The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
Abstract
Clusterin is an extracellular chaperone present in all disease‐associated extracellular amyloid deposits, but its roles in amyloid formation and protein deposition in vivo are poorly understood. The current study initially aimed to characterize the effects of clusterin on amyloid formation in vitro by a panel of eight protein substrates. Two of the substrates (Alzheimer's beta peptide and a PI3‐SH3 domain) were then used in further experiments to examine the effects of clusterin on amyloid cytotoxicity and to probe the mechanism of clusterin action. We show that clusterin exerts potent effects on amyloid formation, the nature and extent of which vary greatly with the clusterin: substrate ratio, and provide evidence that these effects are exerted via interactions with prefibrillar species that share common structural features. Proamyloido‐genic effects of clusterin appear to be restricted to conditions in which the substrate protein is present at a very large molar excess;under these same conditions, clusterin coincorporates with substrate protein into insoluble aggregates. However, when clusterin is present at much higher but still substoichiometric levels (e.g. , a molar ratio of clusterin:substrate = 1:10), it potently inhibits amyloid formation and provides substantial cytoprotection. These findings suggest that clus‐terin is an important element in the control of extracellular protein misfolding.—Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., Wilson, M. R. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 21, 2312–2322 (2007)
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Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Self-citationInherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Self-citationHarper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 991
ApoE and Clusterin Cooperatively Suppress Aβ Levels and Deposition
DeMattos, R. B., Cirrito, J. R., Parsadanian, M., May, P. C., O'Dell, M. A., Taylor, J. W., Harmony, J. A. K., Aronow, B. J., Bales, K. R., Paul, S. M., et al. (2004) · Neuron · doi:10.1016/s0896-6273(03)00850-x · Cited by 459
Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins
Humphreys, D. T., Carver, J. A., Easterbrook-Smith, S. B., & Wilson, M. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.6875 · Cited by 455
Self-citationDeMattos, R. B., O'dell, M. A., Parsadanian, M., Taylor, J. W., Harmony, J. A. K., Bales, K. R., Paul, S. M., Aronow, B. J., & Holtzman, D. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162228299 · Cited by 359
Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352
Lichtenfels, R., Biddison, W. E., Schulz, H., Vogt, A. B., & Martin, R. (1994) · Journal of Immunological Methods · doi:10.1016/0022-1759(94)90110-4 · Cited by 263
Apolipoprotein J (clusterin) and Alzheimer's disease
Calero, M., Rostagno, A., Matsubara, E., Zlokovic, B., Frangione, B., & Ghiso, J. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20000815)50:4<305::aid-jemt10>3.0.co;2-l · Cited by 256
Poon, S., Easterbrook-Smith, S. B., Rybchyn, M. S., Carver, J. A., & Wilson, M. R. (2000) · Biochemistry · doi:10.1021/bi002189x · Cited by 252
Self-citationChaperone‐like activity of synucleins
Souza, J. M., Giasson, B. I., Lee, V. M.-Y., & Ischiropoulos, H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01563-5 · Cited by 221
α 2 -macroglobulin associates with β-amyloid peptide and prevents fibril formation
Hughes, S. R., Khorkova, O., Goyal, S., Knaeblein, J., Heroux, J., Riedel, N. G., & Sahasrabudhe, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3275 · Cited by 216
Apolipoprotein J and Alzheimer's amyloid β solubility
MATSUBARA, E., SOTO, C., GOVERNALE, S., FRANGIONE, B., & GHISO, J. (1996) · Biochemical Journal · doi:10.1042/bj3160671 · Cited by 190
Exploring amyloid formation by a de novo design
Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306786101 · Cited by 164
Self-citationQuality control of protein folding in extracellular space
Yerbury, J. J., Stewart, E. M., Wyatt, A. R., & Wilson, M. R. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400586 · Cited by 138
Self-citationKlug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
Clusterin (Apo J) Protects Against In Vitro Amyloid‐β(1–40) Neurotoxicity
Boggs, L. N., Fuson, K. S., Baez, M., Churgay, L. M., McClure, D. B., Becker, G., & May, P. C. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031324.x · Cited by 108
