메뉴 건너뛰기




Volumn 49, Issue 7, 2005, Pages 1088-1099

Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro

Author keywords

Amyloid fibrils; Alzheimer's disease; Electron microscopy; Non steroidal anti inflammatory drugs; Thioflavin T

Indexed keywords

ACETYLSALICYLIC ACID; AMYLOID BETA PROTEIN; DICLOFENAC; FLURBIPROFEN; IBUPROFEN; KETOPROFEN; MECLOFENAMATE SODIUM; NAPROXEN; NONSTEROID ANTIINFLAMMATORY AGENT; SULINDAC SULFIDE; THIOFLAVINE;

EID: 27144513779     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2005.07.004     Document Type: Article
Times cited : (134)

References (40)
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem 72 1976 248 254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0043162103 scopus 로고    scopus 로고
    • Novel anti-inflammatory therapy for Parkinson's disease
    • H.M. Gao, B. Liu, W. Zhang, and J.S. Hong Novel anti-inflammatory therapy for Parkinson's disease Trends Pharmacol. Sci. 24 2003 395 401
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 395-401
    • Gao, H.M.1    Liu, B.2    Zhang, W.3    Hong, J.S.4
  • 8
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Y. Gong, L. Chang, K.L. Viola, P.N. Lacor, M.P. Lambert, C.E. Finch, G.A. Krafft, and W.L. Klein Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc. Natl. Acad. Sci. USA 100 2003 10417 10422
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 9
    • 0033598697 scopus 로고    scopus 로고
    • Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro
    • K. Hasegawa, I. Yamaguchi, S. Omata, F. Gejyo, and H. Naiki Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro Biochemistry 38 1999 15514 15521
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5
  • 10
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance
    • K. Hasegawa, K. Ono, M. Yamada, and H. Naiki Kinetic modeling and determination of reaction constants of Alzheimer's β-amyloid fibril extension and dissociation using surface plasmon resonance Biochemistry 41 2002 13489 13498
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3    Naiki, H.4
  • 11
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • J.T. Jarrett, and P.T. Lansbury Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 12
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small-molecule anionic sulfonates or sulfates: Implications for Alzheimer's disease
    • R. Kisilevsky, L.J. Lemieux, P.E. Fraser, X. Kong, P.G. Hultin, and W.A. Szarek Arresting amyloidosis in vivo using small-molecule anionic sulfonates or sulfates: implications for Alzheimer's disease Nat. Med 1 1995 143 148
    • (1995) Nat. Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3    Kong, X.4    Hultin, P.G.5    Szarek, W.A.6
  • 13
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • J. Li, M. Zhu, A.B. Manning-Bog, D.A. Di Monte, and A.L. Fink Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease FASEBJ 9 2004 962 964
    • (2004) FASEBJ , vol.9 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 16
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases
    • P.L. McGeer, and E.G. McGeer The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases Brain. Res. Brain. Res. Rev. 21 1995 195 218
    • (1995) Brain. Res. Brain. Res. Rev. , vol.21 , pp. 195-218
    • McGeer, P.L.1    McGeer, E.G.2
  • 17
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • P.L. McGeer, M. Schulzer, and E.G. McGeer Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies Neurology 47 1996 425 432
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 18
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • H. Naiki, and F. Gejyo Kinetic analysis of amyloid fibril formation Methods Enzymol 309 1999 305 318
    • (1999) Methods Enzymol , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 19
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • H. Naiki, and K. Nakakuki First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro Lab. Invest 74 1996 374 383
    • (1996) Lab. Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 20
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein e and antioxidants have different mechanisms of inhibiting Alzheimer's β-amyloid fibril formation in vitro
    • H. Naiki, K. Hasegawa, I. Yamaguchi, H. Nakamura, F. Gejyo, and K. Nakakuki Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's β-amyloid fibril formation in vitro Biochemistry 37 1998 17882 17889
    • (1998) Biochemistry , vol.37 , pp. 17882-17889
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Gejyo, F.5    Nakakuki, K.6
  • 21
    • 0036838889 scopus 로고    scopus 로고
    • Nicotine breaks down preformed Alzheimer's β-amyloid fibrils in vitro
    • K. Ono, K. Hasegawa, M. Yamada, and H. Naiki Nicotine breaks down preformed Alzheimer's β-amyloid fibrils in vitro Biol. Psychiatry 52 2002 880 886
    • (2002) Biol. Psychiatry , vol.52 , pp. 880-886
    • Ono, K.1    Hasegawa, K.2    Yamada, M.3    Naiki, H.4
  • 22
    • 0036313066 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's β-amyloid fibrils in vitro
    • K. Ono, K. Hasegawa, Y. Yoshiike, A. Takashima, M. Yamada, and H. Naiki Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's β-amyloid fibrils in vitro J. Neurochem 81 2002 434 440
    • (2002) J. Neurochem , vol.81 , pp. 434-440
    • Ono, K.1    Hasegawa, K.2    Yoshiike, Y.3    Takashima, A.4    Yamada, M.5    Naiki, H.6
  • 23
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • K. Ono, Y. Yoshiike, A. Takashima, K. Hasegawa, H. Naiki, and M. Yamada Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease J. Neurochem 87 2003 172 181
    • (2003) J. Neurochem , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 24
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro
    • K. Ono, K. Hasegawa, H. Naiki, and M. Yamada Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro Biochim. Biophys. Acta 1690 2004 193 202
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 25
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • K. Ono, K. Hasegawa, H. Naiki, and M. Yamada Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro J. Neurosci. Res. 75 2004 742 750
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 27
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • C.J. Pike, A.J. Walencewicz-Wasserman, J. Kosmoski, D.H. Cribbs, C.G. Glabe, and C.W. Cotman Structure-activity analyses of β-amyloid peptides: contributions of the β25-35 region to aggregation and neurotoxicity J. Neurochem 64 1995 253 265
    • (1995) J. Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 29
    • 0042878457 scopus 로고    scopus 로고
    • The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of κb kinase, and NF κb, do not reduce amyloid β42 production
    • S.A. Sagi, S. Weggen, J. Eriksen, T.E. Golde, and E.H. Koo The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of κB kinase, and NF κB, do not reduce amyloid β42 production J. Biol. Chem. 278 2003 31825 31830
    • (2003) J. Biol. Chem. , vol.278 , pp. 31825-31830
    • Sagi, S.A.1    Weggen, S.2    Eriksen, J.3    Golde, T.E.4    Koo, E.H.5
  • 30
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • D.J. Selkoe Alzheimer's disease: genes, proteins, and therapy Physiol. Rev. 81 2001 741 766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 31
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation
    • C. Soto, M.S. Kindy, M. Baumann, and B. Frangione Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation Biochem. Biophys. Res. Commun 226 1996 672 680
    • (1996) Biochem. Biophys. Res. Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3    Frangione, B.4
  • 33
    • 0035968743 scopus 로고    scopus 로고
    • Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation
    • T. Thomas, T.G. Nadackal, and K. Thomas Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation NeuroReport 12 2001 3263 3267
    • (2001) NeuroReport , vol.12 , pp. 3263-3267
    • Thomas, T.1    Nadackal, T.G.2    Thomas, K.3
  • 34
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger
    • T. Tomiyama, A. Shoji, K. Kataoka, Y. Suwa, S. Asano, H. Kaneko, and N. Endo Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger J. Biol. Chem. 271 1996 6839 6844
    • (1996) J. Biol. Chem. , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.