Macromolecular and small-molecule modulation of intracellular Aβ 42 aggregation and associated toxicity

Biochemical Journal

Volumn 442, Issue 3, 2012, Pages 507-515

  Chakrabortee, Sohini ^a,e   Liu, Yun ^b   Zhang, Liao ^b   Matthews, Helena R ^a   Zhang, Hanrui ^c   Pan, Ni ^c   Cheng, Chun Ru ^d   Guan, Shu Hong ^d   Guo, De An ^d   Huang, Zebo ^c   Zheng, Yizhi ^b   Tunnacliffe, Alan ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b SHENZHEN UNIVERSITY   (China)

^c WUHAN UNIVERSITY   (China)

^d SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^e WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

Amyloid peptide (A ); Late embryogenesis abundant (LEA) protein; Polysaccharide; Protein aggregation; Traditional Chinese medicine

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; ATRACTYLENOLIDE 3; CHLOROGENIC ACID; ENHANCED GREEN FLUORESCENT PROTEIN; EUPHORBIA EXTRACT; EUPHORBIA FACTOR L2; EUPHORBIA FACTOR L3; GANODERIC ACID D; GANODERIC ACID DM; HELMINTH PROTEIN; ISOLIQUIRITIGENIN; LATE EMBRYOGENESIS ABUNDANT PROTEIN 1; PLANT EXTRACT; POLYSACCHARIDE; PROTEASOME; PROTOCATECHUIC ACID; STEROL DERIVATIVE; THIOFLAVINE; UNCLASSIFIED DRUG;

ACHYRANTHES BIDENTATA; ADENOPHORA TETRAPHYLLA; ARTICLE; ASTRAGALUS MEMBRANACEUS; CELL DEATH; CONCENTRATION RESPONSE; CONTROLLED STUDY; CUSCUTA CHINENSIS; CYTOTOXICITY; DRUG PURIFICATION; DRUG SCREENING; EMBRYO; EMBRYO CELL; EUPHORBIA; FALLOPIA MULTIFLORA; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; KIDNEY CELL; MEDICINAL PLANT; PORIA COCOS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; RHUBARB; RUBIA CORDIFOLIA; SALVIA MILTIORRHIZA; SCHISANDRA CHINENSIS; VISCUM COLORATUM;

AMYLOID BETA-PEPTIDES; CELLS, CULTURED; GREEN FLUORESCENT PROTEINS; HUMANS; MACROMOLECULAR SUBSTANCES; MEMBRANE GLYCOPROTEINS; PEPTIDE FRAGMENTS; TRANSFECTION;

APHELENCHUS AVENAE; FUNGI; MAMMALIA;

EID: 84863274677     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111661     Document Type: Article

References (48)

