메뉴 건너뛰기




Volumn 50, Issue 13, 2011, Pages 2445-2455

Biflavonoids are superior to monoflavonoids in inhibiting amyloid-β toxicity and fibrillogenesis via accumulation of nontoxic oligomer-like structures

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; DIFFERENTIAL EFFECT; FIBRILLOGENESIS; INSOLUBLE FIBRILS; OLIGOMERIC STRUCTURE; SMALL MOLECULES; THERAPEUTIC STRATEGY;

EID: 79953199374     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101731d     Document Type: Article
Times cited : (101)

References (42)
  • 1
    • 0027374493 scopus 로고
    • Normal cellular processing of the β-amyloid precursor protein results in the secretion of the amyloid β peptide and related molecules
    • DOI 10.1111/j.1749-6632.1993.tb23037.x
    • Haass, C., Hung, A. Y., Schlossmacher, M. G., Oltersdorf, T., Teplow, D. B., and Selkoe, D. J. (1993) Normal cellular processing of the β-amyloid precursor protein results in the secretion of the amyloid β peptide and related molecules Ann. N.Y. Acad. Sci. 695, 109-116 (Pubitemid 23348246)
    • (1993) Annals of the New York Academy of Sciences , vol.695 , pp. 109-116
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Oltersdorf, T.4    Teplow, D.B.5    Selkoe, D.J.6
  • 2
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • DOI 10.1126/science.1079469
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300, 486-489 (Pubitemid 36444329)
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabel, C.G.7
  • 3
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh, D. M. and Selkoe, D. J. (2007) Aβ oligomers: A decade of discovery J. Neurochem. 101, 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 4
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G. G. and Wong, C. W. (1984) Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein Biochem. Biophys. Res. Commun. 122, 1131-1135 (Pubitemid 14027629)
    • (1984) Biochemical and Biophysical Research Communications , vol.122 , Issue.3 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease: Genes, proteins, and therapy Physiol. Rev. 81, 741-766 (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 6
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 33749507375 scopus 로고    scopus 로고
    • Conformation-dependent anti-amyloid oligomer antibodies
    • DOI 10.1016/S0076-6879(06)13017-7, PII S0076687906130177, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Kayed, R. and Glabe, C. G. (2006) Conformation-dependent anti-amyloid oligomer antibodies Methods Enzymol. 413, 326-344 (Pubitemid 44528698)
    • (2006) Methods in Enzymology , vol.413 , pp. 326-344
    • Kayed, R.1    Glabe, C.G.2
  • 8
    • 0035005101 scopus 로고    scopus 로고
    • New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage
    • DOI 10.1038/35074581
    • Petit, A., Bihel, F., Alves da Costa, C., Pourquie, O., Checler, F., and Kraus, J. L. (2001) New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage Nat. Cell Biol. 3, 507-511 (Pubitemid 32422088)
    • (2001) Nature Cell Biology , vol.3 , Issue.5 , pp. 507-511
    • Petit, A.1    Bihel, F.2    Da Costa, C.A.3    Pourquie, O.4    Checler, F.5    Kraus, J.-L.6
  • 10
    • 0345669752 scopus 로고    scopus 로고
    • Alzheimer's disease: The cholesterol connection
    • DOI 10.1038/nn0403-345
    • Puglielli, L., Tanzi, R. E., and Kovacs, D. M. (2003) Alzheimer's disease: The cholesterol connection Nat. Neurosci. 6, 345-351 (Pubitemid 36373979)
    • (2003) Nature Neuroscience , vol.6 , Issue.4 , pp. 345-351
    • Puglielli, L.1    Tanzi, R.E.2    Kovacs, D.M.3
  • 12
    • 34548182307 scopus 로고    scopus 로고
    • Structure-activity relationships of amyloid beta-aggregation inhibitors based on curcumin: Influence of linker length and flexibility
    • DOI 10.1111/j.1747-0285.2007.00557.x
    • Reinke, A. A. and Gestwicki, J. E. (2007) Structure-activity relationships of amyloid β-aggregation inhibitors based on curcumin: Influence of linker length and flexibility Chem. Biol. Drug Des. 70, 206-215 (Pubitemid 47305405)
    • (2007) Chemical Biology and Drug Design , vol.70 , Issue.3 , pp. 206-215
