The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins
Open accessAbstract
Clusterin is a highly conserved protein which is expressed at increased levels by many cell types in response to a broad variety of stress conditions. A genuine physiological function for clusterin has not yet been established. The results presented here demonstrate for the first time that clusterin has chaperone-like activity. At physiological concentrations, clusterin potently protected glutathione S-transferase and catalase from heat-induced precipitation and alpha-lactalbumin and bovine serum albumin from precipitation induced by reduction with dithiothreitol. Enzyme-linked immunosorbent assay data showed that clusterin bound preferentially to heat-stressed glutathione S-transferase and to dithiothreitol-treated bovine serum albumin and alpha-lactalbumin. Size exclusion chromatography and SDS-polyacrylamide gel electrophoresis analyses showed that clusterin formed high molecular weight complexes (HMW) with all four proteins tested. Small heat shock proteins (sHSP) also act in this way to prevent protein precipitation and protect cells from heat and other stresses. The stoichiometric subunit molar ratios of clusterin:stressed protein during formation of HMW complexes (which for the four proteins tested ranged from 1.0:1.3 to 1.0:11) is less than the reported ratios for sHSP-mediated formation of HMW complexes (1.0:1.0 or greater), indicating that clusterin is a very efficient chaperone. Our results suggest that clusterin may play a sHSP-like role in cytoprotection.
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Cites
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Cited by
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
Cholesterol in brain disease: Sometimes determinant and frequently implicated
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Clusterin: A forgotten player in Alzheimer's disease
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Molecular chaperones and proteostasis regulation during redox imbalance
Niforou, K., Cheimonidou, C., & Trougakos, I. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.017 · Cited by 250
Metadata
- Authors
- Humphreys, D. T., Carver, J. A., Easterbrook-Smith, S. B., & Wilson, M. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-03
- Volume
- 274
- Issue
- 11
- Pages
- 6875-6881
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2117170342
- Cited by
- 455
- References
- 35
- FWCI
- 6.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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