메뉴 건너뛰기




Volumn 21, Issue 8, 2010, Pages 726-735

Oleuropein aglycon prevents cytotoxic amyloid aggregation of human amylin

Author keywords

Amylin; Amyloid cytotoxicity; Extra virgin olive oil; HIAPP; Oleuropein; Type two diabetes

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; AMYLIN; AMYLOID; CASPASE 3; OLEUROPEIN; OLEUROPEIN AGLYCON; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 77954661025     PISSN: 09552863     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2009.04.010     Document Type: Article
Times cited : (111)

References (38)
  • 1
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003, 81:678-699.
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick S.B., Miranker A.D. Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 2002, 41:4694-4703.
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 4
    • 0026452254 scopus 로고
    • Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series
    • Rocken C., Linke R.P., Saeger W. Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series. Virchows Arch A Pathol Anat Histopathol 1992, 421:339-344.
    • (1992) Virchows Arch A Pathol Anat Histopathol , vol.421 , pp. 339-344
    • Rocken, C.1    Linke, R.P.2    Saeger, W.3
  • 5
    • 33747055111 scopus 로고    scopus 로고
    • β-cell deficit due to increased apoptosis in the human Islet Amyloid Polypeptide Transgenic (HIP) rat recapitulates the metabolic defects present in Type 2 Diabetes
    • Matveyenko A.V., Butler P.C. β-cell deficit due to increased apoptosis in the human Islet Amyloid Polypeptide Transgenic (HIP) rat recapitulates the metabolic defects present in Type 2 Diabetes. Diabetes 2006, 55:2106-2114.
    • (2006) Diabetes , vol.55 , pp. 2106-2114
    • Matveyenko, A.V.1    Butler, P.C.2
  • 6
    • 33644834054 scopus 로고    scopus 로고
    • Role of Islet amyloid in Type 2 diabetes mellitus
    • Höppener J.W.M., Lips C.J. Role of Islet amyloid in Type 2 diabetes mellitus. Int J Biochem Cell Biol 2006, 38:726-736.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 726-736
    • Höppener, J.W.M.1    Lips, C.J.2
  • 7
    • 0038015599 scopus 로고    scopus 로고
    • Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis
    • Ritzel R.A., Butler P.C. Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis. Diabetes 2003, 52:1701-1708.
    • (2003) Diabetes , vol.52 , pp. 1701-1708
    • Ritzel, R.A.1    Butler, P.C.2
  • 8
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in Type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L., Gurlo T., Huang J., Butler P.C. Islet amyloid in Type 2 diabetes, and the toxic oligomer hypothesis. Endocrin Rev 2008, 29:303-316.
    • (2008) Endocrin Rev , vol.29 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, J.3    Butler, P.C.4
  • 10
    • 3843148352 scopus 로고    scopus 로고
    • Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity
    • Bucciantini M., Calloni G., Chiti F., Formigli L., Nosi D., Dobson C.M., et al. Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 2004, 279:31374-31382.
    • (2004) J Biol Chem , vol.279 , pp. 31374-31382
    • Bucciantini, M.1    Calloni, G.2    Chiti, F.3    Formigli, L.4    Nosi, D.5    Dobson, C.M.6
  • 11
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield A.D. Amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic Res 2002, 36:1307-1313.
    • (2002) Free Radic Res , vol.36 , pp. 1307-1313
    • Butterfield, A.D.1
  • 13
    • 0036136289 scopus 로고    scopus 로고
    • Antioxidant and other biological activities of phenols from olives and olive oil
    • Visioli F., Poli A., Galli C. Antioxidant and other biological activities of phenols from olives and olive oil. Med Res Rev 2002, 22:65-75.
    • (2002) Med Res Rev , vol.22 , pp. 65-75
    • Visioli, F.1    Poli, A.2    Galli, C.3
  • 14
    • 0032472374 scopus 로고    scopus 로고
    • Oleuropein, the bitter principles of olives, enhances nitric oxide production by mouse macrophages
    • Visioli F., Bellosta S., Galli C. Oleuropein, the bitter principles of olives, enhances nitric oxide production by mouse macrophages. Life Sci 1998, 62:541-546.
    • (1998) Life Sci , vol.62 , pp. 541-546
    • Visioli, F.1    Bellosta, S.2    Galli, C.3
  • 15
    • 0037387575 scopus 로고    scopus 로고