    • Reinke, A.A.1    Gestwicki, J.E.2
  • 13
    • 0036848056 scopus 로고    scopus 로고
    • A novel β-sheet breaker, RS-0406, reverses amyloid β-induced cytotoxicity and impairment of long-term potentiation in vitro
    • DOI 10.1038/sj.bjp.0704911
    • Nakagami, Y., Nishimura, S., Murasugi, T., Kaneko, I., Meguro, M., Marumoto, S., Kogen, H., Koyama, K., and Oda, T. (2002) A novel β-sheet breaker, RS-0406, reverses amyloid β-induced cytotoxicity and impairment of long-term potentiation in vitro Br. J. Pharmacol. 137, 676-682 (Pubitemid 35333093)
    • (2002) British Journal of Pharmacology , vol.137 , Issue.5 , pp. 676-682
    • Nakagami, Y.1    Nishimura, S.2    Murasugi, T.3    Kaneko, I.4    Meguro, M.5    Marumoto, S.6    Kogen, H.7    Koyama, K.8    Oda, T.9
  • 15
    • 34250674908 scopus 로고    scopus 로고
    • Ferulic acid and benzothiazole dimer derivatives with high binding affinity to β-amyloid fibrils
    • DOI 10.1016/j.bmcl.2007.04.079, PII S0960894X07005124
    • Byeon, S. R., Jin, Y. J., Lim, S. J., Lee, J. H., Yoo, K. H., Shin, K. J., Oh, S. J., and Kim, D. J. (2007) Ferulic acid and benzothiazole dimer derivatives with high binding affinity to β-amyloid fibrils Bioorg. Med. Chem. Lett. 17, 4022-4025 (Pubitemid 46929075)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.14 , pp. 4022-4025
    • Byeon, S.R.1    Jin, Y.J.2    Lim, S.J.3    Lee, J.H.4    Yoo, K.H.5    Shin, K.J.6    Oh, S.J.7    Kim, D.J.8
  • 16
    • 13744252140 scopus 로고    scopus 로고
    • A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by β-amyloid (1-42)
    • DOI 10.1016/j.bbrc.2005.01.030
    • Lee, K. H., Shin, B. H., Shin, K. J., Kim, D. J., and Yu, J. (2005) A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by β-amyloid (1-42) Biochem. Biophys. Res. Commun. 328, 816-823 (Pubitemid 40238712)
    • (2005) Biochemical and Biophysical Research Communications , vol.328 , Issue.4 , pp. 816-823
    • Lee, K.H.1    Shin, B.H.2    Shin, K.J.3    Kim, D.J.4    Yu, J.5
  • 18
    • 1942472491 scopus 로고    scopus 로고
    • Neuroprotective effects of resveratrol against β-amyloid-induced neurotoxicity in rat hippocampal neurons: Involvement of protein kinase C
    • DOI 10.1038/sj.bjp.0705688
    • Han, Y. S., Zheng, W. H., Bastianetto, S., Chabot, J. G., and Quirion, R. (2004) Neuroprotective effects of resveratrol against β-amyloid-induced neurotoxicity in rat hippocampal neurons: Involvement of protein kinase C Br. J. Pharmacol. 141, 997-1005 (Pubitemid 38510083)
    • (2004) British Journal of Pharmacology , vol.141 , Issue.6 , pp. 997-1005
    • Han, Y.-S.1    Zheng, W.-H.2    Bastianetto, S.3    Chabot, J.-G.4    Quirion, R.5
  • 19
    • 33745173188 scopus 로고    scopus 로고
    • Anti-amyloidogenic effects of antioxidants: Implications for the prevention and therapeutics of Alzheimer's disease
    • DOI 10.1016/j.bbadis.2006.03.002, PII S0925443906000469
    • Ono, K., Hamaguchi, T., Naiki, H., and Yamada, M. (2006) Anti-amyloidogenic effects of antioxidants: Implications for the prevention and therapeutics of Alzheimer's disease Biochim. Biophys. Acta 1762, 575-586 (Pubitemid 43903118)
    • (2006) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1762 , Issue.6 , pp. 575-586
    • Ono, K.1    Hamaguchi, T.2    Naiki, H.3    Yamada, M.4
  • 20
    • 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
    • DOI 10.1046/j.1471-4159.2003.01976.x
    • Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., and Yamada, M. (2003) Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease J. Neurochem. 87, 172-181 (Pubitemid 37210651)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.1 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 21
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • DOI 10.1096/fj.06-7986com
    • Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., and Wilson, M. R. (2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures FASEB J. 21, 2312-2322 (Pubitemid 47230661)
    • (2007) FASEB Journal , vol.21 , Issue.10 , pp. 2312-2322
