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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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InfluentialCellular environment facilitates protein accumulation in aged rat hippocampus
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“Friguet and colleagues showed an age-related increase of post-translational oxidative modifications (HNE and glycoxidaton adducts) of proteasome subunits and decreased peptidase activities in peripheral blood lymphocytes and in human lens cells (18, 21, 155).”
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Pickering, A. M., & Davies, K. J. A. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00006-7 · Cited by 173
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Self-citationHallmarks and detection techniques of cellular senescence and cellular ageing in immune cells
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“Proteasome activity declines progressively in aged mammalian cell (Carrard et al., 2003).”
BackgroundCatalytic site‐specific inhibition of the 20S proteasome by 4‐hydroxynonenal
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Self-citationA brain atlas of synapse protein lifetime across the mouse lifespan
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Chondrogianni, N., Voutetakis, K., Καπετάνου, Μ., Delitsikou, V., Papaevgeniou, N., Sakellari, M., Lefaki, M., Filippopoulou, K., & Gonos, E. S. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.12.003 · Cited by 115
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Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.031 · Cited by 94
“Proteasome activities have been reported to decline during aging in several human tissues including lens [290], lymphocytes [291,292], and epidermis [90,293,294].”
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“The hydrolytic inactivation appears to be an indirect effect of HNE-modified proteasomal a subunits and proteolytic inactive b subunits, since hardly any HNE was found to be attached to the enzymatic b subunits (32, 37, 95).”
Protein oxidation and degradation during aging: Role in skin aging and neurodegeneration
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“Previous studies have also shown an inactivation of the proteasome as a consequence of the oxidation of some of its subunits [29-31].”
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“whereas the makeup of 26S is unchanged (Carrard et al., 2003).”
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“glycation) Inefficiency in degradation of damaged proteins [12, 13]”
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“This would turn such proteins into the Achilles’ heel of the proteome in conditions where proteasomal function is significantly reduced, such as is reported for normal human ageing [22,23,24,25].”
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Self-citationCross-species Comparison of Proteome Turnover Kinetics
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“This correlation was somewhat unexpected in light of numerous studies indicating that faster protein turnover is generally beneficial for healthy aging (35-37).”
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“Moreover, protein oxidation was higher in OO when compared with YC group indicating that not only the advancing age, but also the ovariectomy increased protein damage.(40,41) OVX has caused an increase in GPx activity in YO and OO, when compared with YC and OC.”
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Self-citationAdvances in Proteasome Enhancement by Small Molecules
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“These age-related modifications mainly occur on the 20S subunits and to a lesser extent on the 19S subunits (19).”
Li, Y., Wang, Y., Shen, X., Hui, Y.-N., Han, J., Zhao, W., & Zhu, J. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.08.052 · Cited by 38
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“For example, studies have demonstrated a potential role for proteasome inhibition occurring as the result of increased levels of oxidized and/or aggregated proteins [27], increased oxidative modifications to the proteasome complexes [23,28 36] and deleterious changes in proteasome composition [25,29].”
BackgroundKabashi, E., Agar, J. N., Hong, Y. H., Taylor, D. M., Minotti, S., Figlewicz, D. A., & Durham, H. D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05317.x · Cited by 37
“The major post-translational modifications of 20S subunits that have been detected in aging/senescence along with decreased proteasomal activity are carbonylation, conjugation with a lipid peroxidation product, glycation, and ubiquitination (Bulteau et al. 2000; Keller et al. 2000; Carrard et al. 2003; Farout et al. 2…”
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“Proteasomal dysfunction is manifest through a reduction in the level of individual subunit levels, as well as the modification or substitution of proteasome subunits, proteasome disassembly, and proteasome inactivation [141–143].”
BackgroundRedox regulation of the proteasome in T lymphocytes during aging
Das, R., Ponnappan, S., & Ponnappan, U. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.020 · Cited by 36
“chymotrypsin-like activity to be most sensitive to age-related modifications is in line with our previously reported observation obtained with 26S proteasomes, as well as, data reported by Carrard et al, employing peripheral blood lymphocytes from human subjects [4,22].”
BackgroundResultTuning the proteasome to brighten the end of the journey
Mayor, T., Sharon, M., & Glickman, M. H. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00198.2016 · Cited by 32
“, rat liver, heart, and brain cortex) and human cell types (epidermal and lymphocytes) derived from older organisms (12, 13, 15, 43, 55).”