Zenkel, M., Kruse, F. E., nemann, A. G. J., Naumann, G. O. H., & Schlo¨tzer-Schrehardt, U. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-1580 · Cited by 108
Mildly Acidic pH Activates the Extracellular Molecular Chaperone Clusterin
Poon, S., Rybchyn, M. S., Easterbrook‐Smith, S. B., Carver, J. A., Pankhurst, G. J., & Wilson, M. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204855200 · Cited by 104
Self-citationMaat–Schieman, M. L. C., van Duinen, S. G., Bornebroek, M., Haan, J., & Roos, R. A. C. (1996) · Brain Pathology · doi:10.1111/j.1750-3639.1996.tb00794.x · Cited by 100
Clusterin binds by a multivalent mechanism to the Fc and Fab regions of IgG
Wilson, M. R., & Easterbrook‐Smith, S. B. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90062-i · Cited by 100
Self-citationKumita, J. R., Poon, S., Caddy, G. L., Hagan, C. L., Dumoulin, M., Yerbury, J. J., Stewart, E. M., Robinson, C. V., Wilson, M. R., & Dobson, C. M. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.095 · Cited by 85
Self-citationKida, E., Choi-Miura, N.-H., & Wisniewski, K. E. (1995) · Brain Research · doi:10.1016/0006-8993(95)00482-6 · Cited by 79
Evidence That Clusterin Has Discrete Chaperone and Ligand Binding Sites
Lakins, J. N., Poon, S., Easterbrook‐Smith, S. B., Carver, J. A., Tenniswood, M., & Wilson, M. R. (2001) · Biochemistry · doi:10.1021/bi0157666 · Cited by 73
Self-citation(1993) · PubMed Central · Cited by 68
Suppression of apolipoprotein C‐II amyloid formation by the extracellular chaperone, clusterin
Hatters, D. M., Wilson, M. R., Easterbrook‐Smith, S. B., & Howlett, G. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02957.x · Cited by 58
Self-citationClusterin is Present in Drusen in Age-related Macular Degeneration
Sakaguchi, H., Miyagi, M., Shadrach, K. G., Rayborn, M. E., Crabb, J. W., & Hollyfield, J. G. (2002) · Experimental Eye Research · doi:10.1006/exer.2002.1186 · Cited by 54
Clusterin solubility and aggregation in Creutzfeldt-Jakob disease
Freixes, M., Puig, B., Rodr�guez, A. C., Torrejón-Escribano, B., Blanco, R., & Ferrer, I. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0891-6 · Cited by 50
Clusterin Prevents Aggregation of Neuropeptide 106-126 in Vitro
McHattie, S., & Edington, N. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0781 · Cited by 43
Nishida, K., Quantock, A. J., Dota, A., Choi-Miura, N.-H., & Kinoshita, S. (1999) · British Journal of Ophthalmology · doi:10.1136/bjo.83.10.1178 · Cited by 33
Clusterin (SGP‐2) Induction in Rat Astroglial Cells Exposed to Prion Protein Fragment 106–126
Chiesa, R., Angeretti, N., Lucca, E., Salmona, M., Tagliavini, F., Bugiani, O., & Forloni, G. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01244.x · Cited by 30
Ghiso, J. A., Plant, G. T., Révész, T., Wısnıewskı, T., & Frangione, B. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)00274-r · Cited by 29
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Griciuc, A., Serrano-Pozo, A., Parrado, A. R., Lesinski, A. N., Asselin, C. N., Mullin, K., Hooli, B., Choi, S. H., Hyman, B. T., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.014 · Cited by 1,004
Cerebral amyloid angiopathy and Alzheimer disease — one peptide, two pathways
Greenberg, S. M., Bacskai, B. J., Hernandez-Guillamon, M., Pruzin, J., Sperling, R., & van Veluw, S. J. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-019-0281-2 · Cited by 947
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584
Thambisetty, M., Simmons, A., Velayudhan, L., Hye, A., Campbell, J., Zhang, Y., Wahlund, L.-O., Westman, E., Kinsey, A., Güntert, A., et al. (2010) · Archives of General Psychiatry · doi:10.1001/archgenpsychiatry.2010.78 · Cited by 405
Clusterin in Alzheimer’s Disease: Mechanisms, Genetics, and Lessons From Other Pathologies
Foster, E. M., Dangla-Valls, A., Lovestone, S., Ribe, E. M., & Buckley, N. J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00164 · Cited by 381
Metadata
- Authors
- Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., & Wilson, M. R.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2007-04-05
- Volume
- 21
- Issue
- 10
- Pages
- 2312-2322
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1964998879
- Cited by
- 324
- References
- 34
- FWCI
- 6.64
- Type
- journal article
- Language
- en
- Open access
- closed
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