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Volumn 4, Issue 1, 2010, Pages 26-31

Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins

Author keywords

Amyloid fibril; Amyloid ; Cytotoxicity; Fibril formation; Inhibitor; Prion; Pyrroloquinoline quinone

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; PRION PROTEIN; PYRROLOQUINOLINEQUINONE;

EID: 77949286151     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.4.1.10889     Document Type: Article
Times cited : (35)

References (36)
  • 2
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimer's disease
    • Goedert M, Spillantini MG. A century of Alzheimer's disease. Science 2006; 314:777-81.
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT. Protofibrils, pores, fibrils and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003; 26:267-98.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 5
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006; 443:774-9.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 6
    • 0034103006 scopus 로고    scopus 로고
    • Physiological importance of quinoenzymes and the O-quinone family of cofactors
    • Stites TE, Mitchell AE, Rucker RB. Physiological importance of quinoenzymes and the O-quinone family of cofactors. J Nutr 2000; 130:719-27.
    • (2000) J Nutr , vol.130 , pp. 719-727
    • Stites, T.E.1    Mitchell, A.E.2    Rucker, R.B.3
  • 9
    • 0242668745 scopus 로고    scopus 로고
    • Nutritional biochemistry: A new redox-cofactor vitamin for mammals
    • Kasahara T, Kato T. Nutritional biochemistry: A new redox-cofactor vitamin for mammals. Nature 2003; 422:832.
    • (2003) Nature , vol.422 , pp. 832
    • Kasahara, T.1    Kato, T.2
  • 10
    • 33745255091 scopus 로고    scopus 로고
    • Neuroprotection by pyrroloquinoline quinone (PQQ) in reversible middle cerebral artery occlusion in the adult rat
    • Zhang Y, Feustel PJ, Kimelberg HK. Neuroprotection by pyrroloquinoline quinone (PQQ) in reversible middle cerebral artery occlusion in the adult rat. Brain Res 2006; 1094:200-6.
    • (2006) Brain Res , vol.1094 , pp. 200-206
    • Zhang, Y.1    Feustel, P.J.2    Kimelberg, H.K.3
  • 12
    • 33749034211 scopus 로고    scopus 로고
    • Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42
    • Zameer A, Schulz P, Wang MS, Sierks MR. Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42. Biochemistry 2006; 45:11532-9.
    • (2006) Biochemistry , vol.45 , pp. 11532-11539
    • Zameer, A.1    Schulz, P.2    Wang, M.S.3    Sierks, M.R.4
  • 13
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42
    • Liu R, Barkhordarian H, Emadi S, Park CB, Sierks MR. 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
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.B.4    Sierks, M.R.5
  • 14
    • 33748504563 scopus 로고    scopus 로고
    • Inhibitor discovery targeting the intermediate structure of beta-amyloid peptide on the conformational transition pathway: Implications in the aggregation mechanism of beta-amyloid peptide
    • Liu D, Xu Y, Feng Y, Liu H, Shen X, Chen K, et al. Inhibitor discovery targeting the intermediate structure of beta-amyloid peptide on the conformational transition pathway: implications in the aggregation mechanism of beta-amyloid peptide. Biochemistry 2006; 45:10963-72.
    • (2006) Biochemistry , vol.45 , pp. 10963-10972
    • Liu, D.1    Xu, Y.2    Feng, Y.3    Liu, H.4    Shen, X.5    Chen, K.6
  • 15
    • 0038795608 scopus 로고    scopus 로고
    • An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
    • Sabate R, Gallardo M, Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 2003; 71:190-5.
    • (2003) Biopolymers , vol.71 , pp. 190-195
    • Sabate, R.1    Gallardo, M.2    Estelrich, J.3
  • 16
    • 22544478124 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein. Implication for dopaminergic neurodegeneration
    • Li HT, Lin DH, Luo XY, Zhang F, Ji LN, Du HN, et al. Inhibition of alpha-synuclein fibrillization by dopamine analogs via reaction with the amino groups of alpha-synuclein. Implication for dopaminergic neurodegeneration. Febs J 2005; 272:3661-72.
    • (2005) Febs J , vol.272 , pp. 3661-3672
    • Li, H.T.1    Lin, D.H.2    Luo, X.Y.3    Zhang, F.4    Ji5    LN, D.H.6
  • 17
    • 2442534084 scopus 로고    scopus 로고
    • Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine
    • Moussa CE, Wersinger C, Tomita Y, Sidhu A. Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine. Biochemistry 2004; 43:5539-50.
    • (2004) Biochemistry , vol.43 , pp. 5539-5550
    • Moussa, C.E.1    Wersinger, C.2    Tomita, Y.3    Sidhu, A.4
  • 19
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova OV, Breydo L, Parfenov AS, Salnikov VV, Baskakov IV. In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J Mol Biol 2005; 346:645-59.
    • (2005) J Mol Biol , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 20
    • 0037385673 scopus 로고    scopus 로고
    • In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion
    • Kirby L, Birkett CR, Rudyk H, Gilbert IH, Hope J. In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion. J Gen Virol 2003; 84:1013-20.
    • (2003) J Gen Virol , vol.84 , pp. 1013-1020
    • Kirby, L.1    Birkett, C.R.2    Rudyk, H.3    Gilbert, I.H.4    Hope, J.5
  • 21
    • 14044250915 scopus 로고    scopus 로고
    • In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features