BackgroundProteostasis and ageing: insights from long‐lived mutant mice
Sands, W. A., Page, M. M., & Selman, C. (2017) · The Journal of Physiology · doi:10.1113/jp274334 · Cited by 32
“For example, activity of the 26S proteasome declines in human peripheral blood lymphocytes with age, and this was correlated with an increased number of post-translational modifications on proteasomal subunits (Carrard et al. 2003).”
BackgroundProteomic map of peripheral blood mononuclear cells
Vergara, D., Chiriacò, F., Acierno, R., et al. (2008) · PROTEOMICS · doi:10.1002/pmic.200700726 · Cited by 30
“An age-related decrease in proteasome activity has been observed in human lymphocytes [40] and a reduction in 20S proteasome activity has recently been shown in peripheral blood lymphocytes of patients with Parkinson disease [41].”
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“Additionally, a decrease in proteasome degradation can be, to some extent, a result of AGE modification of lysine residues that are then inaccessible for ubiquitinylation or glycation by the proteasome itself((83,84)).”
Bulteau, A., Moreau, M., Nizard, C., & Friguet, B. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1395.029 · Cited by 28
Self-citationProteasomal Oscillation during Mild Heat Shock in Aging Human Skin Fibroblasts
Kraft, D. C. E., Deocaris, C. C., & Rattan, S. I. S. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1354.028 · Cited by 28
Person‐specific differences in ubiquitin‐proteasome mediated proteostasis in human neurons
Hsieh, Y., Augur, Z. M., Arbery, M. R., Ashour, N., Barrett, K., Pearse, R. V., Tio, E. S., Duong, D. M., Felsky, D., Jager, P. L. D., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13680 · Cited by 26
Rattan, S. I. S., Gonzalez‐Dosal, R., Nielsen, E. R., Kraft, D. C. E., WEIBEL, J., & Kahns, S. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3586 · Cited by 27
“Another reason suggested for the age-related decline in proteasomal activities is the post-translational modifications, such as oxidation, glycation and glycoxidation (Bulteau et al., 2000; Carrard et al., 2002; Carrard et al., 2003).”
BackgroundOstrowska, H., Hempel, D., Holub, M., et al. (2008) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2008.08.063 · Cited by 25
“Moreover, the two isoforms of theα6 subunit (C2) are known to result from an alternative splicing, essential for proteasome activation, and/or from post-translational modification upon 20S proteasome assembly [29,30].”
BackgroundCabreiro, F., Perichon, M., Jatje, J., Malavolta, M., Mocchegiani, E., Friguet, B., & Petropoulos, I. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.10.007 · Cited by 23
“…study on the effect of aging on proteasome structure and function in human PBL, a decrease in proteasome proteolytic activity was associated with the modification of certain catalytic and regulatory subunits by glycation or by conjugation with a lipid peroxidation product (Carrard et al., 2003).”
BackgroundInfluentialSelf-citationUPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review
Papaevgeniou, N., & Chondrogianni, N. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_1 · Cited by 23
Witkowski, J. M., Mikosik, A., Bryl, E., & Fülöp, T. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.10.009 · Cited by 22
“However, as was mentioned above, both types of proteasomes make “presentable” peptides for the MHC; thus, if less effective, they churn out fewer such peptides, which also in this way may adversely affect the adaptive immune response (Carrard et al., 2003; Ponnappan et al., 2007; Ponnappan et al., 1999).”
BackgroundOliviero, G., Kovalchuk, S. I., Rogowska-Wrzesińska, A., Schwämmle, V., & Jensen, O. N. (2022) · eLife · doi:10.7554/elife.73524 · Cited by 25
“Recent reports suggested a decline of proteasome function related to senescence observed in several mammalian tissues and human cells ( Bulteau et al., 2000 ; Carrard et al., 2003 ; Petropoulos et al., 2000 ; Bardag-Gorce et al., 1999 ).”
Yusri, K., Kumar, S., Fong, S., Gruber, J., & Sorrentino, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126793 · Cited by 22
“The UPS pathway exhibits decreased efficiency with age; proteasome expression and activity decrease during aging [185–187].”
BackgroundChanges in cellular degradation activity in young and old worker honeybees (Apis mellifera)
Hsu, C., Chuang, Y.-L., & Chan, Y.-P. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.12.003 · Cited by 18
Phage‐Displayed Antibodies for the Detection of Glycated Proteasome in Aging Cells
Gonzalez‐Dosal, R., Sørensen, M. D., Clark, B. F. C., et al. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1354.068 · Cited by 18
Gressler, A. E., Leng, H., Zinecker, H., & Simon, A. K. (2023) · Seminars in Immunology · doi:10.1016/j.smim.2023.101838 · Cited by 15
“However, several studies argue for unchanged expression of proteasomes in aged human lymphocytes [118], including T cells [119].”
