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Lysosomes in iron metabolism, ageing and apoptosis
Open accessAbstract
The lysosomal compartment is essential for a variety of cellular functions, including the normal turnover of most long-lived proteins and all organelles. The compartment consists of numerous acidic vesicles (pH approximately 4 to 5) that constantly fuse and divide. It receives a large number of hydrolases ( approximately 50) from the trans-Golgi network, and substrates from both the cells' outside (heterophagy) and inside (autophagy). Many macromolecules contain iron that gives rise to an iron-rich environment in lysosomes that recently have degraded such macromolecules. Iron-rich lysosomes are sensitive to oxidative stress, while 'resting' lysosomes, which have not recently participated in autophagic events, are not. The magnitude of oxidative stress determines the degree of lysosomal destabilization and, consequently, whether arrested growth, reparative autophagy, apoptosis, or necrosis will follow. Heterophagy is the first step in the process by which immunocompetent cells modify antigens and produce antibodies, while exocytosis of lysosomal enzymes may promote tumor invasion, angiogenesis, and metastasis. Apart from being an essential turnover process, autophagy is also a mechanism by which cells will be able to sustain temporary starvation and rid themselves of intracellular organisms that have invaded, although some pathogens have evolved mechanisms to prevent their destruction. Mutated lysosomal enzymes are the underlying cause of a number of lysosomal storage diseases involving the accumulation of materials that would be the substrate for the corresponding hydrolases, were they not defective. The normal, low-level diffusion of hydrogen peroxide into iron-rich lysosomes causes the slow formation of lipofuscin in long-lived postmitotic cells, where it occupies a substantial part of the lysosomal compartment at the end of the life span. This seems to result in the diversion of newly produced lysosomal enzymes away from autophagosomes, leading to the accumulation of malfunctioning mitochondria and proteins with consequent cellular dysfunction. If autophagy were a perfect turnover process, postmitotic ageing and several age-related neurodegenerative diseases would, perhaps, not take place.
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“Lipofuscin, an age-related iron rich pigment is non-degradable and not hydrolyzed by lysosomal enzymes.As a result, lipofuscin accumulates in the lysosomes.Lysosomes do not have the capacity to remove intralysosomal iron bound to lipofuscin, leading to excessive iron accumulation.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
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“It has been shown that lysosomes are a source of rapidly mobilized, chelatable iron, with accumulation of iron being higher with ageing.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
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“Low internal pH i.e. 4 to 5 , presence of reducing equivalents, such as cysteine, ascorbic acid and glutathione favour intralysosomal Fenton reaction (Kurz et al., 2008).”
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“Iron depletion has been found to damage lysosomes although it has been suggested that the mechanism may be a consequence of other apopotogenic factors (Kurz et al., 2008).”
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“Even under normal conditions, some iron-catalyzed peroxidation occurs intralysosomally (lysosomes are rich in redox-active iron), resulting in oxidative modification of autophagocytosed material and yielding lipofuscin, a polymeric compound slowly accumulating within ageing postmitotic cells at a rate that is inversely correlated to the longevity across species (Kurz et al, 2008).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al, 2008
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“ROS play a prominent causal role in LMP, not only as the H2O2-driven luminal production of hydroxyl radicals by Fenton reactions destabilizes the lysosomal membrane upon lipid peroxidation [766, 767]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [767]
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Self-citationNILSSON, S. E. G., Sundelin, S. P., Wihlmark, U., & Brunk, U. T. (2003) · Documenta Ophthalmologica · doi:10.1023/a:1022419606629 · Cited by 107
Self-citationInsights Into the Diagnosis and Treatment of Lysosomal Storage Diseases
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Terman, A., Dalen, H., & Brunk, U. T. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(99)00070-4 · Cited by 106
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Doulias, P., Christoforidis, S., Brunk, U. T., & Galaris, D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00396-4 · Cited by 96
Self-citationGiant mitochondria do not fuse and exchange their contents with normal mitochondria
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Self-citationBrain Iron Metabolism and Neurodegenerative Disorders
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Ceroid/Lipofuscin-loaded human fibroblasts show increased susceptibility to oxidative stress
Terman, A., Abrahamsson, N., & Brunk, U. T. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(99)00045-5 · Cited by 93
Self-citationMitochondria in hematopoiesis and hematological diseases
Fontenay, M., Cathelin, S., Amiot, M., Gyan, E., & Solary, É. (2006) · Oncogene · doi:10.1038/sj.onc.1209606 · Cited by 92
Colocalization of iron and ceroid in human atherosclerotic lesions
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Bergamini, E. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.001 · Cited by 90
LIPOFUSCIN IN BOVINE MUSCLE AND BRAIN: A MODEL FOR STUDYING AGE PIGMENT
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Cathepsin D–Bax death pathway in oxidative stressed neuroblastoma cells
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Brunk, U. T., & Dricsson, J. L. E. (1972) · The Histochemical Journal · doi:10.1007/bf01011128 · Cited by 85
Self-citationBaumgartner, H. K., Gerasimenko, J. V., Thorne, C., Ashurst, L. H., Barrow, S. L., Chvanov, M., Gillies, S., Criddle, D. N., Tepikin, A. V., Petersen, O. H., et al. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00103.2007 · Cited by 85
Lysosomal heterogeneity between and within cells with respect to resistance against oxidative stress
Nilsson, E., Ghassemifar, R., & Brunk, U. T. (1997) · The Histochemical Journal · doi:10.1023/a:1026441907803 · Cited by 81
Self-citationThe aging myocardium: roles of mitochondrial damage and lysosomal degradation
Terman, A., & Brunk, U. T. (2005) · Heart, Lung and Circulation · doi:10.1016/j.hlc.2004.12.023 · Cited by 80
Self-citationYeung, B. H. Y., Huang, D.-C., & Sinicrope, F. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508533200 · Cited by 80
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Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
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Self-citationVaisman, B. L., Fibach, E., & Konijn, A. M. (1997) · Blood · doi:10.1182/blood.v90.2.831 · Cited by 72
3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin
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Metadata
- Authors
- Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T.
- Affiliations
- Linköping University (SE)
- Linköping University Hospital (SE)
- Corresponding author
- Brunk, Ulf T.
- Venue
- Histochemistry and Cell Biology
- Published
- 2008-02-08
- Volume
- 129
- Issue
- 4
- Pages
- 389-406
- ISSN
- 0948-6143 (ISSN-L)
- 1432-119X
- PMC
- PMC2668650
- OpenAlex
- W2130287342
- Cited by
- 302
- References
- 143
- Citations by year
- 2026: 11 · 2025: 20 · 2024: 10 · 2023: 19 · 2022: 20 · 2021: 15 · 2020: 16 · 2019: 10 · 2018: 12 · 2017: 19 · 2016: 18 · 2015: 24 · 2014: 7 · 2013: 21 · 2012: 17
- FWCI
- 2.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Histochemistry and Cell Biology (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KTH Publication Database DiVA (KTH Royal Institute of Technology) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- lysosomes, iron metabolism, aging, apoptosis, autophagy, heterophagy, oxidative stress, lysosomal destabilization, lysosomal enzymes, lysosomal storage disease, lipofuscin, hydrogen peroxide, mitochondrial dysfunction, age-related neurodegenerative diseases, necrosis
- MeSH terms
- Aging, Animals, Humans, Iron, Lipofuscin, Lysosomes, Mitochondria, Models, Biological, Oxidative Stress
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