    • Baskakov IV, Bocharova OV. In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features. Biochemistry 2005; 44:2339-48.
    • (2005) Biochemistry , vol.44 , pp. 2339-2348
    • Baskakov, I.V.1    Bocharova, O.V.2
  • 22
    • 68949207033 scopus 로고    scopus 로고
    • Nanostructure fabrication based on engineered α-synuclein
    • Kobayashi M, Han S, Nakamura C, Sode K. Nanostructure fabrication based on engineered α-synuclein. NanoBioTechnology 2008; 4:50-5.
    • (2008) NanoBioTechnology , vol.4 , pp. 50-55
    • Kobayashi, M.1    Han, S.2    Nakamura, C.3    Sode, K.4
  • 23
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • Porat Y, Abramowitz A, Gazit E. Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des 2006; 67:27-37.
    • (2006) Chem Biol Drug Des , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 24
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alphasynuclein and disaggregates existing fibrils
    • Zhu M, Rajamani S, Kaylor J, Han S, Zhou F, Fink AL. The flavonoid baicalein inhibits fibrillation of alphasynuclein and disaggregates existing fibrils. J Biol Chem 2004; 279:26846-57.
    • (2004) J Biol Chem , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajamani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 25
    • 33644945380 scopus 로고    scopus 로고
    • Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro
    • Ono K, Yamada M. Antioxidant compounds have potent anti-fibrillogenic and fibril-destabilizing effects for alpha-synuclein fibrils in vitro. J Neurochem 2006; 97:105-15.
    • (2006) J Neurochem , vol.97 , pp. 105-115
    • Ono, K.1    Yamada, M.2
  • 26
    • 33847769109 scopus 로고    scopus 로고
    • Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: Evidence for multiple steps and lateral association coupled to conformational conversion
    • Kumar S, Mohanty SK, Udgaonkar JB. Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion. J Mol Biol 2007; 367:1186-204.
    • (2007) J Mol Biol , vol.367 , pp. 1186-1204
    • Kumar, S.1    Mohanty, S.K.2    Udgaonkar, J.B.3
  • 27
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments
    • El-Agnaf OM, Jakes R, Curran MD, Middleton D, Ingenito R, Bianchi E, et al. Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett 1998; 440:71-5.
    • (1998) FEBS Lett , vol.440 , pp. 71-75
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6
  • 28
    • 0029904487 scopus 로고    scopus 로고
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-15.
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996; 35:13709-15.
  • 29
    • 33846465955 scopus 로고    scopus 로고
    • Effect of Reparation of Repeat Sequences in the Human alpha-Synuclein on Fibrillation Ability
    • Sode K, Ochiai S, Kobayashi N, Usuzaka E. Effect of Reparation of Repeat Sequences in the Human alpha-Synuclein on Fibrillation Ability. Int J Biol Sci 2007; 3:1-7.
    • (2007) Int J Biol Sci , vol.3 , pp. 1-7
    • Sode, K.1    Ochiai, S.2    Kobayashi, N.3    Usuzaka, E.4
  • 31
    • 0030878056 scopus 로고    scopus 로고
    • Recombinant full-length murine prion protein, mPrP(23-231): Purification and spectroscopic characterization
    • Hornemann S, Korth C, Oesch B, Riek R, Wider G, Wuthrich K, et al. Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. FEBS Lett 1997; 413:277-81.
    • (1997) FEBS Lett , vol.413 , pp. 277-281
    • Hornemann, S.1    Korth, C.2    Oesch, B.3    Riek, R.4    Wider, G.5    Wuthrich, K.6
  • 32
    • 0025760181 scopus 로고
    • Intestinal absorption and tissue distribution of [14C] pyrroloquinoline quinone in mice
    • Smidt CR, Unkefer CJ, Houck DR, Rucker RB. Intestinal absorption and tissue distribution of [14C] pyrroloquinoline quinone in mice. Proc Soc Exp Biol Med 1991; 197:27-31.
    • (1991) Proc Soc Exp Biol Med , vol.197 , pp. 27-31
    • Smidt, C.R.1    Unkefer, C.J.2    Houck, D.R.3    Rucker, R.B.4
  • 33
    • 63349090588 scopus 로고    scopus 로고
    • Recent advances in medicinal chemistry and pharmaceutical technology - strategies for drug delivery to the brain
    • Denora N, Trapani A, Laquintana V, Lopedota A, Trapani G. Recent advances in medicinal chemistry and pharmaceutical technology - strategies for drug delivery to the brain. Curr Top Med Chem 2009; 9:182-96.
    • (2009) Curr Top Med Chem , vol.9 , pp. 182-196
    • Denora, N.1    Trapani, A.2    Laquintana, V.3    Lopedota, A.4    Trapani, G.5
  • 34
    • 4544227975 scopus 로고    scopus 로고
    • Vitamin A exhibits potent antiamy-loidogenic and fibril-destabilizing effects in vitro
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M. Vitamin A exhibits potent antiamy-loidogenic and fibril-destabilizing effects in vitro. Exp Neurol 2004; 189:380-92.
    • (2004) Exp Neurol , vol.189 , pp. 380-392
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 35
    • 0033935718 scopus 로고    scopus 로고
    • Use of firefly luciferase in ATP-related assays of biomass, enzymes and metabolites
    • Lundin A. Use of firefly luciferase in ATP-related assays of biomass, enzymes and metabolites. Methods Enzymol 2000; 305:346-70.
    • (2000) Methods Enzymol , vol.305 , pp. 346-370
    • Lundin, A.1
  • 36
    • 0035823098 scopus 로고    scopus 로고
    • Cytotoxicity tests for high-throughput drug discovery
    • Slater K. Cytotoxicity tests for high-throughput drug discovery. Curr Opin Biotechnol 2001; 12:70-4.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 70-74
    • Slater, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.