1. LaFerla, F. M., Green, K. N. and Oddo, S. (2007) Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci. 8, 499-509
2. Hardy, J. and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388
3. Braak, H. and Braak, E. (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259
4. 42 accumulation in human brain. Am. J. Pathol. 156, 15-20
5. Gouras, G. K., Tampellini, D., Takahashi, R. H. and Capetillo-Zarate, E. (2010) Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol. 119, 523-541
6. Bayer, T. A. and Wirths, O. (2010) Intracellular accumulation of amyloid-β - a predictor for synaptic dysfunction and neuron loss in Alzheimer's disease. Front Aging Neurosci. 2, 8
7. Chakrabortee, S., Boschetti, C., Walton, L. J., Sarkar, S., Rubinsztein, D. C. and Tunnacliffe, A. (2007) Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function. Proc. Natl. Acad. Sci. U.S.A. 104, 18073-18078 (Pubitemid 350210822)
8. Liu, Y., Chakrabortee, S., Li, R. H., Zheng, Y. Z. and Tunnacliffe, A. (2011) Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation. FEBS Lett. 585, 630-634
9. Chakrabortee, S., Meersman, F., Kaminski Schierle, G. S., Bertoncini, C. W., McGee, B., Kaminski, C. F. and Tunnacliffe, A. (2010) Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. Proc. Natl. Acad. Sci. U.S.A. 107, 16084-16089
10. Tunnacliffe, A., Hincha, D. K., Leprince, O. and Macherel, D. (2010) LEA proteins: versatility of form and function. In Dormancy and Resistance in Harsh Environments (Lubzens, E., Cerda, J. and Clark, M. S., eds), pp. 91-108, Springer, Berlin
11. Shih, M., Hoekstra, F. and Hsing, Y. (2008) Late embryogenesis abundant proteins. Adv. Bot. Res. 48, 211-255
12. Goyal, K., Walton, L. J. and Tunnacliffe, A. (2005) LEA proteins prevent protein aggregation due to water stress. Biochem. J. 388, 151-157 (Pubitemid 40732942)
13. Chakrabortee, S., Tripathi, R., Watson, M., Kaminski Schierle, G. S., Kurniawan, D. P., Kaminski, C. F., Wise, M. J. and Tunnacliffe, A. (2012) Intrinsically disordered proteins as molecular shields. Mol. Biosyst. 8, 210-219
14. 42 aggregation using peptides selected from combinatorial libraries. J. Pept. Sci. 15, 499-503
15. Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A. P. and Rubinsztein, D. C. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 11, 1137-1151 (Pubitemid 34521094)
16. Huang, Z. B., Liu, Y. D., Paulsen, B. S. and Klaveness, D. (1998) Studies on polysaccharides from three edible species of Nostoc (Cyanobacteria) with different colony morphologies: comparison of monosaccharide compositions and viscosities of polysaccharides from field colonies and suspension cultures. J. Phycol. 34, 962-968 (Pubitemid 29032832)
17. Staub, A. M. (1965) Removal of proteins. Sevag method. Methods Carbohydr. Chem. 5, 5-6
18. Cheng, C. R., Yue, Q. X., Wu, Z. Y., Song, X. Y., Tao, S. J., Wu, X. H., Xu, P. P., Liu, X., Guan, S. H. and Guo, D. A. (2010) Cytotoxic triterpenoids from Ganoderma lucidum. Phytochemistry 71, 1579-1585
19. Lee, L. L., Ha, H., Chang, Y. T. and DeLisa, M. P. (2009) Discovery of amyloid-β aggregation inhibitors using an engineered assay for intracellular protein folding and solubility. Protein Sci. 18, 277-286
20. Shen, D., Coleman, J., Chan, E., Nicholson, T. P., Dai, L. J., Sheppard, P. W. and Patton, W. F. (2011) Novel cell- and tissue-based assays for detecting misfolded and aggregated protein accumulation within aggresomes and inclusion bodies. Cell Biochem. Biophys. 60, 173-185
21. Lee, J. W., Lee, Y. K., Ban, J. O., Ha, T. Y., Yun, Y. P., Han, S. B., Oh, K. W. and Hong, J. T. (2009) Green tea (-)-epigallocatechin-3-gallate inhibits β-amyloid-induced cognitive dysfunction through modification of secretase activity via inhibition of ERK and NF-κB pathways in mice. J. Nutr. 139, 1987-1993
22. Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A. and Wanker, E. E. (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat. Struct. Mol. Biol. 15, 558-566 (Pubitemid 351799141)
23. Kim, W., Kim, Y., Min, J., Kim, D. J., Chang, Y. T. and Hecht, M. H. (2006) A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem. Biol. 1, 461-469
24. Fonte, V., Kapulkin, V., Taft, A., Fluet, A., Friedman, D. and Link, C. D. (2002) Interaction of intracellular β amyloid peptide with chaperone proteins. Proc. Natl. Acad. Sci. U.S.A. 99, 9439-9444 (Pubitemid 34764632)
25. Evans, C. G., Wisen, S. and Gestwicki, J. E. (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J. Biol. Chem. 281, 33182-33191 (Pubitemid 46036699)
26. Kumar, P., Ambasta, R. K., Veereshwarayya, V., Rosen, K. M., Kosik, K. S., Band, H., Mestril, R., Patterson, C. and Querfurth, H. W. (2007) CHIP and HSPs interact with β-APP in a proteasome-dependent manner and influence Aβ metabolism. Hum. Mol. Genet. 16, 848-864 (Pubitemid 47061630)