    • Olive oil and red wine antioxidant polyphenols inhibit endothelial activation: antiatherogenic properties of mediterranean diet phytochemicals
    • Carluccio M.A., Siculella L., Ancora M.A., Massaro M., Scoditti E., Storelli C., et al. Olive oil and red wine antioxidant polyphenols inhibit endothelial activation: antiatherogenic properties of mediterranean diet phytochemicals. Arterioscler Thromb Vasc Biol 2003, 23:622-629.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 622-629
    • Carluccio, M.A.1    Siculella, L.2    Ancora, M.A.3    Massaro, M.4    Scoditti, E.5    Storelli, C.6
  • 17
    • 33847691208 scopus 로고    scopus 로고
    • Acute doxorubicin cardiotoxicity is successfully treated with the phytochemical oleuropein through suppression of oxidative and nitrosative stress
    • Andreadou I., Sigala F., Iliodromitis E.K., Papaefthimiou M., Sigalas C., Aligiannis N., et al. Acute doxorubicin cardiotoxicity is successfully treated with the phytochemical oleuropein through suppression of oxidative and nitrosative stress. J Mol Cell Cardiol 2007, 42:549-558.
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 549-558
    • Andreadou, I.1    Sigala, F.2    Iliodromitis, E.K.3    Papaefthimiou, M.4    Sigalas, C.5    Aligiannis, N.6
  • 18
    • 33746614354 scopus 로고    scopus 로고
    • The olive constituent oleuropein exhibits anti-ischemic, antioxidative, and hypolipidemic effects in anesthetized rabbits
    • Andreadou I., Iliodromitis E.K., Mikros E., Constantinou M., Agalias A., Magiatis P., et al. The olive constituent oleuropein exhibits anti-ischemic, antioxidative, and hypolipidemic effects in anesthetized rabbits. J Nutr 2006, 136:2213-2219.
    • (2006) J Nutr , vol.136 , pp. 2213-2219
    • Andreadou, I.1    Iliodromitis, E.K.2    Mikros, E.3    Constantinou, M.4    Agalias, A.5    Magiatis, P.6
  • 19
    • 33645125772 scopus 로고    scopus 로고
    • Noncovalent interaction between amyloid-β-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry
    • Bazoti F.N., Bergquist J., Markides K.E., Tsarbopoulos A. Noncovalent interaction between amyloid-β-peptide (1-40) and oleuropein studied by electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 2006, 17:568-575.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 568-575
    • Bazoti, F.N.1    Bergquist, J.2    Markides, K.E.3    Tsarbopoulos, A.4
  • 20
    • 48349093043 scopus 로고    scopus 로고
    • Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry
    • Bazoti F.N., Bergquist J., Markides K., Tsarbopoulos A. Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry. J Am Soc Mass Spectrom 2008, 19:1078-1085.
    • (2008) J Am Soc Mass Spectrom , vol.19 , pp. 1078-1085
    • Bazoti, F.N.1    Bergquist, J.2    Markides, K.3    Tsarbopoulos, A.4
  • 21
    • 33845467504 scopus 로고    scopus 로고
    • Inhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP
    • Meier J.J., Kayed R., Lin C.Y., Gurlo T., Haataja L., Jayasinghe S.J., et al. Inhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP. Am J Physiol Endocrinol Metab 2006, 291:1317-1324.
    • (2006) Am J Physiol Endocrinol Metab , vol.291 , pp. 1317-1324
    • Meier, J.J.1    Kayed, R.2    Lin, C.Y.3    Gurlo, T.4    Haataja, L.5    Jayasinghe, S.J.6
  • 22
    • 33144464982 scopus 로고    scopus 로고
    • Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis
    • Yan L.M., Tatarek-Nossol M., Velkova A., Kazantzis A., Kapurniotu A. Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis. Proc Natl Acad Sci U S A 2006, 103:2046-2051.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2046-2051
    • Yan, L.M.1    Tatarek-Nossol, M.2    Velkova, A.3    Kazantzis, A.4    Kapurniotu, A.5
  • 23
    • 0033529748 scopus 로고    scopus 로고
    • Enzymatic activation of oleuropein: a protein crosslinker used as chemical defence by privet tree
    • Konno K., Hirayama C., Yasui H., Nakamura M. Enzymatic activation of oleuropein: a protein crosslinker used as chemical defence by privet tree. Proc Natl Acad Sci U S A 1999, 96:9159-9162.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9159-9162
    • Konno, K.1    Hirayama, C.2    Yasui, H.3    Nakamura, M.4
  • 24
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 25
    • 0033538015 scopus 로고    scopus 로고
    • Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
