The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Impact of ageing on proteasome structure and function in human lymphocytes
Abstract
Key actors of the immune response, lymphocytes exhibit functional deficits with advancing age. For instance, the age-related decline in lymphocyte proliferation may be related to alteration in the degradation of crucial proteins such as cell-cycle regulators. Degradation of these proteins is mediated by the ubiquitin-26S proteasome system. The proteasome is also the major "housekeeping" proteolytic complex responsible for eliminating intracellular damaged proteins. To investigate the occurrence of proteasome structural and functional age-related alterations, 26S proteasome was purified from peripheral blood lymphocytes of 20-63-year-old donors. Changes in peptidase activity were measured and modifications in the proteasome particle structure were analysed using bi-dimensional electrophoresis. We found the age-related decline of 26S proteasome-specific activity to be associated with an increased yield of post-translational modifications of proteasome subunits, while proteasome content and subunit composition were unchanged. In particular, some catalytic and assembly subunits of the 20S proteasome were preferentially modified with age. Western blotting of proteasome subunits resolved by bi-dimensional electrophoresis showed some of these modified subunits to be glycated, conjugated with a lipid peroxidation product and/or ubiquitinated. In conclusion, it is suggested that structural alterations of proteasome subunits may contribute to the observed decline of proteasome activity with age and could play a major role in immune senescence.
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“Many reports have shown different degrees of decrease in the activity of the proteasome with age in several tissues, although, in contrast to the lysosomal system, the decline in activity with age does not seem to be universal (Carrard et al., 2003; Ferrington et al., 2005; Keller et al., 2000 b; Shibatani et al., 1996).”
From Protein Homeostasis and Aging: the importance of exquisite quality control (2011) · cites this paper as Carrard et al., 2003
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Cites
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Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
Gene expression profile of aging and its retardation by caloric restriction
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Antigen processing by the proteasome
Kloetzel, P. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056572 · Cited by 638
Mitotic Misregulation and Human Aging
Ly, D. H., Lockhart, D. J., Lerner, R. A., & Schultz, P. G. (2000) · Science · doi:10.1126/science.287.5462.2486 · Cited by 599
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Oxidative Modification and Inactivation of the Proteasome during Coronary Occlusion/Reperfusion
Bulteau, A., Lundberg, K. C., Humphries, K. M., Sadek, H. A., Szweda, P. A., Friguet, B., & Szweda, L. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100142200 · Cited by 354
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Sorted by citations
Protein Homeostasis and Aging: the importance of exquisite quality control
Koga, H., Kaushik, S., & Cuervo, A. M. (2011) · Ageing research reviews · doi:10.1016/j.arr.2010.02.001 · Cited by 476
Regulation of proteasome activity in health and disease
Schmidt, M., & Finley, D. J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.08.012 · Cited by 480
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 401
The Mechanistic Links Between Proteasome Activity, Aging and Agerelated Diseases
Sáez, I., & Vı́lchez, D. (2014) · Current Genomics · doi:10.2174/138920291501140306113344 · Cited by 331
“A decline in proteasome function during aging and senescence has been observed in several mammalian tissues and cells such as human skin, epidermal cells, fibroblasts and lymphocytes [85-88], bovine eye lens [89] and rat liver, lung, heart, kidney, spinal cord, hippocampus, cerebral cortex and muscle tissues [90-95].”
BackgroundOxidative stress and lipotoxicity
Hauck, A. K., & Bernlohr, D. (2016) · Journal of Lipid Research · doi:10.1194/jlr.r066597 · Cited by 299
Metadata
- Authors
- Carrard, G., Dieu, M., Raes, M., Toussaint, O., & Friguet, B.
- Affiliations
- Université Paris Diderot (FR)
- University of Namur (BE)
- Corresponding author
- Friguet, Bertrand
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 35
- Issue
- 5
- Pages
- 728-739
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W1968569587
- Cited by
- 131
- References
- 42
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 6 · 2015: 8 · 2014: 8 · 2013: 4 · 2012: 7
- FWCI
- 3.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Libraries (submittedVersion)
- Repository of the University of Namur (submittedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- aging, 26S proteasome, proteasome structure, proteasome activity, lymphocytes, immunosenescence, post-translational modification, proteasome subunits, glycation, lipid peroxidation, ubiquitination, proteolytic activity, protein degradation, cell cycle regulators
- MeSH terms
- Adult, Aging, Cysteine Endopeptidases, Electrophoresis, Humans, Lymphocytes, Middle Aged, Multienzyme Complexes, Peptide Hydrolases, Phosphorylation, Ubiquitins, Blotting, Western, Oxidative Stress, Spectrometry, Mass, Electrospray Ionization, Proteasome Endopeptidase Complex
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