CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control
Open accessAbstract
During the course of biological aging, there is a gradual accumulation of damaged proteins and a concomitant functional decline in the protein degradation system. Protein quality control is normally ensured by the coordinated actions of molecular chaperones and the protein degradation system that collectively help to maintain protein homeostasis. The carboxyl terminus of Hsp70-interacting protein (CHIP), a ubiquitin ligase/cochaperone, participates in protein quality control by targeting a broad range of chaperone substrates for proteasome degradation via the ubiquitin-proteasome system, demonstrating a broad involvement of CHIP in maintaining cytoplasmic protein quality control. In the present study, we have investigated the influence that protein quality control exerts on the aging process by using CHIP-/- mice. CHIP deficiency in mice leads to a markedly reduced life span, along with accelerated age-related pathophysiological phenotypes. These features were accompanied by indications of accelerated cellular senescence and increased indices of oxidative stress. In addition, CHIP-/- mice exhibit a deregulation of protein quality control, as indicated by elevated levels of toxic oligomer proteins and a decline in proteasome activity. Taken together, these data reveal that impaired protein quality control contributes to cellular senescence and implicates CHIP-dependent quality control mechanisms in the regulation of mammalian longevity in vivo.
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Studies in CHIP defective mice support an important role for the UPS in longevity and health-span.
“studies in CHIP defective mice also support an important role for the UPS in longevity and health-span (Min et al., 2008)”
From Protein Homeostasis and Aging: the importance of exquisite quality control (2011) · cites this paper as Min et al., 2008
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BackgroundStankiewicz, M., Nikolay, R., Rybin, V., & Mayer, M. P. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07737.x · Cited by 120 · see citing works
The ubiquitin-proteasome system in cardiac proteinopathy: a quality control perspective
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Heterozygous STUB1 mutation causes familial ataxia with cognitive affective syndrome (SCA48)
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“STUB1 participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation.(48) The effects of c.”
BackgroundProtein aggregation as a paradigm of aging
Lindner, A. B., & Démarez, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.005 · Cited by 106 · see citing works
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“The decreased proteasomal activity and the dysfunction of the protein quality control system in these animals lead to increased levels of toxic protein oligomers in the brain of these animals prior to the emergence of most of the age-related phenotypes [36].”
BackgroundWilliams, A. J., Knutson, T. M., Gould, V. F. C., & Paulson, H. L. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.10.016 · Cited by 103 · see citing works
“Although a recent paper shows a 50% mortality rate in CHIP-null mice by 12 months (Min et al., 2008), we did not observe increased mortality in our experiments unless the Q71-B transgene was also present (Fig.”
BackgroundIdentification of CHIP as a Novel Causative Gene for Autosomal Recessive Cerebellar Ataxia
Shi, Y., Wang, J., Li, J., Ren, H., Guan, W., He, M., Yan, W., Zhou, Y., Hu, Z., Zhang, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081884 · Cited by 102 · see citing works
“Previous studies have also shown that CHIP-deficient mice exhibit profound dysbasia, low body weights and premature aging phenotypes [36,43].”
BackgroundDoes Damage to DNA and Other Macromolecules Play a Role in Aging? If So, How?
Campisi, J., & Vijg, J. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/gln065 · Cited by 104 · see citing works
Extracellular Matrix Dynamics as an Emerging yet Understudied Hallmark of Aging and Longevity
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HSF1Base: A Comprehensive Database of HSF1 (Heat Shock Factor 1) Target Genes
Kovács, D., Sigmond, T., Hotzi, B., Bohár, B., Fazekas, D., Deák, V., Vellai, T., & Barna, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225815 · Cited by 99 · see citing works
“Furthermore, mutant mice defective for co-chaperone (CHIP) activity age faster than normal [72], and certain HSP-encoding genes become upregulated in long-lived mutant mouse strains [73].”
BackgroundOlive Oil and the Hallmarks of Aging
Fernández-del-Río, L., Gutiérrez-Casado, E., Varela‐López, A., & Villalba, J. M. (2016) · Molecules · doi:10.3390/molecules21020163 · Cited by 96 · see citing works
“organelle-specific chaperones is significantly impaired in aging [73] and research with animal models supports the positive impact of chaperones on longevity [74–77].”
