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Fibroblast cultures from healthy centenarians have an active proteasome
Abstract
Healthy centenarians represent the best example of successful ageing. Various studies have shown that centenarians have escaped the major age-associated diseases, they have several well-conserved immune parameters and at least one gene allele has been identified and linked with their increased longevity. During ageing there is an accumulation of oxidised proteins, a phenomenon that has been related to an impaired function of the 20S proteasome in aged cells. We have, therefore, analysed the expression and the proteolytic activity of the proteasome in centenarian cells. Four fibroblast cultures derived from healthy centenarians were studied and compared with cultures derived from adult donors of different ages. Analysis of several proteasome subunits RNA expression levels, determination of one peptidase activity and identification of oxidised proteins in these samples revealed that centenarian cultures have a functional proteasome. In addition, it was found that the centenarian cultures exhibit characteristics similar to the younger rather than the older control donors derived cultures in all three assays. These data indicate that centenarian cells may be different from elderly donors cells, thus opening up new dimensions for the identification and characterisation of factors that are linked with longevity.
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“Cultured fibroblasts from healthy centenarians have a more active proteasome (Chondrogianni et al., 2000)”
From Protein Homeostasis and Aging: the importance of exquisite quality control (2011) · cites this paper as Chondrogianni et al., 2000
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Cites
STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES
Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438
Degradation of oxidized proteins in mammalian cells
Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835
γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
Gaczynska, M. E., Rock, K. L., & Goldberg, A. L. (1993) · Nature · doi:10.1038/365264a0 · Cited by 571
Cristofalo, V. J., Allen, R. G., Pignolo, R. J., Martin, B. G., & Beck, J. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10614 · Cited by 554
The immunology of exceptional individuals: the lesson of centenarians
Franceschi, C., Monti, D., Sansoni, P., & Cossarizza, A. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80064-6 · Cited by 535
Self-citationGaczynska, M., Rock, K. L., Spies, T., & Goldberg, A. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.20.9213 · Cited by 312
Conconi, M., Szweda, L. I., Levine, R. L., Stadtman, E. R., & Friguet, B. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0303 · Cited by 213
Self-citationPetropoulos, I., Conconi, M., Wang, X., Hoenel, B., Brégégère, F. M., Milner, Y., & Friguet, B. (2000) · The Journals of Gerontology Series A · doi:10.1093/gerona/55.5.b220 · Cited by 212
Self-citationAhn, J. Y., Tanahashi, N., Akiyama, K., Hisamatsu, H., Noda, C., Tanaka, K., Chung, C. H., Shibmara, N., Willy, P. J., Mott, J. D., et al. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00492-r · Cited by 198
Protein Degradation by the Proteasome and Its Implications in Aging
Friguet, B., Bulteau, A., Chondrogianni, N., Conconi, M., & Petropoulos, I. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06643.x · Cited by 172
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Mishto, M., Santoro, A., Bellavista, E., Sessions, R. B., Textoris‐Taube, K., Piaz, F. D., Carrard, G., Forti, K., Salvioli, S., Friguet, B., et al. (2006) · Biological Chemistry · doi:10.1515/bc.2006.056 · Cited by 37
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Self-citationFranceschi, C., Salvioli, S., Capri, M., Tieri, P., Loroni, J., Barbi, C., Invidia, L., Altilia, S., Santoro, A., Pirazzini, C., et al. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208783413266 · Cited by 9
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Zironi, I., Gaibani, P., Remondini, D., Salvioli, S., Altilia, S., Pierini, M., Aicardi, G., Verondini, E., Milanesi, L., Bersani, F., et al. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.09.004 · Cited by 8
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Gutiérrez‐Merino, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813846 · Cited by 4
Burov, A. V., Funikov, S. Y., Astakhova, T. M., Teterina, E. V., Nebogatikov, V. O., Erokhov, P. A., Ustyugov, A. A., Карпов, В. Л., & Morozov, A. V. (2023) · Molecular Biology · doi:10.1134/s0026893323050035 · Cited by 2
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Gonos, E. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.114
Self-citationFriguet, B. (2008) · Experimental Dermatology · doi:10.1111/j.1600-0625.2007.00665_4.x
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Goutas, A., & Trachana, V. (2023) · Advances in biogerontology · doi:10.1016/bs.abger.2023.07.002
Burov, A. V., Funikov, S. Y., Astakhova, T. M., Teterina, E. V., Nebogatikov, V. O., Erokhov, P. A., Ustyugov, A. A., Карпов, В. Л., & Morozov, A. V. (2023) · Molecular Biology · doi:10.31857/s0026898423050038
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Osiewacz, H. D. (2026) · The mycota · doi:10.1007/978-3-032-15548-1_4
Martin, I. (2008) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/pgcp-c821
Links between Aging and Proteostasis Decline in Saccharomyces cerevisiae
Andersson, V. (2014) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Metadata
- Authors
- Chondrogianni, N., Petropoulos, I., Franceschi, C., Friguet, B., & Gonos, E. S.
- Affiliations
- National Hellenic Research Foundation (GR)
- Université Paris Diderot (FR)
- University of Bologna (IT)
- Corresponding author
- Gonos, E.S
- Venue
- Experimental Gerontology
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 35
- Issue
- 6-7
- Pages
- 721-728
- ISSN
- 0531-5565 (ISSN-L)
- OpenAlex
- W2143588591
- Cited by
- 200
- References
- 22
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 9 · 2022: 6 · 2021: 9 · 2020: 8 · 2019: 11 · 2018: 13 · 2017: 14 · 2016: 12 · 2015: 4 · 2014: 13 · 2013: 7 · 2012: 4
- FWCI
- 2.60
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Gerontology (publishedVersion)
- PubMed (publishedVersion)
- National Hellenic Research Foundation Helios Repository (National Hellenic Research Foundation) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- centenarians, proteasome, 20S proteasome, fibroblasts, successful aging, longevity, protein oxidation, proteolytic activity
- MeSH terms
- Adult, Aged, Aged, 80 and over, Aging, Child, Cysteine Endopeptidases, Female, Fibroblasts, Humans, Middle Aged, Multienzyme Complexes, Proteasome Endopeptidase Complex
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