메뉴 건너뛰기




Volumn 1822, Issue 8, 2012, Pages 1207-1215

Inhibitory effect of curcumin on the Al(III)-induced Aβ42 aggregation and neurotoxicity in vitro

Author keywords

Aggregate morphology; Alzheimer's disease; Fibrillation inhibitor; Protein conformation

Indexed keywords

ALUMINUM; AMYLOID; AMYLOID BETA PROTEIN[1-42]; CURCUMIN; THIOFLAVINE;

EID: 84861155036     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.04.015     Document Type: Article
Times cited : (62)

References (56)
  • 1
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid beta peptide
    • Barnham K.J., Smith D.G., Cappai R. The redox chemistry of the Alzheimer's disease amyloid beta peptide. Bba-Biomembranes 2007, 1768:1976-1990.
    • (2007) Bba-Biomembranes , vol.1768 , pp. 1976-1990
    • Barnham, K.J.1    Smith, D.G.2    Cappai, R.3
  • 2
    • 0025992417 scopus 로고
    • Invitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike C.J., Walencewicz A.J., Glabe C.G., Cotman C.W. Invitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 1991, 563:311-314.
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 3
    • 0031902295 scopus 로고    scopus 로고
    • Alzheimer's disease-etiologies, pathophysiology, cognitive reserve, and treatment opportunities
    • Cummings J.L., Vinters H.V., Cole G.M., Khachaturian Z.S. Alzheimer's disease-etiologies, pathophysiology, cognitive reserve, and treatment opportunities. Neurology 1998, 51:S2-S17.
    • (1998) Neurology , vol.51
    • Cummings, J.L.1    Vinters, H.V.2    Cole, G.M.3    Khachaturian, Z.S.4
  • 4
    • 79954613385 scopus 로고    scopus 로고
    • Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization
    • Chen Y.R., Ni C.L., Shi H.P., Yu H.M., Chang Y.C. Folding stability of amyloid-beta 40 monomer is an important determinant of the nucleation kinetics in fibrillization. FASEB J. 2011, 25:1390-1401.
    • (2011) FASEB J. , vol.25 , pp. 1390-1401
    • Chen, Y.R.1    Ni, C.L.2    Shi, H.P.3    Yu, H.M.4    Chang, Y.C.5
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 2007, 8:101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 79955663093 scopus 로고    scopus 로고
    • High ability of apolipoprotein E4 to stabilize amyloid-beta peptide oligomers, the pathological entities responsible for Alzheimer's disease
    • Raussens V., Cerf E., Gustot A., Goormaghtigh E., Ruysschaert J.M. High ability of apolipoprotein E4 to stabilize amyloid-beta peptide oligomers, the pathological entities responsible for Alzheimer's disease. FASEB J. 2011, 25:1585-1595.
    • (2011) FASEB J. , vol.25 , pp. 1585-1595
    • Raussens, V.1    Cerf, E.2    Gustot, A.3    Goormaghtigh, E.4    Ruysschaert, J.M.5
  • 8
    • 0142226864 scopus 로고    scopus 로고
    • The role of metals in neurodegenerative processes: aluminum, manganese, and zinc
    • Zatta P., Lucchini R., van Rensburg S.J., Taylor A. The role of metals in neurodegenerative processes: aluminum, manganese, and zinc. Brain Res. Bull. 2003, 62:15-28.
    • (2003) Brain Res. Bull. , vol.62 , pp. 15-28
    • Zatta, P.1    Lucchini, R.2    van Rensburg, S.J.3    Taylor, A.4
  • 9
    • 3042666730 scopus 로고    scopus 로고
    • Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of A beta(42) in a manner which may have consequences for metal chelation therapy in Alzheimer's disease
    • Exley C., House E., Collingwood J., Khan A., Korchazkina O., Berthon G. Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of A beta(42) in a manner which may have consequences for metal chelation therapy in Alzheimer's disease. J. Alzheimers Dis. 2004, 6:291-301.