Endothelial cell senescence and thrombosis: Ageing clots
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Decoding the contribution of dopaminergic genes and pathways to autism spectrum disorder (ASD)
Nguyen, M., Roth, A., Kyzar, E. J., Poudel, M. K., Wong, K., Stewart, A., & Kalueff, A. V. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.01.002 · Cited by 95 · see citing works
“…and its expression in the brain is down-regulated in autistic patients (Nakamura et al., 2011) STUB1: Encodes STUB1 (CHIP), a ubiquitin ligase/co-chaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008).”
Horikawa, I., Fujita, K., Jenkins, L. M. M., Hiyoshi, Y., Mondal, A. M., Vojtěšek, B., Lane, D. P., Appella, E., & Harris, C. C. (2014) · Nature Communications · doi:10.1038/ncomms5706 · Cited by 93 · see citing works
The role of hydrogen sulfide in aging and age-related pathologies
Perridon, B. W., Leuvenink, H. G. D., Hillebrands, J., van Goor, H., & Bos, E. M. (2016) · Aging · doi:10.18632/aging.101026 · Cited by 89 · see citing works
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle
Li, Z., Hartl, F. U., & Bracher, A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2608 · Cited by 87 · see citing works
Facilitating Akt Clearance via Manipulation of Hsp70 Activity and Levels
Koren, J., Jinwal, U. K., Jin, Y., O’Leary, J. C., Jones, J. R., Johnson, A. G., Blair, L. J., Abisambra, J. F., Chang, L., Miyata, Y., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057208 · Cited by 85 · see citing works
Zhu, X., Zhang, J., Sun, H., Jiang, C., Dong, Y., Shan, Q., Su, S., Xie, Y., Xu, N., Lou, X., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562868 · Cited by 84 · see citing works
“As mentioned above, the ectopic expression of H-RAS G12V in primary human melanocytes regulated the UPR and induced senescence (26); on the other hand, aging was accelerated in CHIP knock-out mice (27).”
BackgroundThe Ubiquitin Ligase CHIP Prevents SirT6 Degradation through Noncanonical Ubiquitination
Ronnebaum, S. M., Wu, Y., McDonough, H., & Patterson, C. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00480-13 · Cited by 78 · see citing works
“Similar to our observations of CHIP / mice (5), SirT6 / mice that survive the perinatal period are smaller than WT littermates and exhibit a premature-aging phenotype characterized by loss of subcutaneous fat, decreased bone mineral density, lordokyphosis, and increased senescence-associated -galactosidase staining (2…”
BackgroundResultSelf-citationThe Amazing Ubiquitin-Proteasome System: Structural Components and Implication in Aging
Tsakiri, E. N., & Trougakos, I. P. (2014) · International review of cytology · doi:10.1016/bs.ircmb.2014.09.002 · Cited by 78 · see citing works
Hunt, L. C., Schadeberg, B., Stover, J., Haugen, B., Pagala, V., Wang, Y., Puglise, J. M., Barton, E. R., Peng, J., & Demontis, F. (2021) · Nature Communications · doi:10.1038/s41467-021-21738-8 · Cited by 76 · see citing works
Ubiquitin receptors and protein quality control
Wang, X., & Terpstra, E. J. M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.09.012 · Cited by 74 · see citing works
“Indeed, CHIP knockout mice display accelerated aging [21].”
BackgroundJoshi, V., Amanullah, A., Upadhyay, A., Mishra, R., Kumar, A., & Mishra, A. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00093 · Cited by 74 · see citing works
CHIP protects against cardiac pressure overload through regulation of AMPK
Schisler, J. C., Rubel, C. E., Zhang, C., Lockyer, P. P., Cyr, D., & Patterson, C. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69080 · Cited by 71 · see citing works
Self-citationOn the enigma of carnosine’s anti-ageing actions
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“Decreased intracellular elimination of aberrant polypeptides by proteasomal activity and autophagy can contribute to altered protein accumulation, while upregulation of certain proteolytic functions is associated with increased longevity (Min et al., 2008; Yun et al., 2008; Bonelli et al., 2008; Cuervo 2008; Bergami e…”
BackgroundHeimdal, K., Sánchez-Guixé, M., Aukrust, I., Bollerslev, J., Bruland, O., Jablonski, G. E., Erichsen, A. K., Gude, E., Koht, J. A., Erdal, S., et al. (2014) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-014-0146-0 · Cited by 71 · see citing works
“The Asn-residue at position 65 is highly conserved (from human to C. elegans) and previously shown to be directly involved in binding of substrates such as Smad1, HSC70, HSP70 and HSP90 [21].”
