The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Chaperones Hsp70 and Hsp40 Suppress Aggregate Formation and Apoptosis in Cultured Neuronal Cells Expressing Truncated Androgen Receptor Protein with Expanded Polyglutamine Tract
Open accessAbstract
Spinal and bulbar muscular atrophy (SBMA) is one of a group of human inherited neurodegenerative diseases caused by polyglutamine expansion. We have previously demonstrated that the SBMA gene product, the androgen receptor protein, is toxic and aggregates when truncated. Heat shock proteins function as molecular chaperones, which recognize and renaturate misfolded protein (aggregate). We thus assessed the effect of a variety of chaperones in a cultured neuronal cell model of SBMA. Overexpression of chaperones reduces aggregate formation and suppresses apoptosis in a cultured neuronal cell model of SBMA to differing degrees depending on the chaperones and their combinations. Combination of Hsp70 and Hsp40 was the most effective among the chaperones in reducing aggregate formation and providing cellular protection, reflecting that Hsp70 and Hsp40 act together in chaperoning mutant and disabled proteins. Although Hdj2/Hsdj chaperone has been previously reported to suppress expanded polyglutamine tract-formed aggregate, Hsdj/Hdj2 showed little effect in our system. These findings indicate that chaperones may be one of the key factors in the developing of CAG repeat disease and suggested that increasing expression level or enhancing the function of chaperones will provide an avenue for the treatment of CAG repeat disease.
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MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1
Orr, H. T., Chung, M.-Y., Banfi, S., Kwiatkowski, T. J., Servadio, A., Beaudet, A. L., McCall, A. E., Duvick, L. A., Ranum, L. P. W., & Zoghbi, H. Y. (1993) · Nature Genetics · doi:10.1038/ng0793-221 · Cited by 1,632
Cited by
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Hsp70 Reduces α-Synuclein Aggregation and Toxicity
Klucken, J., Shin, Y., Masliah, E., Hyman, B. T., & McLean, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400255200 · Cited by 508
17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Tanaka, F., Inukai, A., Doyu, M., & Sobue, G. (2005) · Nature Medicine · doi:10.1038/nm1298 · Cited by 395
Self-citationTorsinA and heat shock proteins act as molecular chaperones: suppression of α‐synuclein aggregation
McLean, P. J., Kawamata, H., Shariff, S., Hewett, J., Sharma, N., Ueda, K., Breakefield, X. O., & Hyman, B. T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01190.x · Cited by 324
Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., & Clark, J. B. (2001) · Neurochemical Research · doi:10.1023/a:1010955807739 · Cited by 263
Metadata
- Authors
- Kobayashi, Y., Kume, A., Li, M., Doyu, M., Hata, M., Ohtsuka, K., & Sobue, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-03
- Volume
- 275
- Issue
- 12
- Pages
- 8772-8778
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2002431899
- Cited by
- 316
- References
- 2
- FWCI
- 12.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kobayashi, Y., Kume, A., Li, M., Doyu, M., Hata, M., Ohtsuka, K., & Sobue, G. (2000). Chaperones Hsp70 and Hsp40 Suppress Aggregate Formation and Apoptosis in Cultured Neuronal Cells Expressing Truncated Androgen Receptor Protein with Expanded Polyglutamine Tract. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.12.8772
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