2014
DOI: 10.18632/aging.100698
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Abstract: We analyzed an ex vivo model of in situ aged human dermal fibroblasts, obtained from 15 adult healthy donors from three different age groups using an unbiased quantitative proteome-wide approach applying label-free mass spectrometry. Thereby, we identified 2409 proteins, including 43 proteins with an age-associated abundance change. Most of the differentially abundant proteins have not been described in the context of fibroblasts’ aging before, but the deduced biological processes confirmed known hallmarks of … Show more

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Cited by 52 publications
(56 citation statements)
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References 58 publications
(80 reference statements)
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“…It is unlikely that this is a biological phenomenon but rather an artificial observation based on the proteins that are targeted by the SOMAmers. Other proteomic aging studies in humans using technology such as two‐dimensional gel electrophoresis (Byerley et al., 2010) or quantitative mass spectrometry (Waldera‐Lupa et al., 2014) showed an equal number of age‐associated proteins that decreased as well as increased with age. Second, the SOMAscan is not an absolute measure of proteins, and therefore, we cannot make comparisons between proteins.…”
Section: Discussionmentioning
confidence: 99%
“…It is unlikely that this is a biological phenomenon but rather an artificial observation based on the proteins that are targeted by the SOMAmers. Other proteomic aging studies in humans using technology such as two‐dimensional gel electrophoresis (Byerley et al., 2010) or quantitative mass spectrometry (Waldera‐Lupa et al., 2014) showed an equal number of age‐associated proteins that decreased as well as increased with age. Second, the SOMAscan is not an absolute measure of proteins, and therefore, we cannot make comparisons between proteins.…”
Section: Discussionmentioning
confidence: 99%
“…27,28 Although the previous work greatly advanced our understanding of age-associated changes of DNA DSB repair, due to a lack of proper tools for the analysis of NHEJ and HR efficiency and fidelity separately, and the hardship of acquiring a sufficient number of human samples, whether NHEJ efficiency and fidelity, and HR efficiency change with age in humans and the consequences of any such change, and its underlying molecular mechanism are not well understood. Here, we established 50 eyelids fibroblast cell lines derived from donors who are evenly distributed by age.…”
Section: Discussionmentioning
confidence: 99%
“…Similar changes in proteostasis have been reported for mammals; aged mice show decreased levels of mitochondrial proteins, proteins involved in defence against oxidative stress, and chaperones involved in the stress response [60][61][62] . In addition, ageing of human der mal fibroblasts ex vivo is also associated with reduced levels of chaperone, proteasomal, ribosomal, and mitochondrial proteins 22 .…”
Section: Derailment During Normal Ageingmentioning
confidence: 99%
“…With ageing, the gradual accumulation of misfolded or damaged pro teins, together with concomitant failure of PQC, results in proteotoxic stress and compromised defence against reactive oxygen species (ROS) 10 , a process that is likely to be accelerated in various age related diseases includ ing neurodegenerative diseases 12,13 , type 2 diabetes mel litus 14 , cancer 15 , and cardiac diseases [16][17][18][19][20] . In addition to the accumulation of misfolded proteins, ageing is accompanied by an imbalance in the proteome, as indi cated by lowered expression of chaperone, proteaso mal, ribosomal, and mitochondrial proteins, whereas proteins related to oxidative stress are upregulated 21,22 . Although mild impairment of proteostasis extends lifespan in Caenorhabditis elegans, referred to as hormesis, sustained impairment is accompanied by loss of PQC to neutralize this effect 3,5 .…”
mentioning
confidence: 99%