    • Yerbury, J.J.1    Poon, S.2    Meehan, S.3    Thompson, B.4    Kumita, J.R.5    Dobson, C.M.6    Wilson, M.R.7
  • 22
    • 33750853036 scopus 로고    scopus 로고
    • The development of preventives and therapeutics for Alzheimer's disease that inhibit the formation of β-amyloid fibrils (fAβ), as well as destabilize preformed fAβ
    • DOI 10.2174/138161206778793010
    • Ono, K., Naiki, H., and Yamada, M. (2006) The development of preventives and therapeutics for Alzheimer's disease that inhibit the formation of β-amyloid fibrils (fAβ), as well as destabilize preformed fAβ Curr. Pharm. Des. 12, 4357-4375 (Pubitemid 44718294)
    • (2006) Current Pharmaceutical Design , vol.12 , Issue.33 , pp. 4357-4375
    • Ono, K.1    Naiki, H.2    Yamada, M.3
  • 24
    • 38549085819 scopus 로고    scopus 로고
    • Biflavonoids isolated from Selaginella tamariscina regulate the expression of matrix metalloproteinase in human skin fibroblasts
    • DOI 10.1016/j.bmc.2007.10.036, PII S0968089607009054
    • Lee, C. W., Choi, H. J., Kim, H. S., Kim, D. H., Chang, I. S., Moon, H. T., Lee, S. Y., Oh, W. K., and Woo, E. R. (2008) Biflavonoids isolated from Selaginella tamariscina regulate the expression of matrix metalloproteinase in human skin fibroblasts Bioorg. Med. Chem. 16, 732-738 (Pubitemid 351163066)
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.2 , pp. 732-738
    • Lee, C.-W.1    Choi, H.-J.2    Kim, H.-S.3    Kim, D.-H.4    Chang, I.-S.5    Moon, H.T.6    Lee, S.-Y.7    Oh, W.K.8    Woo, E.-R.9
  • 25
    • 34250206336 scopus 로고    scopus 로고
    • Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides
    • DOI 10.1016/j.bbrc.2007.05.186, PII S0006291X07011825
    • Shahnawaz, M., Thapa, A., and Park, I. S. (2007) Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides Biochem. Biophys. Res. Commun. 359, 801-805 (Pubitemid 46899021)
    • (2007) Biochemical and Biophysical Research Communications , vol.359 , Issue.3 , pp. 801-805
    • Shahnawaz, M.1    Thapa, A.2    Park, I.-S.3
  • 26
    • 18944407388 scopus 로고    scopus 로고
    • Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • DOI 10.1523/JNEUROSCI.2381-04.2005
    • Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., and Rydel, R. E. (2005) Nucleation-dependent polymerization is an essential component of amyloid-mediated neuronal cell death J. Neurosci. 25, 1071-1080 (Pubitemid 41741352)
    • (2005) Journal of Neuroscience , vol.25 , Issue.5 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 27
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's β-amyloid fibril formation in vitro
    • DOI 10.1021/bi980550y
    • Naiki, H., Hasegawa, K., Yamaguchi, I., Nakamura, H., Gejyo, F., and Nakakuki, K. (1998) Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer's β-amyloid fibril formation in vitro Biochemistry 37, 17882-17889 (Pubitemid 29023943)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17882-17889
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Gejyo, F.5    Nakakuki, K.6
  • 28
    • 0024595042 scopus 로고
    • Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill
    • DOI 10.1016/0022-1759(89)90397-9
    • Hansen, M. B., Nielsen, S. E., and Berg, K. (1989) Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill J. Immunol. Methods 119, 203-210 (Pubitemid 19132276)
    • (1989) Journal of Immunological Methods , vol.119 , Issue.2 , pp. 203-210
    • Hansen, M.B.1    Nielsen, S.E.2    Berg, K.3
  • 29
    • 36248979229 scopus 로고    scopus 로고
    • + inhibits apoptosis by suppressing the Apaf-1 apoptosome formation and subsequent downstream pathways but not cytochrome c release
    • DOI 10.1038/sj.cdd.4402221, PII 4402221
    • + inhibits apoptosis by suppressing the Apaf-1 apoptosome formation and subsequent downstream pathways but not cytochrome c release Cell Death Differ. 14, 2068-2075 (Pubitemid 350131156)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.12 , pp. 2068-2075
    • Karki, P.1    Seong, C.2    Kim, J.-E.3    Hur, K.4    Shin, S.Y.5    Lee, J.S.6    Cho, B.7    Park, I.-S.8
  • 30
