메뉴 건너뛰기




Volumn 583, Issue 22, 2009, Pages 3569-3576

Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity

Author keywords

( ) Epigallocatechin 3 gallate; Aggregation; Amyloid; Transthyretin

Indexed keywords

CATECHIN; EPIGALLOCATECHIN GALLATE; PREALBUMIN;

EID: 71749085436     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.062     Document Type: Article
Times cited : (115)

References (31)
  • 2
    • 67049115575 scopus 로고    scopus 로고
    • The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection
    • Hauber I., Hohenberg H., Holstermann B., Hunstein W., and Hauber J. The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc. Natl. Acad. Sci. USA 106 22 (2009) 9033-9038
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.22 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5
  • 3
    • 34848818004 scopus 로고    scopus 로고
    • The molecular biology and clinical features of amyloid neuropathy
    • Benson M.D., and Kincaid J.C. The molecular biology and clinical features of amyloid neuropathy. Muscle Nerve 36 (2007) 411-423
    • (2007) Muscle Nerve , vol.36 , pp. 411-423
    • Benson, M.D.1    Kincaid, J.C.2
  • 4
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)
    • Saraiva M.J., Birken S., Costa P.P., and Goodman D.S. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J. Clin. Invest. 74 (1984) 104-119
    • (1984) J. Clin. Invest. , vol.74 , pp. 104-119
    • Saraiva, M.J.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 5
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • Cardoso I., Goldsbury C.S., Müller S.A., Olivieri V., Wirtz S., Damas A.M., Aebi U., and Saraiva M.J. Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. J. Mol. Biol. 317 (2002) 683-695
    • (2002) J. Mol. Biol. , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Müller, S.A.3    Olivieri, V.4    Wirtz, S.5    Damas, A.M.6    Aebi, U.7    Saraiva, M.J.8
  • 6
    • 0034405428 scopus 로고    scopus 로고
    • Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils
    • Redondo C., Damas A.M., Olofsson A., Lundgren E., and Saraiva M.J. Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils. J. Mol. Biol. 304 (2000) 461-470
    • (2000) J. Mol. Biol. , vol.304 , pp. 461-470
    • Redondo, C.1    Damas, A.M.2    Olofsson, A.3    Lundgren, E.4    Saraiva, M.J.5
  • 7
    • 0030694782 scopus 로고    scopus 로고
    • The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution
    • Quintas A., Saraiva M.J., and Brito R.M. The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution. FEBS Lett. 418 (1997) 297-300
    • (1997) FEBS Lett. , vol.418 , pp. 297-300
    • Quintas, A.1    Saraiva, M.J.2    Brito, R.M.3
  • 8
    • 0017824077 scopus 로고
    • Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
    • Blake C.C., Geisow M.J., Oatley S.J., Rerat B., and Rerat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J. Mol. Biol. 121 (1978) 339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 9
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen S.L., Lai Z., Miroy G.J., Kelly J.W., and Colón W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34 41 (1995) 13527-13536
    • (1995) Biochemistry , vol.34 , Issue.41 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colón, W.5
  • 10
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A., Vaz D.C., Cardoso I., Saraiva M.J., and Brito R.M. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J. Biol. Chem. 276 29 (2001) 27207-27213
    • (2001) J. Biol. Chem. , vol.276 , Issue.29 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 12
    • 0032970177 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
    • Baures P.W., Oza V.B., Peterson S.A., and Kelly J.W. Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid. Bioorg. Med. Chem. 7 (1999) 1339-1347
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1339-1347
    • Baures, P.W.1    Oza, V.B.2    Peterson, S.A.3    Kelly, J.W.4
  • 16
    • 3242807241 scopus 로고    scopus 로고
    • Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative
    • Almeida M.R., Macedo B., Cardoso I., Alves I., Valencia G., Arsequell G., Planas A., and Saraiva M.J. Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative. Biochem. J. 381 (2004) 351-356