    • (2004) J. Alzheimers Dis. , vol.6 , pp. 291-301
    • Exley, C.1    House, E.2    Collingwood, J.3    Khan, A.4    Korchazkina, O.5    Berthon, G.6
  • 10
    • 23844434035 scopus 로고    scopus 로고
    • Aluminum-triggered structural modifications and aggregation of beta-amyloids
    • Zatta P., Ricchelli F., Drago D., Filippi B., Tognon G. Aluminum-triggered structural modifications and aggregation of beta-amyloids. Cell. Mol. Life Sci. 2005, 62:1724-1733.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1724-1733
    • Zatta, P.1    Ricchelli, F.2    Drago, D.3    Filippi, B.4    Tognon, G.5
  • 11
    • 33751107948 scopus 로고    scopus 로고
    • Aluminium and iron, but neither copper nor zinc, are key to the precipitation of beta-sheets of A beta(42) in senile plaque cores in Alzheimer's disease
    • Exley C. Aluminium and iron, but neither copper nor zinc, are key to the precipitation of beta-sheets of A beta(42) in senile plaque cores in Alzheimer's disease. J. Alzheimers Dis. 2006, 10:173-177.
    • (2006) J. Alzheimers Dis. , vol.10 , pp. 173-177
    • Exley, C.1
  • 12
    • 0036089833 scopus 로고    scopus 로고
    • Aluminum: impacts and disease
    • Nayak P. Aluminum: impacts and disease. Environ. Res. 2002, 89:101-115.
    • (2002) Environ. Res. , vol.89 , pp. 101-115
    • Nayak, P.1
  • 14
    • 37849189833 scopus 로고    scopus 로고
    • Aluminum inhibits proteolytic degradation of amyloid beta peptide by cathepsin D: a potential link between aluminum accumulation and neuritic plaque deposition
    • Sakamoto T., Saito H., Ishii K., Takahashi H., Tanabe S., Ogasawara Y. Aluminum inhibits proteolytic degradation of amyloid beta peptide by cathepsin D: a potential link between aluminum accumulation and neuritic plaque deposition. FEBS Lett. 2006, 580:6543-6549.
    • (2006) FEBS Lett. , vol.580 , pp. 6543-6549
    • Sakamoto, T.1    Saito, H.2    Ishii, K.3    Takahashi, H.4    Tanabe, S.5    Ogasawara, Y.6
  • 15
    • 0029793482 scopus 로고    scopus 로고
    • Can the controversy of the role of aluminum in Alzheimer's disease be resolved? What are the suggested approaches to this controversy and methodological issues to be considered?
    • Savory J., Exley C., Forbes W.F., Huang Y., Joshi J.G., Kruck T., McLachlan D.R.C., Wakayama I. Can the controversy of the role of aluminum in Alzheimer's disease be resolved? What are the suggested approaches to this controversy and methodological issues to be considered?. J. Toxicol. Environ. Health 1996, 48:615-635.
    • (1996) J. Toxicol. Environ. Health , vol.48 , pp. 615-635
    • Savory, J.1    Exley, C.2    Forbes, W.F.3    Huang, Y.4    Joshi, J.G.5    Kruck, T.6    McLachlan, D.R.C.7    Wakayama, I.8
  • 16
    • 0027509140 scopus 로고
    • Regulation of serine protease activity by aluminum-implications for Alzheimer-disease
    • Clauberg M., Joshi J.G. Regulation of serine protease activity by aluminum-implications for Alzheimer-disease. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:1009-1012.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1009-1012
    • Clauberg, M.1    Joshi, J.G.2
  • 17
    • 0036634409 scopus 로고    scopus 로고
    • Aluminum modulates brain amyloidosis through oxidative stress in APP transgenic mice
    • Pratico D., Uryu K., Sung S., Tang S., Trojanowski J.Q., Lee V.M.Y. Aluminum modulates brain amyloidosis through oxidative stress in APP transgenic mice. FASEB J. 2002, 16:1138-1140.
