Effect of Green Tea Polyphenol Epigallocatechin-3-gallate on the Aggregation of αA(66-80) Peptide, a Major Fragment of αA-crystallin Involved in Cataract Development

References

• Ecroyd H, Carver JA. Crystallin proteins and amyloid fibrils. Cell Mol Life Sci 2009;66:62–81.
   PubMed Web of Science ®Google Scholar
• Sharma KK, Santhoshkumar P. Lens Aging: effects of crystallins. Biochim Biophys Acta 2009;1790:1095–1108.
   PubMed Web of Science ®Google Scholar
• Bloemendal H, de Jong W, Jaenicke R, Lubsen NH, Slingsby C, Tardieu A. Ageing and vision: structure, stability and function of lens crystallins. Prog Biophys Mol Biol 2004;86:407–485.
   PubMed Web of Science ®Google Scholar
• Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992;89:10449–10453.
   PubMed Web of Science ®Google Scholar
• Horwitz J, Emmons T, Takemoto L. The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent. Curr Eye Res 1992;11:817–822.
   PubMed Web of Science ®Google Scholar
• Hanson SR, Hasan A, Smith DL, Smith JB. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp Eye Res 2000;71:195–207.
   PubMed Web of Science ®Google Scholar
• Hariharapura R, Santhoshkumar P, Krishna Sharma K. Profiling of lens protease involved in generation of alphaA-66-80 crystallin peptide using an internally quenched protease substrate. Exp Eye Res 2013;109:51–59.
   PubMed Web of Science ®Google Scholar
• Lund AL, Smith JB, Smith DL. Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res 1996;63:661–672.
   PubMed Web of Science ®Google Scholar
• Harrington V, McCall S, Huynh S, Srivastava K, Srivastava OP. Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses. Mol Vis 2004;10:476–489.
   PubMed Web of Science ®Google Scholar
• Srivastava OP, Kirk MC, Srivastava K. Characterization of covalent multimers of crystallins in aging human lenses. J Biol Chem 2004;279:10901–10909.
   PubMed Web of Science ®Google Scholar
• Santhoshkumar P, Udupa P, Murugesan R, Sharma KK. Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation. J Biol Chem 2008;283:8477–8485.
   PubMed Web of Science ®Google Scholar
• Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 1998;7:471–474.
   PubMed Web of Science ®Google Scholar
• Vicart P, Caron A, Guicheney P, Li Z, Prévost MC, Faure A, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 1998;20:92–95.
   PubMed Web of Science ®Google Scholar
• Hains PG, Truscott RJ. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J Proteome Res 2007;6:3935–3943.
   PubMed Web of Science ®Google Scholar
• Hains PG, Truscott RJ. Proteomic analysis of the oxidation of cysteine residues in human age-related nuclear cataract lenses. Biochim Biophys Acta 2008;1784:1959–1964.
   PubMed Web of Science ®Google Scholar
• Lampi KJ, Zhixiang MA, Hanson SR, Azuma M, Shih M, Shearer TR, et al. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Exp Eye Res 1998;67:31–43.
   PubMed Web of Science ®Google Scholar
• Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, Smith JB. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 1998;67:21–30.
   PubMed Web of Science ®Google Scholar
• Zhang Z, Smith DL, Smith JB. Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate. Exp Eye Res 2003;77:259–272.
   PubMed Web of Science ®Google Scholar
• Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J 1995;9:1173–1182.
   PubMed Web of Science ®Google Scholar
• Srivastava OP. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp Eye Res 1988;47:525–543.
   PubMed Web of Science ®Google Scholar
• Su SP, McArthur JD, Andrew Aquilina J. Localization of low molecular weight crystallin peptides in the aging human lens using a MALDI mass spectrometry imaging approach. Exp Eye Res 2010;91:97–103.
   PubMed Web of Science ®Google Scholar
• Sreelakshmi Y, Santhoshkumar P, Bhattacharyya J, Sharma KK. αA-crystallin interacting regions in the small heat shock protein, αB-crystallin. Biochemistry 2004;43:15785–15795.
   PubMed Web of Science ®Google Scholar
• Santhoshkumar P, Raju M, Sharma KK. AlphaA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of alpha-crystallin and induces lens protein aggregation. PloS One 2011;6:e19291.
   PubMed Web of Science ®Google Scholar
• Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, et al. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 2011;144:67–78.
   PubMed Web of Science ®Google Scholar
• Carifi G, Miller MH, Pitsas C, Zygoura V, Deshmukh RR, Kopsachilis N, et al. Complications and outcomes of phacoemulsification cataract surgery complicated by anterior capsule tear. Am J Ophthalmol 2015;159:463–469.
   PubMed Web of Science ®Google Scholar
• Modi SS, Lehmann RP, Walters TR, Fong R, Christie WC, Roel L, et al. Once-daily nepafenac ophthalmic suspension 0.3% to prevent and treat ocular inflammation and pain after cataract surgery: phase 3 study. J Cataract Refract Surg 2014;40:203–211.
   PubMed Web of Science ®Google Scholar
• Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, et al. EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity. Proc Natl Acad Sci USA 2010;107:7710–7715.
   PubMed Web of Science ®Google Scholar
• Meng F, Abedini A, Plesner A, Bruce Verchere C, Raleigh DP. The flavanol (−)-epigallocatechin-3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils and protects cultured cells against IAPP induced toxicity. Biochemistry 2010;49:8127–8133.
   PubMed Web of Science ®Google Scholar
• Roberts BE, Duennwald ML, Wang H, Chung C, Lopreiato NP, Sweeny EA. A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat Chem Biol 2009;5:936–946.