    • (2004) Biochem. J. , vol.381 , pp. 351-356
    • Almeida, M.R.1    Macedo, B.2    Cardoso, I.3    Alves, I.4    Valencia, G.5    Arsequell, G.6    Planas, A.7    Saraiva, M.J.8
  • 18
    • 1642419758 scopus 로고    scopus 로고
    • Thermodynamics of interaction between hydrophobically modified polyelectrolyte and sodium dodecyl sulfate in aqueous solution
    • Bai G., Santos L.M.N.B.F., Nichifor M., Lopes A., and Bastos M. Thermodynamics of interaction between hydrophobically modified polyelectrolyte and sodium dodecyl sulfate in aqueous solution. J. Phys. Chem. B 108 (2004) 405-413
    • (2004) J. Phys. Chem. B , vol.108 , pp. 405-413
    • Bai, G.1    Santos, L.M.N.B.F.2    Nichifor, M.3    Lopes, A.4    Bastos, M.5
  • 19
    • 0025785547 scopus 로고
    • Fast titration experiments using heat conduction microcalorimeters
    • Bastos M., Hägg S., Lönnbro P., and Wadsö I. Fast titration experiments using heat conduction microcalorimeters. J. Biochem. Biophys. Meth. 23 (1991) 255-258
    • (1991) J. Biochem. Biophys. Meth. , vol.23 , pp. 255-258
    • Bastos, M.1    Hägg, S.2    Lönnbro, P.3    Wadsö, I.4
  • 20
    • 0032994562 scopus 로고    scopus 로고
    • Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradients
    • Altland K., Winter P., and Sauerborn M.K. Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradients. Electrophoresis 20 (1999) 1349-1364
    • (1999) Electrophoresis , vol.20 , pp. 1349-1364
    • Altland, K.1    Winter, P.2    Sauerborn, M.K.3
  • 21
    • 36348960658 scopus 로고    scopus 로고
    • Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design
    • Cardoso I., Almeida M.R., Ferreira N., Arsequell G., Valencia G., and Saraiva M.J. Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design. Biochem. J. 408 (2007) 131-138
    • (2007) Biochem. J. , vol.408 , pp. 131-138
    • Cardoso, I.1    Almeida, M.R.2    Ferreira, N.3    Arsequell, G.4    Valencia, G.5    Saraiva, M.J.6
  • 26
    • 0042334847 scopus 로고    scopus 로고
    • Pharmacokinetics and safety of green tea polyphenols after multiple-dose administration of epigallocatechin gallate and polyphenon E in healthy individuals
    • Chow H.H., Cai Y., Hakim I.A., Crowell J.A., Shahi F., Brooks C.A., Dorr R.T., Hara Y., and Alberts D.S. Pharmacokinetics and safety of green tea polyphenols after multiple-dose administration of epigallocatechin gallate and polyphenon E in healthy individuals. Clin. Cancer Res. 9 9 (2003) 3312-3319
    • (2003) Clin. Cancer Res. , vol.9 , Issue.9 , pp. 3312-3319
    • Chow, H.H.1    Cai, Y.2    Hakim, I.A.3    Crowell, J.A.4    Shahi, F.5    Brooks, C.A.6    Dorr, R.T.7    Hara, Y.8    Alberts, D.S.9
  • 27
    • 33745610160 scopus 로고    scopus 로고
    • Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: fluorescence, Fourier transform infrared, circular dichroism, and docking studies
    • Maiti T.K., Ghosh K.S., and Dasgupta S. Interaction of (-)-epigallocatechin-3-gallate with human serum albumin: fluorescence, Fourier transform infrared, circular dichroism, and docking studies. Proteins 64 (2006) 355-362
    • (2006) Proteins , vol.64 , pp. 355-362
    • Maiti, T.K.1    Ghosh, K.S.2    Dasgupta, S.3
  • 29
    • 34249861281 scopus 로고    scopus 로고
    • Pharmacokinetics of (-)-epigallocatechin-3-gallate in conscious and freely moving rats and its brain regional distribution
    • Lin L.C., Wang M.N., Tseng T.Y., Sung J.S., and Tsai T.H. Pharmacokinetics of (-)-epigallocatechin-3-gallate in conscious and freely moving rats and its brain regional distribution. J. Agric. Food Chem. 55 (2007) 1517-1524
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 1517-1524
    • Lin, L.C.1    Wang, M.N.2    Tseng, T.Y.3    Sung, J.S.4    Tsai, T.H.5
  • 31
    • 48349135202 scopus 로고    scopus 로고
    • A new Thr49Pro transthyretin gene mutation associated with leptomeningeal amyloidosis
    • Nakagawa K., Sheikh S.I., Snuderl M., Frosch M.P., and Greenberg S.M. A new Thr49Pro transthyretin gene mutation associated with leptomeningeal amyloidosis. J. Neurol. Sci. 272 (2008) 186-190
    • (2008) J. Neurol. Sci. , vol.272 , pp. 186-190
    • Nakagawa, K.1    Sheikh, S.I.2    Snuderl, M.3    Frosch, M.P.4    Greenberg, S.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.