    • (2002) FASEB J. , vol.16 , pp. 1138-1140
    • Pratico, D.1    Uryu, K.2    Sung, S.3    Tang, S.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 20
    • 22544478124 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein
    • Li H.T., Lin D.H., Luo X.Y., Zhang F., Ji L.N., Du H.N., Song G.Q., Hu J., Zhou J.W., Hu H.Y. Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein. FEBS J. 2005, 272:3661-3672.
    • (2005) FEBS J. , vol.272 , pp. 3661-3672
    • Li, H.T.1    Lin, D.H.2    Luo, X.Y.3    Zhang, F.4    Ji, L.N.5    Du, H.N.6    Song, G.Q.7    Hu, J.8    Zhou, J.W.9    Hu, H.Y.10
  • 23
    • 42249112650 scopus 로고    scopus 로고
    • The effect of curcumin (turmeric) on Alzheimer's disease: an overview
    • Mishra S., Palanivelu K. The effect of curcumin (turmeric) on Alzheimer's disease: an overview. Ann. Indian Acad. Neurol. 2008, 11:13-19.
    • (2008) Ann. Indian Acad. Neurol. , vol.11 , pp. 13-19
    • Mishra, S.1    Palanivelu, K.2
  • 24
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim G.P., Chu T., Yang F.S., Beech W., Frautschy S.A., Cole G.M. The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J. Neurosci. 2001, 21:8370-8377.
    • (2001) J. Neurosci. , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.S.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 25
    • 34547451145 scopus 로고    scopus 로고
    • Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model
    • Garcia-Alloza M., Borrelli L.A., Rozkalne A., Hyman B.T., Bacskai B.J. Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model. J. Neurochem. 2007, 102:1095-1104.
    • (2007) J. Neurochem. , vol.102 , pp. 1095-1104
    • Garcia-Alloza, M.1    Borrelli, L.A.2    Rozkalne, A.3    Hyman, B.T.4    Bacskai, B.J.5
  • 27
    • 78649329126 scopus 로고    scopus 로고
    • Interaction of curcumin with Zn(II) and Cu(II) ions based on experiment and theoretical calculation
    • Zhao X.Z., Jiang T., Wang L., Yang H., Zhang S., Zhou P. Interaction of curcumin with Zn(II) and Cu(II) ions based on experiment and theoretical calculation. J. Mol. Struct. 2010, 984:316-325.
    • (2010) J. Mol. Struct. , vol.984 , pp. 316-325
    • Zhao, X.Z.1    Jiang, T.2    Wang, L.3    Yang, H.4    Zhang, S.5    Zhou, P.6
  • 28
    • 79955428361 scopus 로고    scopus 로고
    • Gastroprotective and antidepressant effects of a new zinc(II)-curcumin complex in rodent models of gastric ulcer and depression induced by stresses
    • Xu D.H., Mei X.T., Xu S.K., Zheng Y.P., Xu S.B. Gastroprotective and antidepressant effects of a new zinc(II)-curcumin complex in rodent models of gastric ulcer and depression induced by stresses. Pharmacol. Biochem. Behav. 2011, 99:66-74.
    • (2011) Pharmacol. Biochem. Behav. , vol.99 , pp. 66-74
    • Xu, D.H.1    Mei, X.T.2    Xu, S.K.3    Zheng, Y.P.4    Xu, S.B.5
  • 29
    • 34249337528 scopus 로고    scopus 로고
    • Iron dysregulation in Alzheimer's disease: multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents
    • Youdim M.B.H., Mandel S., Amit T., Bar-Am O. Iron dysregulation in Alzheimer's disease: multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents. Prog. Neurobiol. 2007, 82:348-360.
    • (2007) Prog. Neurobiol. , vol.82 , pp. 348-360
    • Youdim, M.B.H.1    Mandel, S.2    Amit, T.3    Bar-Am, O.4
  • 30
    • 80053571379 scopus 로고    scopus 로고
    • Interaction of curcumin with Al(III) and its complex structures based on experiments and theoretical calculations
    • Jiang T., Wang L., Zhang S., Sun P.C., Ding C.F., Chu Y.Q., Ping Z. Interaction of curcumin with Al(III) and its complex structures based on experiments and theoretical calculations. J. Mol. Struct. 2011, 1004:163-173.
