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
Citations
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“…activity declines with age in animal cells, including human soma cells such as epidermal cells, fibroblasts and lymphocytes (Bulteau et al. 2000; Carrard et al. 2003; Chondrogianni et al. 2003) and rat organ cells like lung, liver, heart, kidney, spinal cord, hippocampus, cerebral cortex,…”
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“The organelle that is responsible for removing proteins with oxidative damage is the proteasome and the activity of this organelle decreases with age in a number of tissues (Shibatani et al., 1996; Shang et al., 1997; Bulteau et al., 2000; Keller et al., 2000; Petropoulos et al., 2000; Louie et al., 2002; Carrard et a…”
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Étude du métabolisme des protéines carbamylées intracellulaires
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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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