Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts
Open accessAbstract
Changes in the two main intracellular degradation systems, the Ubiquitin-Proteasome System and the Autophagy-Lysosome pathway (ALP) are widely discussed as a hallmark of the aging process. To follow the age-related behavior of both degradation systems we examined their impact on ferritin, known to be degradable by both. Ferritin H was analyzed in young and senescent human fibroblasts, revealing a higher steady-state level in the senescent cells. By blocking both proteolytic systems, we confirmed that particularly the ALP plays a crucial role in ferritin H turnover. However, an unexpected increase in lysosomal activity in the senescent cells, suggests a dysregulation in the autophagy pathway. To further investigate the impaired ferritin H turnover, confocal microscopic colocalization studies of ferritin H with lysosomal-associated membrane protein 2a (Lamp2a) and monodansylcadaverine (MDC) were performed and clearly revealed the degradation of ferritin by macroautophagy. By induction of autophagy via inhibition of mTOR using rapamycin an increase of ferritin H turnover was obtained in senescent cells, demonstrating a mTOR dependent reduction of autophagy in senescent human fibroblasts.
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Impaired autophagy in senescent cells has previously been shown to reduce ferritin turnover, but intracellular iron levels or major iron homeostasis proteins were not evaluated in that study.
“Coincidently, impaired autophagy in senescent cells has previously been shown to reduce ferritin turnover, but in this study intracellular iron levels or the levels of major iron homeostasis proteins were not evaluated [77].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [77]
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- Authors
- Ott, C., König, J., Höhn, A., Jung, T., & Grune, T.
- Affiliations
- German Institute of Human Nutrition (DE)
- German Center for Diabetes Research (DE)
- German Centre for Cardiovascular Research (DE)
- Corresponding author
- Grune, Tilman
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2016-12
- Volume
- 101
- Pages
- 325-333
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2534897332
- Cited by
- 29
- References
- 46
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 4 · 2021: 1 · 2020: 1 · 2019: 6 · 2018: 5 · 2017: 5 · 2016: 1
- FWCI
- 5.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Free Radical Biology and Medicine (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion, cc-by-nc-nd)
- Funders
- Deutsche Forschungsgemeinschaft (Gr1240/18-1)
- Friedrich-Schiller-Universität Jena
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy, H-ferritin, protein turnover, cellular senescence, fibroblasts, autophagy-lysosome pathway, ubiquitin-proteasome system, lysosomal activity, mTOR, rapamycin, aging, LAMP2A
- MeSH terms
- Apoferritins, Autophagy, Cadaverine, Deferoxamine, Enzyme Inhibitors, Fibroblasts, Hemin, Humans, Kinetics, Lysosomes, Male, Gene Expression, Cellular Senescence, Sirolimus, Proteasome Endopeptidase Complex, Lysosomal-Associated Membrane Protein 2, Foreskin, TOR Serine-Threonine Kinases, Proteolysis, Primary Cell Culture
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