    • (2011) J. Mol. Struct. , vol.1004 , pp. 163-173
    • Jiang, T.1    Wang, L.2    Zhang, S.3    Sun, P.C.4    Ding, C.F.5    Chu, Y.Q.6    Ping, Z.7
  • 31
    • 0347627467 scopus 로고    scopus 로고
    • Manganese complexes of curcumin and its derivatives: evaluation for the radical scavenging ability and neuroprotective activity
    • Vajragupta O., Boonchoong P., Watanabe H., Tohda M., Kummasud N., Sumanont Y. Manganese complexes of curcumin and its derivatives: evaluation for the radical scavenging ability and neuroprotective activity. Free Radic. Biol. Med. 2003, 35:1632-1644.
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 1632-1644
    • Vajragupta, O.1    Boonchoong, P.2    Watanabe, H.3    Tohda, M.4    Kummasud, N.5    Sumanont, Y.6
  • 34
    • 32444435388 scopus 로고    scopus 로고
    • Validated LC/MS/MS assay for curcumin and tetrahydrocurcumin in rat plasma and application to pharmacokinetic study of phospholipid complex of curcumin
    • Lou H.X., Liu A.C., Zhao L.X., Fan P.H. Validated LC/MS/MS assay for curcumin and tetrahydrocurcumin in rat plasma and application to pharmacokinetic study of phospholipid complex of curcumin. J. Pharmaceut. Biomed. 2006, 40:720-727.
    • (2006) J. Pharmaceut. Biomed. , vol.40 , pp. 720-727
    • Lou, H.X.1    Liu, A.C.2    Zhao, L.X.3    Fan, P.H.4
  • 35
    • 77953958625 scopus 로고    scopus 로고
    • The in vitro stability and in vivo pharmacokinetics of curcumin prepared as an aqueous nanoparticulate formulation
    • Sahoo S.K., Mohanty C. The in vitro stability and in vivo pharmacokinetics of curcumin prepared as an aqueous nanoparticulate formulation. Biomaterials 2010, 31:6597-6611.
    • (2010) Biomaterials , vol.31 , pp. 6597-6611
    • Sahoo, S.K.1    Mohanty, C.2
  • 37
    • 55249123932 scopus 로고    scopus 로고
    • The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease
    • Streltsov V.A., Titmuss S.J., Epa V.C., Barnham K.J., Masters C.L., Varghese J.N. The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease. Biophys. J. 2008, 95:3447-3456.
    • (2008) Biophys. J. , vol.95 , pp. 3447-3456
    • Streltsov, V.A.1    Titmuss, S.J.2    Epa, V.C.3    Barnham, K.J.4    Masters, C.L.5    Varghese, J.N.6
  • 38
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42
    • Sierks M.R., Liu R., Barkhordarian H., Emadi S., Park C.B. Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42. Neurobiol. Dis. 2005, 20:74-81.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 74-81
    • Sierks, M.R.1    Liu, R.2    Barkhordarian, H.3    Emadi, S.4    Park, C.B.5
  • 39
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to amyloid fibrils
    • Biancalana M., Koide S. Molecular mechanism of thioflavin-T binding to amyloid fibrils. Bba-Proteins Proteomics 2010, 1804:1405-1412.
    • (2010) Bba-Proteins Proteomics , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 40
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: localisation and implications
    • Krebs M.R.H., Bromley E.H.C., Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 2005, 149:30-37.
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 41
    • 52049121032 scopus 로고    scopus 로고
    • Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties
    • Ulrih N.P., Barry C.H., Fink A.L. Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties. Bba-Mol. Basis Dis. 2008, 1782:581-585.