BackgroundJust, J., Jung, T., Friis, N. A., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.405 · Cited by 15
“the cellular content of the proteasome [15,16], pointing to other”
BackgroundPetersen, A. H., Honarvar, A. K. S., & Zetterberg, M. (2010) · Current Gerontology and Geriatrics Research · doi:10.1155/2010/230697 · Cited by 15
Hansen, T. Ø., Sarup, P. M., Loeschcke, V., et al. (2012) · Biogerontology · doi:10.1007/s10522-012-9387-2 · Cited by 14
“…Aarhus, Denmark S. I. S. Rattan Laboratory of Cellular Ageing, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark subunits are prone to different kinds of modifications, and a change in proteasome structure leads to decreased proteasome activity (Carrard et al. 2003).”
BackgroundThe Role of Proteasomes in Disease
Dahlmann, B. (2007) · Targeted Protein Database · doi:10.2970/tpdb.2007.32 · Cited by 14
Keeping the beat against time: Mitochondrial fitness in the aging heart
Mendoza, A., & Karch, J. M. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.951417 · Cited by 13
“there is an increase in the number of post-translational modifications of individual proteasome subunits, which contributed to age-related decline of 26S proteasome-specific activity (Carrard et al., 2003).”
BackgroundProteasome Biology: Chemistry and Bioengineering Insights
Račková, L., & Csekes, E. (2020) · Polymers · doi:10.3390/polym12122909 · Cited by 14
“Consistently, impaired chymotrypsin-like activity was observed in aged tissues [218,219], correlated with increased HNE-modification of the β5i subunit detected in leukocyte-enriched fractions of human blood appearing around the age of 40 years [218].”
BackgroundInfluentialLim, J. J., Noh, S., Kang, W., Hyun, B., Lee, B., & Hyun, S. (2024) · Autophagy · doi:10.1080/15548627.2024.2389607 · Cited by 12
“Similar to proteasomal activity, autophagy decreases with age in various tissues, including cardiac myocytes [60], hepatocytes [61], retinal cells [55,62], and fibroblasts [63].”
Song, Y., Liu, Y. S., Talarico, F., Zhang, Y., Hayward, J., Wang, M., Stroulia, E., Dixon, R. A., Greiner, R., Li, X., et al. (2023) · Gerontology · doi:10.1159/000534015 · Cited by 10
“For example, lymphocytes [15], red blood cell counts [16], alanine aminotransferase [17], and ferritin [18] have been iden-ti fi ed to be associated with aging.”
BackgroundKang, D., Baek, Y., & Lee, J. (2022) · Cells · doi:10.3390/cells11244062 · Cited by 9
Does lung aging have an impact on chronic obstructive pulmonary disease?
Ito, K. (2007) · Journal of Organ Dysfunction · doi:10.1080/17471060601137407 · Cited by 9
Zhao, S. G., Jackson, W., Kothari, V., et al. (2015) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2015.22 · Cited by 9
Characterization of the 20S proteasome in human glioblastomas.
Piccinini, M., RINAUDO, M. T., Anselmino, A., et al. (2005) · PubMed · Cited by 9
Cellular degradation activity is maintained during aging in long-living queen bees
Hsu, C., Qiu, J.-T. T., & Chan, Y.-P. (2016) · Biogerontology · doi:10.1007/s10522-016-9652-x · Cited by 8
“…significant differences, as determined by two-sample t tests (**P\ 0.01) et al. 2000a; Beedholm et al. 2004), lymphocytes (Ponnappan et al. 1999; Carrard et al. 2003), keratinocytes (Petropoulos et al. 2000), and epidermal cells (Bulteau et al. 2000), murine brain (Ohtsuka et al. 1995) and…”
BackgroundMethodInfluentialFemale Mice Reaching Exceptionally High Old Age Have Preserved 20S Proteasome Activities
de Toda, I. M., Rattan, S. I. S., la Fuente, M. D., & Arranz, L. (2021) · Antioxidants · doi:10.3390/antiox10091397 · Cited by 6
“In human lymphocytes, decreased agerelated specific activity of the 26 proteasome is associated with increased post-translational modifications, whereas levels and subunit composition are unaffected [19].”
Background
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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