The DOI matches its Crossref record; 295 of the 295 references it cites were found in a registry or an index.
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Open accessAbstract
Reactive oxygen and nitrogen species change cellular responses through diverse mechanisms that are now being defined. At low levels, they are signalling molecules, and at high levels, they damage organelles, particularly the mitochondria. Oxidative damage and the associated mitochondrial dysfunction may result in energy depletion, accumulation of cytotoxic mediators and cell death. Understanding the interface between stress adaptation and cell death then is important for understanding redox biology and disease pathogenesis. Recent studies have found that one major sensor of redox signalling at this switch in cellular responses is autophagy. Autophagic activities are mediated by a complex molecular machinery including more than 30 Atg (AuTophaGy-related) proteins and 50 lysosomal hydrolases. Autophagosomes form membrane structures, sequester damaged, oxidized or dysfunctional intracellular components and organelles, and direct them to the lysosomes for degradation. This autophagic process is the sole known mechanism for mitochondrial turnover. It has been speculated that dysfunction of autophagy may result in abnormal mitochondrial function and oxidative or nitrative stress. Emerging investigations have provided new understanding of how autophagy of mitochondria (also known as mitophagy) is controlled, and the impact of autophagic dysfunction on cellular oxidative stress. The present review highlights recent studies on redox signalling in the regulation of autophagy, in the context of the basic mechanisms of mitophagy. Furthermore, we discuss the impact of autophagy on mitochondrial function and accumulation of reactive species. This is particularly relevant to degenerative diseases in which oxidative stress occurs over time, and dysfunction in both the mitochondrial and autophagic pathways play a role.
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“Oxidative stress has been shown to be an initiator and major contributor to both endoplasmic reticulum (ER) stress (Hotamisligil 2010; Kaneto et al. 2005) and lysosome-mediated autophagy (Lee et al. 2012)”
From Particulate matter 2.5 damages skin cells by inducing oxidative stress, subcellular organelle dysfunction, and apoptosis (2018) · cites this paper as Lee et al. 2012
In the citing paper
“In response to oxidative stress, autophagy increases in an attempt to remove oxidatively damaged organelles (Lee et al., 2012; Seo et al., 2012).”
From Microtubule-associated protein 1 light chain 3B, (LC3B) is necessary to maintain lipid-mediated homeostasis in the retinal pigment epithelium (2018) · cites this paper as Lee et al., 2012
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Citations
Cites
2 retracted
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RetractedChen, W., Li, N., Chen, T., Han, Y., Li, C., Wang, Y., He, W., Zhang, L., Wan, T. Y., & Cao, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502190200 · Cited by 82
RetractedHow mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
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Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154
An Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521
Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148
Ageing as a Risk Factor for Disease
Niccoli, T., & Partridge, L. (2012) · Current Biology · doi:10.1016/j.cub.2012.07.024 · Cited by 1,831
Metadata
- Authors
- Lee, J., Giordano, S., & Zhang, J.
- Affiliations
- University of Alabama at Birmingham (US)
- Corresponding author
- Zhang, Jianhua
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-12-21
- Volume
- 441
- Issue
- 2
- Pages
- 523-540
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC3258656
- OpenAlex
- W2124105006
- Cited by
- 1,438
- References
- 295
- Citations by year
- 2026: 45 · 2025: 58 · 2024: 65 · 2023: 68 · 2022: 98 · 2021: 99 · 2020: 110 · 2019: 116 · 2018: 143 · 2017: 119 · 2016: 104 · 2015: 115 · 2014: 118 · 2013: 118 · 2012: 62
- FWCI
- 11.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical Journal (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- National Institute for Health and Care Research
- National Institutes of Health (NS064090)
- National Institute of Neurological Disorders and Stroke (R01NS064090)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- autophagy, mitophagy, oxidative stress, redox signaling, reactive oxygen species, reactive nitrogen species, mitochondrial dysfunction, autophagy-related proteins, autophagosome formation, lysosomal degradation, mitochondrial turnover, cell death, degenerative diseases
- MeSH terms
- Protein Deglycase DJ-1, PTEN-Induced Putative Kinase, Animals, Autophagy, Cardiovascular Diseases, Humans, Hydrogen Peroxide, Lysosomes, Mitochondria, Neoplasms, Nitric Oxide, Oxidation-Reduction, Parkinson Disease, Protein Kinases, Transcription, Genetic, Signal Transduction, Oncogene Proteins, Reactive Oxygen Species, Oxidative Stress, Reactive Nitrogen Species, Intracellular Signaling Peptides and Proteins, TOR Serine-Threonine Kinases
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