   PubMed Web of Science ®Google Scholar
• Rambold AS, Miesbauer M, Olschewski D, Seidel R, Riemer C, Smale L, et al. Green tea extracts interfere with the stress-protective activity of PrP and the formation of PrP. J Neurochem 2008;107:218–229.
   PubMed Web of Science ®Google Scholar
• Hauber I, Hohenberg H, Holstermann B, Hunstein W, Hauber J. The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc Natl Acad Sci USA 2009;106:9033–9038.
   PubMed Web of Science ®Google Scholar
• Popovych N, Brender JR, Soong R, Vivekanandan S, Hartman K, Basrur V, et al. Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248–286). J Phys Chem B 2012;116:3650–3658.
   PubMed Web of Science ®Google Scholar
• Ghosh S, Pandey NK, Dasgupta S. (-)-Epicatechin gallate prevents alkali-salt mediated fibrillogenesis of hen egg white lysozyme. Int J Biol Macromol 2013;54:90–98.
   PubMed Web of Science ®Google Scholar
• Ehrnhoefer DE, Bieschke J, Boeddrich A, Herbst M, Masino L, Lurz R, et al. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 2008;15:558–566.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Hyung SJ, DeToma AS, Brender JR, Lee S, Vivekanandan S, Kochi A, et al. Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-beta species. Proc Natl Acad Sci USA 2013;110:3743–3748.
   PubMed Web of Science ®Google Scholar
• Bieschke J, Russ J, Friedrich RP, Ehrnhoefer DE, Wobst H, Neugebauer K, et al. EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity. Proc Natl Acad Sci USA 2010;107:7710–7715.
   PubMed Web of Science ®Google Scholar
• Pithadia A, Brender JR, Fierke CA, Ramamoorthy A. Inhibition of IAPP aggregation and toxicity by natural products and derivatives. J Diabetes Res 2016;2016:2046327.
   PubMed Web of Science ®Google Scholar
• Palhano FL, Lee J, Grimster NP, Kelly JW. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. J Am Chem Soc 2013;135:7503–7510.
   PubMed Web of Science ®Google Scholar
• Hudson SA, Ecroyd H, Dehle FC, Musgrave IF, Carver JA. (−)-Epigallocatechin-3-gallate (EGCG) maintains κ-Casein in its pre-fibrillar state without redirecting its aggregation pathway. J Mol Biol 2009;392:689–700.
   PubMed Web of Science ®Google Scholar
• Stenvang M, Christiansen G, Otzen DE. Epigallocatechin gallate remodels fibrils of lattice corneal dystrophy protein, facilitating proteolytic degradation and preventing formation of membrane-permeabilizing species. Biochemistry 2016;55:2344–2357.
   PubMed Web of Science ®Google Scholar
• Conchillo-Sole O, de Groot NS, Avilés FX, Vendrell J, Daura X, Ventura S. AGGRESCAN: a server for the prediction and evaluation of “hot spots” of aggregation in polypeptides. BMC Bioinformatics 2007;8:65.
   PubMed Web of Science ®Google Scholar
• Pande VS. A universal TANGO? Nat Biotechnol 2004;22:1240–1241.
   PubMed Web of Science ®Google Scholar
• Garbuzynskiy SO, Lobanov MY, Galzitskaya OV. FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics 2010;26:326–332.
   PubMed Web of Science ®Google Scholar
• Tsolis AC, Papandreou NC, Iconomidou VA, Hamodrakas SJ. A consensus method for the prediction of ‘aggregation-prone’ peptides in globular proteins. PLoS One 2013;8:e54175.
   PubMed Web of Science ®Google Scholar
• Klunk WE, Pettegrew JW, Abraham DJ. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 1989;37:1273–1281.
   PubMed Web of Science ®Google Scholar
• Khurana R, Coleman C, Ionescu-Zanetti C, Carter SA, Krishna V, Grover RK, et al. Mechanism of thioflavin T binding to amyloid fibrils. J Struct Biol 2005;151:229–238.
   PubMed Web of Science ®Google Scholar
• Kannan R, Raju M, Sharma KK. The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study. Amyloid 2014;21:103–109.
   PubMed Web of Science ®Google Scholar
• Hawe A, Sutter M, Jiskoot W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm Res 2008;25:1487–1499.
   PubMed Web of Science ®Google Scholar
• Hudson SA, Ecroyd H, Kee TW, Carver JA. The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds. FEBS J 2009;276:5960–5972.
   PubMed Web of Science ®Google Scholar
• Shen D, Coleman J, Chan E, Nicholson TP, Dai L, Sheppard PW, et al. Novel cell and tissue based assays for detecting misfolded and aggregated protein accumulation within aggresomes and inclusion bodies. Cell Biochem Biophys 2011;60:173–185.
   PubMed Web of Science ®Google Scholar
• Navarro S, Ventura S. Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. Biotechnol J 2014;9:1259–1266.
   PubMed Web of Science ®Google Scholar
• Makley LN, McMenimen KA, DeVree BT, Goldman JW, McGlasson BN, Rajagopal P, et al. Pharmacological chaperone for α-crystallin partially restores transparency in cataract models. Science 2015;350:674–677.
   PubMed Web of Science ®Google Scholar
• Zhao L, Chen XJ, Zhu J, Xi YB, Yang X, Hu LD, et al. Lanosterol reverses protein aggregation in cataracts. Nature 2015;523:607–611.
   PubMed Web of Science ®Google Scholar