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct J. Biol. Chem. 282, 10311-10324 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 31
    • 77956622149 scopus 로고    scopus 로고
    • Amyloid-β fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly
    • Chi, E. Y., Frey, S. L., Winans, A., Lam, K. L., Kjaer, K., Majewski, J., and Lee, K. Y. (2010) Amyloid-β fibrillogenesis seeded by interface-induced peptide misfolding and self-assembly Biophys. J. 98, 2299-2308
    • (2010) Biophys. J. , vol.98 , pp. 2299-2308
    • Chi, E.Y.1    Frey, S.L.2    Winans, A.3    Lam, K.L.4    Kjaer, K.5    Majewski, J.6    Lee, K.Y.7
  • 32
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki, H. and Nakakuki, K. (1996) First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro Lab. Invest. 74, 374-383 (Pubitemid 26072080)
    • (1996) Laboratory Investigation , vol.74 , Issue.2 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 34
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic, J. L., Pensalfini, A., Head, E., and Glabe, C. G. (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction Neurobiol. Dis. 35, 352-358
    • (2009) Neurobiol. Dis. , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 35
    • 57149145222 scopus 로고    scopus 로고
    • The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of amyloid-β aggregation, fibrillogenesis, and toxicity
    • Jan, A., Gokce, O., Luthi-Carter, R., and Lashuel, H. A. (2008) The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of amyloid-β aggregation, fibrillogenesis, and toxicity J. Biol. Chem. 283, 28176-28189
    • (2008) J. Biol. Chem. , vol.283 , pp. 28176-28189
    • Jan, A.1    Gokce, O.2    Luthi-Carter, R.3    Lashuel, H.A.4
  • 36
    • 70349481513 scopus 로고    scopus 로고
    • The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds
    • Hudson, S. A., Ecroyd, H., Kee, T. W., and Carver, J. A. (2009) The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds FEBS J. 276, 5960-5972
    • (2009) FEBS J. , vol.276 , pp. 5960-5972
    • Hudson, S.A.1    Ecroyd, H.2    Kee, T.W.3    Carver, J.A.4
  • 39
    • 33644878337 scopus 로고    scopus 로고
    • Polyphenol amentoflavone affords neuroprotection against neonatal hypoxic-ischemic brain damage via multiple mechanisms
    • Shin, D. H., Bae, Y. C., Kim-Han, J. S., Lee, J. H., Choi, I. Y., Son, K. H., Kang, S. S., Kim, W. K., and Han, B. H. (2006) Polyphenol amentoflavone affords neuroprotection against neonatal hypoxic-ischemic brain damage via multiple mechanisms J. Neurochem. 96, 561-572
    • (2006) J. Neurochem. , vol.96 , pp. 561-572
    • Shin, D.H.1    Bae, Y.C.2    Kim-Han, J.S.3    Lee, J.H.4    Choi, I.Y.5    Son, K.H.6    Kang, S.S.7    Kim, W.K.8    Han, B.H.9
  • 40
    • 0035895957 scopus 로고    scopus 로고
    • The neuroprotective effects of phytoestrogens on amyloid β protein-induced toxicity are mediated by abrogating the activation of caspase cascade in rat cortical neurons
    • Wang, C. N., Chi, C. W., Lin, Y. L., Chen, C. F., and Shiao, Y. J. (2001) The neuroprotective effects of phytoestrogens on amyloid β protein-induced toxicity are mediated by abrogating the activation of caspase cascade in rat cortical neurons J. Biol. Chem. 276, 5287-5295
    • (2001) J. Biol. Chem. , vol.276 , pp. 5287-5295
    • Wang, C.N.1    Chi, C.W.2    Lin, Y.L.3    Chen, C.F.4    Shiao, Y.J.5
  • 41
    • 33747188963 scopus 로고    scopus 로고
    • Apigenin-induced-apoptosis is mediated by the activation of PKCδ and caspases in leukemia cells
    • DOI 10.1016/j.bcp.2006.06.010, PII S0006295206003315
    • Vargo, M. A., Voss, O. H., Poustka, F., Cardounel, A. J., Grotewold, E., and Doseff, A. I. (2006) Apigenin-induced-apoptosis is mediated by the activation of PKCδ and caspases in leukemia cells Biochem. Pharmacol. 72, 681-692 (Pubitemid 44233544)
    • (2006) Biochemical Pharmacology , vol.72 , Issue.6 , pp. 681-692
    • Vargo, M.A.1    Voss, O.H.2    Poustka, F.3    Cardounel, A.J.4    Grotewold, E.5    Doseff, A.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.