    • (2008) Bba-Mol. Basis Dis. , vol.1782 , pp. 581-585
    • Ulrih, N.P.1    Barry, C.H.2    Fink, A.L.3
  • 42
    • 0030559160 scopus 로고    scopus 로고
    • Aluminum and Alzheimer's disease: model studies
    • Fasman G.D. Aluminum and Alzheimer's disease: model studies. Coord. Chem. Rev. 1996, 149:125-165.
    • (1996) Coord. Chem. Rev. , vol.149 , pp. 125-165
    • Fasman, G.D.1
  • 43
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura T., Suzuki K., Kohata N., Takeuchi H. Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes. Biochemistry-Us 2000, 39:7024-7031.
    • (2000) Biochemistry-Us , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 44
    • 37049102845 scopus 로고
    • Al-27 nuclear magnetic-resonance investigations of highly alkaline aluminate solutions
    • Akitt J.W., Gessner W. Al-27 nuclear magnetic-resonance investigations of highly alkaline aluminate solutions. J. Chem. Soc. Dalton 1984, 147-148.
    • (1984) J. Chem. Soc. Dalton , pp. 147-148
    • Akitt, J.W.1    Gessner, W.2
  • 45
    • 0031233509 scopus 로고    scopus 로고
    • Molecular thermodynamics of hydrophobic hydration
    • Besseling N.A.M., Lyklema J. Molecular thermodynamics of hydrophobic hydration. J. Phys. Chem. B 1997, 101:7604-7611.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 7604-7611
    • Besseling, N.A.M.1    Lyklema, J.2
  • 46
    • 0024352110 scopus 로고
    • Quantitative-evaluation of Congo Red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W.E., Pettegrew J.W., Abraham D.J. Quantitative-evaluation of Congo Red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 1989, 37:1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 48
    • 0015176952 scopus 로고
    • Selective differentiation between amyloid and connective tissue structures based on collagen specific topo-optical staining reaction with Congo Red
    • Romhanyi G. Selective differentiation between amyloid and connective tissue structures based on collagen specific topo-optical staining reaction with Congo Red. Virchows Arch. A 1971, 354:209-222.
    • (1971) Virchows Arch. A , vol.354 , pp. 209-222
    • Romhanyi, G.1
  • 49
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: formation and toxicity of A beta oligomers
    • Sakono M., Zako T. Amyloid oligomers: formation and toxicity of A beta oligomers. FEBS J. 2010, 277:1348-1358.
    • (2010) FEBS J. , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 51
    • 0035983921 scopus 로고    scopus 로고
    • The challenge of inhibiting A beta polymerization
    • LeVine H. The challenge of inhibiting A beta polymerization. Curr. Med. Chem. 2002, 9:1121-1133.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1121-1133
    • LeVine, H.1
  • 54
    • 0035228371 scopus 로고    scopus 로고
    • Reconsidering the importance of long-term low-level aluminum exposure in renal failure patients
    • Cannata-Andia J.B. Reconsidering the importance of long-term low-level aluminum exposure in renal failure patients. Semin. Dial. 2001, 14:5-7.
    • (2001) Semin. Dial. , vol.14 , pp. 5-7
    • Cannata-Andia, J.B.1
  • 55
    • 0033660022 scopus 로고    scopus 로고
    • The toxicology of aluminum in the brain: a review
    • Yokel R.A. The toxicology of aluminum in the brain: a review. Neurotoxicology 2000, 21:813-828.
    • (2000) Neurotoxicology , vol.21 , pp. 813-828
    • Yokel, R.A.1
  • 56
    • 0344874628 scopus 로고    scopus 로고
    • Aluminium in over-the-counter drugs-risks outweigh benefits?
    • Reinke C.M., Breitkreutz J., Leuenberger H. Aluminium in over-the-counter drugs-risks outweigh benefits?. Drug Saf. 2003, 26:1011-1025.
    • (2003) Drug Saf. , vol.26 , pp. 1011-1025
    • Reinke, C.M.1    Breitkreutz, J.2    Leuenberger, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.