The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Clusterin Is an ATP−Independent Chaperone with Very Broad Substrate Specificity that Stabilizes Stressed Proteins in a Folding-Competent State
Abstract
We recently reported that the ubiquitous, secreted protein clusterin has chaperone activity in vitro [Humphreys et al. (1999) J. Biol. Chem. 274, 6875-6881]. In this study, we demonstrate that clusterin (i) inhibits stress-induced precipitation of a very broad range of structurally divergent protein substrates, (ii) binds irreversibly via an ATP-independent mechanism to stressed proteins to form solubilized high molecular weight complexes, (iii) lacks detectable ATPase activity, (iv) when acting alone, does not effect refolding of stressed proteins in vitro, and (v) stabilizes stressed proteins in a state competent for refolding by heat shock protein 70 (HSP70). Furthermore, we show that, at physiological levels, clusterin inhibits stress-induced precipitation of proteins in undiluted human serum. Clusterin represents the first identified secreted mammalian chaperone. However, reports from others suggest that, at least under stress conditions, clusterin may be retained within cells to exert a protective effect. Regardless of the topological site(s) of action, the demonstration that clusterin can stabilize stressed proteins in a refolding-competent state suggests that, during stresses, the action of clusterin may inhibit rapid and irreversible protein precipitation and produce a reservoir of inactive but stabilized molecules from which other refolding chaperones can subsequently salvage functional proteins.
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Cites
Ehrnsperger, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.221 · Cited by 754
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-citationUrban, J., Parczyk, K., Leutz, A., Kayne, M., & Kondor-Koch, C. (1987) · The Journal of cell biology · doi:10.1083/jcb.105.6.2735 · Cited by 201
Stress-induced transcription of the clusterin/apoJ gene
MICHEL, D., CHATELAIN, G., NORTH, S., & BRUN, G. (1997) · Biochemical Journal · doi:10.1042/bj3280045 · Cited by 194
Viard, I., Wehrli, P., Jornot, L., Bullani, R., Vechietti, J.-L., French, L. E., Schifferli, J. A., & Tschopp, J. (1999) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.1999.00531.x · Cited by 181
Human seminal clusterin (SP-40,40). Isolation and characterization.
O’Bryan, M. K., Baker, H. W. G., Saunders, J. R., Kirszbaum, L., Walker, I. D., Hudson, P. J., Liu, D. Y., Glew, M. D., D'Apice, A. J. F., & Murphy, B. F. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114594 · Cited by 138
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-citationIntracellular processing of apolipoprotein J precursor to the mature heterodimer.
Burkey, B. F., deSilva, H., & Harmony, J. A. K. (1991) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42000-0 · Cited by 92
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Multiple Involvement of Clusterin in Chicken Ovarian Follicle Development
Mahon, M. G., Lindstedt, K. A., Hermann, M., Nimpf, J., & Schneider, W. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4036 · Cited by 72
Cited by
Schöttler, S., Becker, G., Winzen, S., Steinbach, T., Mohr, K., Landfester, K., Mailänder, V., & Wurm, F. R. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2015.330 · Cited by 1,272
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
DeMattos, 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
Expression of Novel Alzheimer’s Disease Risk Genes in Control and Alzheimer’s Disease Brains
Karch, C. M., Jeng, A. T., Nowotny, P., Cady, J., Cruchaga, C., & Goate, A. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050976 · Cited by 328
Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., & Wilson, M. R. (2007) · The FASEB Journal · doi:10.1096/fj.06-7986com · Cited by 324
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Metadata
- Authors
- Poon, S., Easterbrook-Smith, S. B., Rybchyn, M. S., Carver, J. A., & Wilson, M. R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-12-01
- Volume
- 39
- Issue
- 51
- Pages
- 15953-15960
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1976945780
- Cited by
- 252
- References
- 10
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- closed
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- Poon, S., Easterbrook-Smith, S. B., Rybchyn, M. S., Carver, J. A., & Wilson, M. R. (2000). Clusterin Is an ATP−Independent Chaperone with Very Broad Substrate Specificity that Stabilizes Stressed Proteins in a Folding-Competent State. Biochemistry. https://doi.org/10.1021/bi002189x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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