27. Bjorkdahl, C., Sjogren, M. J., Zhou, X., Concha, H., Avila, J., Winblad, B. and Pei, J. J. (2008) Small heat shock proteins Hsp27 or αB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments. J. Neurosci. Res. 86, 1343-1352 (Pubitemid 351571908)
28. Dehle, F. C., Ecroyd, H., Musgrave, I. F. and Carver, J. A. (2010) αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide. Cell Stress Chaperones 15, 1013-1026
29. Goyal, K., Tisi, L., Basran, A., Browne, J., Burnell, A., Zurdo, J. and Tunnacliffe, A. (2003) Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 278, 12977-12984 (Pubitemid 36800064)
30. Howes, M. J. and Houghton, P. J. (2003) Plants used in Chinese and Indian traditional medicine for improvement of memory and cognitive function. Pharmacol. Biochem. Behav. 75, 513-527
31. Carter, M. D., Simms, G. A. and Weaver, D. F. (2010) The development of new therapeutics for Alzheimer's disease. Clin. Pharmacol. Ther. 88, 475-486
32. da Rocha, M. D., Viegas, F. P., Campos, H. C., Nicastro, P. C., Fossaluzza, P. C., Fraga, C. A., Barreiro, E. J. and Viegas, Jr, C. (2011) The role of natural products in the discovery of new drug candidates for the treatment of neurodegenerative disorders II: Alzheimer's disease. CNS Neurol. Disord. Drug Targets 10, 251-270
33. Zhu, H., Yu, J. and Kindy, M. S. (2001) Inhibition of amyloidosis using low-molecular-weight heparins. Mol. Med. 7, 517-522 (Pubitemid 33701957)
34. Yu, M. S., Leung, S. K. Y., Lai, S. W., Che, C. M., Zee, S. Y., So, K. F., Yuen, W. H. and Chang, R. C. C. (2005) Neuroprotective effects of anti-aging oriental medicine Lycium barbarumagainst β-amyloid peptide neurotoxicity. Exp. Gerontol. 40, 716-727
35. Khodagholi, F., Eftekharzadeh, B., Maghsoudi, N. and Rezaei, P. F. (2010) Chitosan prevents oxidative stress-induced amyloid β formation and cytotoxicity in NT2 neurons: involvement of transcription factors Nrf2 and NF-κB. Mol. Cell. Biochem. 337, 39-51
36. Chitra, V. and Pavan Kumar, K. (2009) Neuroprotective studies of Rubia cordifolia Linn. on β-amyloid induced cognitive dysfunction in mice. Int. J. PharmTech. Res. 1, 1000-1009
37. Shiao, M. S. (2003) Natural products of the medicinal fungus Ganoderma lucidum: occurrence, biological activities, and pharmacological functions. Chem. Rec. 3, 172-180
38. Sanodiya, B. S., Thakur, G. S., Baghel, R. K., Prasad, G. and Bisen, P. S. (2009) Ganoderma lucidum: a potent pharmacological macrofungus. Curr. Pharm. Biotechnol. 10, 717-742
39. Weng, C. J. and Yen, G. C. (2010) The in vitroand in vivo experimental evidences disclose the chemopreventive effects of Ganoderma lucidumon cancer invasion and metastasis. Clin. Exp. Metastasis 27, 361-369
40. Cai, H., Wang, F. S., Yang, J. S. and Zhang, Y. M. (1995) Structure of ganoderic acid DM, a new triterpenoid from the fruiting body of Ganoderma lucidum. Chin. Chem. Lett. 6, 1051-1052 (Pubitemid 126012939)
41. Lai, C. S. W., Yu, M. S., Yuen, W. H., So, K. F., Zee, S. Y. and Chang, R. C. C. (2008) Antagonizing β-amyloid peptide neurotoxicity of the anti-aging fungus Ganoderma lucidum. Brain Res. 1190, 215-224
42. Liu, J., Shiono, J., Shimizu, K., Kukita, A., Kukita, T. and Kondo, R. (2009) Ganoderic acid DM: anti-androgenic osteoclastogenesis inhibitor. Bioorg. Med. Chem. Lett. 19, 2154-2157
43. Marambaud, P., Zhao, H. and Davies, P. (2005) Resveratrol promotes clearance of Alzheimer's disease amyloid-β peptides. J. Biol. Chem. 280, 37377-37382 (Pubitemid 41642343)
44. Vingtdeux, V., Giliberto, L., Zhao, H. T., Chandakkar, P., Wu, Q. L., Simon, J. E., Janle, E. M., Lobo, J., Ferruzzi, M. G., Davies, P. and Marambaud, P. (2010) AMP-activated protein kinase signaling activation by resveratrol modulates amyloid-β peptide metabolism. J. Biol. Chem. 285, 9100-9113
45. Albani, D., Polito, L., Batelli, S., De Mauro, S., Fracasso, C., Martelli, G., Colombo, L., Manzoni, C., Salmona, M., Caccia, S. et al. (2009) The SIRT1 activator resveratrol protects SK-N-BE cells from oxidative stress and against toxicity caused by α-synuclein or amyloid-β (1-42) peptide. J. Neurochem. 110, 1445-1456
46. Feng, Y., Wang, X. P., Yang, S. G., Wang, Y. J., Zhang, X., Du, X. T., Sun, X. X., Zhao, M., Huang, L. and Liu, R. T. (2009) Resveratrol inhibits β-amyloid oligomeric cytotoxicity but does not prevent oligomer formation. Neurotoxicology 30, 986-995
47. Lopez Salon, M., Pasquini, L., Besio Moreno, M., Pasquini, J. M. and Soto, E. (2003) Relationship between β-amyloid degradation and the 26S proteasome in neural cells. Exp. Neurol. 180, 131-143 (Pubitemid 36398168)
48. 1-42 clearance. Hum. Mol. Genet. 18, 3206-3216