota N., Mizuno K., and Goto Y. Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6 (1997) 416-421
20. Ono K., Hasegawa K., Yoshiike Y.T., Yamada M., and Naiki H. Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's β-amyloid fibrils in vitro. J. Neurochem. 81 (2002) 434-440
21. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
22. Naiki H., Higuchi K., Hosokawa M., and Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal. Biochem. 177 (1989) 244-249
23. LeVine III H. Thioflavin T interaction with synthetic Alzheimer's disease β amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
24. Krebs M.R.H., Bromley E.H.C., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localization and implications. J. Struc. Biol. 149 (2005) 30-37
25. Benowitz L.I., Rodriguez W., Paskevich P., Mufson E.J., Schenk D., and Neve R.L. The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. Exp. Neurol. 106 (1989) 237-250
26. Cole G.M., Huynh T.V., and Saitoh T. Evidence for lysosomal processing of amyloid β-protein precursor in cultured cells. Neurochem. Res. 14 (1989) 933-939
27. Kirkitadze M.D., Condron M.M., and Teplow D.B. Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis. J. Mol. Biol. 312 (2001) 1103-1119
28. Khandogin J., and Brooks III C.L. Linking folding with aggregation in Alzheimer's β-amyloid peptides. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 16880-16885
29. Fraser P.E., Nguyen J.T., Surewicz W.K., and Kirschner D.A. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 60 (1991) 1190-1201
30. Petkova A.T., Ishii Y., Balbach J.J., Antzutkin O.N., Leapman R.D., Delaglio F., and Tycko R. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. U. S. A 99 (2002) 16742-16747
31. Lu{double acute}hrs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Döbeli H., Schubert D., and Riek R. 3D structure of Alzheimer's amyloid-β(1-42) fibrils. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17342-17347
32. Giacomelli C.E., and Norde W. Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces. Macromol. Biosci. 5 (2005) 401-407
33. Kellermayer M.S., Grama L., Karsai A., Nagy A., Kahn A., Datki Z.L., and Penke B. Reversible mechanical unzipping of amyloid β fibrils. J. Biol. Chem. 280 (2005) 8464-8470
34. Karsai A., Nagy A., Kengyel A., Mártonfalvi Z., Grama L., Penke B., and Kellermayer M.S. Effect of lysine-28 side-chain acetylation on the nanomechanical behavior of Alzheimer amyloid β25-35 fibrils. J. Chem. Inf. Model. 45 (2005) 1641-1646
35. Cistola D.P., Hamilton J.A., Jackson D., and Small D.M. Ionization and phase behavior of fatty acid in water: application of the Gibbs phase rule. Biochemistry 27 (1988) 1881
36. Namani T., Ishikawa T., Morigaki K., and Walde P. Vesicles from docosahexaenoic acid. Colloids Surf. B Biointerfaces 54 (2007) 118-123
37. Dorota T., Jason B.J., Sofia S., Bengt K., and Julie G. DHA-induced changes of supported lipid membrane morphology. Langmuir 23 (2007) 5878-5881
38. Johansson A.S., Garlind A., Berglind-Dehlin F., Karlsson G., Edwards K., Gellerfors P., Ekholm-Pettersson F., Palmblad J., and Lannfelt L. Docosahexaenoic acid stabilizes soluble amyloid-β protofibrils and sustains amyloid-β-induced neurotoxicity in vitro. FEBS J. 274 (2007) 990-1000
39. Bond J.P., Deverin S.P., Inouye H., El-Agnaf O.M.A., Teeter M.M., and Kirschner D.A. Assemblies of Alzheimer's peptides A β 25-35 and A beta 31-35: reverse-turn conformation and side-chain interactions revealed by X-ray diffraction. J. Struct. Biol. 141 (2003) 156-710
40. Hughes E., Burke R.M., and Doig A.J. Inhibition of toxicity in the beta-amyloid peptide fragment β-(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. J. Biol. Chem. 275 (2000) 25109-25115
41. D'Ursi A.M., Armenante M.R., Guerrini R., Salvadori S., Sorrentino G., and Picone D. Solution structure of amyloid β-peptide (25-35) in different media. J. Med. Chem. 47 (2004) 4231-4238
42. Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
43. Cleary J.P., Walsh D.M., Hofmeister J.J., Shankar G.M., Kuskowski M.A., Selkoe D.J., and Ashe K.H. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat. Neurosci. 8 (2005) 79-84
44. Florent S., Malaplate-Armand C., Youssef I., Kriem B., Koziel V., Escanyé M.C., Fifre A., Sponne I., Leininger-Muller B., Olivier J.L., Pillot T., and Oster T. Docosahexaenoic acid prevents neuronal apoptosis induced by soluble amyloid-β oligomers. J. Neurochem. 96 (2006) 385-395
45. Dante S., Hauss T., and Dencher N.A. β-amyloid 25-35 is intercalated in anionic and zwitterrionic lipid membranes to different extents. Biophys. J. 83 (2002) 2610-2616
46. Mason R.P., Jacob R.F., Walter M.F., Mason P.E., Avdulov N.A., Chochina S.V., Igbavboa U., and Wood W.G. Distribution and fluidizing U action of soluble and aggregated amyloid β-peptide in rat synaptic plasma membranes. J. Biol. Chem. 274 (1999) 18801-18807