    • Kayed R., Bernhagen J., Greenfield N., Sweimeh K.M., Brunner H., Voelter W., et al. Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. J Mol Biol 1999, 287:781-796.
    • (1999) J Mol Biol , vol.287 , pp. 781-796
    • Kayed, R.1    Bernhagen, J.2    Greenfield, N.3    Sweimeh, K.M.4    Brunner, H.5    Voelter, W.6
  • 26
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions
    • Porat Y., Mazor Y., Efrat S., Gazit E. Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 2004, 43:14454-14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 27
    • 14644435012 scopus 로고    scopus 로고
    • Patterns of cell death triggered in two different cell lines by HypF-N pre-fibrillar aggregates
    • Bucciantini M., Rigacci S., Berti A., Pieri L., Cecchi C., Nosi D., et al. Patterns of cell death triggered in two different cell lines by HypF-N pre-fibrillar aggregates. FASEB J 2005, 19:437-449.
    • (2005) FASEB J , vol.19 , pp. 437-449
    • Bucciantini, M.1    Rigacci, S.2    Berti, A.3    Pieri, L.4    Cecchi, C.5    Nosi, D.6
  • 29
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with Thioflavine T
    • LeVine H. Quantification of beta-sheet amyloid fibril structures with Thioflavine T. Methods Enzymol 1999, 309:274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine, H.1
  • 30
    • 44649150510 scopus 로고    scopus 로고
    • Recent insight in Islet amyloid polypeptide-induced membrane disruption and its role in β-cell death in Type 2 diabetes mellitus
    • Article ID 421287
    • Khemtémourian L., Killian J.A., Höppener J.W.M., Engel M.F.M. Recent insight in Islet amyloid polypeptide-induced membrane disruption and its role in β-cell death in Type 2 diabetes mellitus. Exp Diabetes Res 2008, Article ID 421287.
    • (2008) Exp Diabetes Res
    • Khemtémourian, L.1    Killian, J.A.2    Höppener, J.W.M.3    Engel, M.F.M.4
  • 31
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • Cerdà-Costa N., Esteras-Chopo A., Aviles F.X., Serrano L., Villegas V. Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J Mol Biol 2007, 366:1351-1353.
    • (2007) J Mol Biol , vol.366 , pp. 1351-1353
    • Cerdà-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 32
    • 43649108895 scopus 로고    scopus 로고
    • The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies
    • Rigacci S., Bucciantini M., Relini A., Pesce A., Gliozzi A., Berti A., et al. The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies. Biophys J 2008, 94:3635-3646.
    • (2008) Biophys J , vol.94 , pp. 3635-3646
    • Rigacci, S.1    Bucciantini, M.2    Relini, A.3    Pesce, A.4    Gliozzi, A.5    Berti, A.6
  • 33
    • 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
  • 34
    • 0032499596 scopus 로고    scopus 로고
    • Free radical-scavenging properties of olive oil polyphenols
    • Visioli F., Bellomo G., Galli C. Free radical-scavenging properties of olive oil polyphenols. Biochem Biophys Res Commun 1998, 247:60-64.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 60-64
    • Visioli, F.1    Bellomo, G.2    Galli, C.3
  • 35
    • 60349096360 scopus 로고    scopus 로고
    • Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol
    • Mishra R., Sellin D., Radovan D., Gohlke A., Winter R. Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol. Chembiochem 2009, 10:445-449.
    • (2009) Chembiochem , vol.10 , pp. 445-449
    • Mishra, R.1    Sellin, D.2    Radovan, D.3    Gohlke, A.4    Winter, R.5
  • 36
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human amylin
    • Tracz S.M., Abedini A., Driscoll M., Raleigh D.P. Role of aromatic interactions in amyloid formation by peptides derived from human amylin. Biochemistry 2004, 43:15901-15908.
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 38
    • 33744794936 scopus 로고    scopus 로고
    • The fate of olive oil polyphenols in the gastrointestinal tract: implications of gastric and colonic microflora-dependent biotransformation
    • Corona G., Tzounis X., Dessì M.A., Deiana M., Debnam E.S., Visioli F., et al. The fate of olive oil polyphenols in the gastrointestinal tract: implications of gastric and colonic microflora-dependent biotransformation. Free Radic Res 2006, 40:647-658.
    • (2006) Free Radic Res , vol.40 , pp. 647-658
    • Corona, G.1    Tzounis, X.2    Dessì, M.A.3    Deiana, M.4    Debnam, E.S.5    Visioli, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.