BackgroundResultInfluentialProtein homeostasis and aging: Role of ubiquitin protein ligases
Jana, N. R. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.02.009 · Cited by 67 · see citing works
HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
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Genetic Pathways of Aging and Their Relevance in the Dog as a Natural Model of Human Aging
Sándor, S., & Kubinyi, E. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00948 · Cited by 66 · see citing works
“…or upregulation of Hsp-s was shown to extend lifespan, together with providing increased stress resistance, in both worms and flies (Walker and Lithgow, 2003; Morrow et al., 2004; Chiang et al., 2012), while reduced chaperone function caused accelerated aging in mice (Min et al., 2008).”
BackgroundPhysiology of ageing of the musculoskeletal system
Boros, K., & Freemont, A. J. (2017) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2017.09.003 · Cited by 65 · see citing works
Trougakos, I. P., Sesti, F., Tsakiri, E. N., & Gorgoulis, V. G. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.02.024 · Cited by 63 · see citing works
“The inactivation of CHIP in mice leads to a marked reduction in lifespan associated with accelerated age-related pathophysiological phenotypes [231].”
Ullah, K., Chen, S., Lü, J., Wang, X., Liu, Q. L., Zhang, Y., Long, Y., Hu, Z., & Xu, G. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011280 · Cited by 61 · see citing works
“It has been discovered that STUB1 protein level is upregulated in senescent human fibroblasts (26), whereas Stub1 knockout mice have reduced life span (27) and STUB1 silencing induces premature senescence (25).”
BackgroundKettern, N., Rogon, C., Limmer, A., Schild, H., & Höhfeld, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016398 · Cited by 60 · see citing works
“Moreover, CHIP deficient mice show an increased sensitivity to oxidative damage [47].”
BackgroundKireev, R. A., Vara, E., Viña, J., & Tresguerres, J. A. F. (2014) · AGE · doi:10.1007/s11357-014-9707-3 · Cited by 59 · see citing works
“This condition caused gradual accumulation of damaged proteins leading to a functional decline in the brain’s endogenous defence system (Rumora et al. 2007; Min et al. 2008) and leading to the activation of stress kinases (JNK and p38 MAPK) (Gabai et al.”
BackgroundChaperone-assisted E3 ligase CHIP: A double agent in cancer
Kumar, S., Basu, M., & Ghosh, M. K. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.003 · Cited by 57 · see citing works
“It has been reported that in STUB1 deficient mice, lagging related biomarkers are increased due to accumulation of toxic proteins.(277) Expression of leucine rich repeat kinase-2 (LRRK2) is high in STUB1 KO mouse model of PD.”
BackgroundThe E3 ubiquitin ligase CHIP in normal cell function and in disease conditions
Wang, T., Wang, W., Wang, Q., Xie, R., LANDAY, A. L., & Chen, D. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14206 · Cited by 57 · see citing works
Kevei, É., Pokrzywa, W., & Hoppe, T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12750 · Cited by 52 · see citing works
Role of S5b/PSMD5 in Proteasome Inhibition Caused by TNF-α/NFκB in Higher Eukaryotes
Shim, S. M., Lee, W., Kim, Y., Chang, J. W., Song, S., & Jung, Y. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.013 · Cited by 49 · see citing works
Zhao, T., Hong, Y., Yin, P., Li, S., & Li, X. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710549114 · Cited by 51 · see citing works
“Mice with CHIP deficiency show increased levels of toxic oligomer proteins and decreased proteasomal activity (6).”
BackgroundmTORC1 Links Protein Quality and Quantity Control by Sensing Chaperone Availability
Qian, S., Zhang, X., Sun, J., Bennink, J. R., Yewdell, J. W., & Patterson, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.120295 · Cited by 51 · see citing works
Self-citationKim, S., Grenert, J. P., Patterson, C., & Correia, M. A. (2016) · Scientific Reports · doi:10.1038/srep29423 · Cited by 51 · see citing works
Self-citationThe roles of ubiquitination in extrinsic cell death pathways and its implications for therapeutics
Seo, J., Kim, M. W., Bae, K., Lee, S. C., Song, J., & Lee, E. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.11.012 · Cited by 47 · see citing works
Autophagy and the ubiquitin-proteasome system in cardiac dysfunction.
Zheng, Q., & Wang, X. (2010) · PubMed · Cited by 48 · see citing works
Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1
Shang, Y., Xu, X., Duan, X., Guo, J., Wang, Y., Ren, F., He, D., & Chang, Z. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.02.124 · Cited by 48 · see citing works
Molecular chaperones as regulators of cell death
Hishiya, A., & Takayama, S.-I. J. (2008) · Oncogene · doi:10.1038/onc.2008.314 · Cited by 47 · see citing works
Protein Homeostasis at the Plasma Membrane
Apaja, P. M., & Lukács, G. L. (2014) · Physiology · doi:10.1152/physiol.00058.2013 · Cited by 46 · see citing works
“These observations with the modest phenotypic manifestation of the CHIP knockout mouse (87) suggest that a complex network of QC E3 ligases has evolved to maintain PM proteostasis with overlapping substrate specificity.”
BackgroundHuang, C., Kuo, W., Lo, J., Ho, T., Pai, P., Chiang, S., Chen, P., Tsai, F.-J., Tsai, C., & Huang, C. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.356 · Cited by 46 · see citing works
Ubiquitin Ligases in Longevity and Aging Skeletal Muscle
Hughes, D. C., Baehr, L. M., Waddell, D. S., Sharples, A. P., & Bodine, S. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147602 · Cited by 45 · see citing works
“In whole body knockout mice, CHIP deficiency significantly reduced mammalian lifespan and was accompanied by reduced proteasome activity in muscle and liver tissues [36].”
BackgroundA CHIPotle in physiology and disease
Paul, I., & Ghosh, M. K. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.10.027 · Cited by 45 · see citing works
Woo, C.-H., Le, N., Shishido, T., Chang, E. B., Lee, H., Heo, K., Mickelsen, D. M., Lu, Y., McClain, C., Spangenberg, T., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-162636 · Cited by 44 · see citing works
Self-citationConnecting chaperone-mediated autophagy dysfunction to cellular senescence
Moreno-Blas, D., Gorostieta-Salas, E., & Castro‐Obregón, S. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.11.001 · Cited by 42 · see citing works
Luan, H., Mohapatra, B. C., Bielecki, T. A., Mushtaq, I., Mirza, S., Jennings, T. A., Clubb, R. J., An, W., Ahmed, D., Ansari, R. E., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-16-2140 · Cited by 42 · see citing works
Willis, M. S., Min, J., Wang, S., McDonough, H., Lockyer, P. P., Wadosky, K. M., & Patterson, C. (2013) · Cell Biochemistry and Function · doi:10.1002/cbf.2962 · Cited by 40 · see citing works
“This may account for the disproportionate increase in HW/BW versus the cross-sectional areas of the CHIP / and wild-type mice, which has previously been reported.(29) The running performance of both CHIP / and wild-type mice improved during the course of voluntary running (Supplemental Figure 1A).”
BackgroundMethodInfluentialSelf-citationZhou, Y., Zhu, Y., Zhang, L., Wu, T., Wu, T., Zhang, W., Decker, A. M., He, J., Liu, J., Wu, Y., et al. (2016) · Stem Cells · doi:10.1002/stem.2321 · Cited by 41 · see citing works
Chronic obstructive pulmonary disease and the hallmarks of aging
Kukrety, S., Parekh, J. D., & Bailey, K. (2018) · Lung India · doi:10.4103/lungindia.lungindia_266_17 · Cited by 38 · see citing works
“[41] Genetically modified mice deficient in HSP demonstrates accelerated aging.[42] Function of the proteolytic systems also diminishes with aging.”
BackgroundSpinocerebellar ataxia type 48: last but not least
Michele, G. D., Galatolo, D., Barghigiani, M., Iacovo, D. D., Trovato, R., Tessa, A., Salvatore, E., Filla, A., Michele, G. D., & Santorelli, F. (2020) · Neurological Sciences · doi:10.1007/s10072-020-04408-3 · Cited by 34 · see citing works
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E6-AP association promotes SOD1 aggresomes degradation and suppresses toxicity
Mishra, A., Maheshwari, M., Chhangani, D., Fujimori-Tonou, N., Endo, F., Joshi, A. P., Jana, N. R., & Yamanaka, K. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.08.016 · Cited by 40 · see citing works
Germain, D. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06502.x · Cited by 40 · see citing works
“Since protein oxidation increases with age, while proteasome activity decreases with age (Berlett and Stadtman, 1997; Min et al., 2008; Morimoto, 2008), if correct this possibility would suggest that proteasome activators in combination with antioxidants may represent a novel anti-ageing strategy.”
BackgroundRonnebaum, S. M., Patterson, C., & Schisler, J. C. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1180 · Cited by 37 · see citing works
“Additionally, our laboratory recently reported on a novel interaction between AMPK and C terminus of heat shock protein 70-interacting protein (CHIP), an E3 ubiquitin ligase that mediates protein quality control during acute and chronic stress (66, 67).”
BackgroundSelf-citationThe E3 Ligase CHIP Mediates p21 Degradation to Maintain Radioresistance
Biswas, K., Sarkar, S., Du, K., Brautigan, D. L., Abbas, T., & Larner, J. M. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0466 · Cited by 38 · see citing works
“Consistently, CHIP-deficient mice (chip / ) exhibit reduced life span with accelerated aging phenotypes including osteoporosis, cellular senescence, and accumulation of oxidized lipids (10).”
BackgroundNeuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein
Lizama, B. N., Palubinsky, A. M., Raveendran, V. A., Moore, A. M., Federspiel, J. D., Codreanu, S. G., Liebler, D. C., & McLaughlin, B. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0699-18.2018 · Cited by 37 · see citing works
“Because chronic loss of CHIP causes profound changes in the proteome and intracellular milieu (Min et al., 2008; Palubinsky et al., 2015), we chose to acutely deplete rat primary neurons of endogenous CHIP using siRNA to test this hypothesis.”
BackgroundMethodHuang, P., Kuo, W., Shen, C.-Y., Chen, Y.-F., Lin, Y.-M., Ho, T., Padma, V. V., Lo, J., Huang, K. C., & Huang, C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091588 · Cited by 37 · see citing works
“Moreover, CHIP exerts its cardioprotective effect via regulating protein stability during heart failure [67,68].”
Background
- Authors
- Min, J.-N., Whaley, R. A., Sharpless, N. E., Lockyer, P., Portbury, A. L., & Patterson, C.
- Affiliations
- Carolina Cardiovascular Biology Center
- UNC Lineberger Comprehensive Cancer Center (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Patterson, Cam
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2008-06-01
- Volume
- 28
- Issue
- 12
- Pages
- 4018-4025
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC2423116
- OpenAlex
- W2143659623
- Cited by
- 256
- References
- 49
- Citations by year
- 2026: 8 · 2025: 5 · 2024: 5 · 2023: 12 · 2022: 8 · 2021: 16 · 2020: 20 · 2019: 14 · 2018: 18 · 2017: 19 · 2016: 17 · 2015: 11 · 2014: 22 · 2013: 19 · 2012: 14
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- American Heart Association
- National Institutes of Health (5r01gm061728-12)
- National Institute on Aging (AG 024282, P01 AG 024282)
- National Heart, Lung, and Blood Institute (HL 65619, R01HL065619, R37HL065619)
- National Institute of General Medical Sciences (GM-61728, R01-GM061728)
- 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 › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- CHIP, protein quality control, aging, longevity, accelerated aging, cellular senescence, proteasome activity, ubiquitin-proteasome system, oxidative stress, protein aggregation, proteostasis
- MeSH terms
- Aging, Animals, Brain, Cytoplasm, Lipids, Mice, Inbred C57BL, Mice, Transgenic, Models, Biological, Oxygen, Phenotype, Cellular Senescence, Molecular Chaperones, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Mice
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