Inhibitors of succinate: quinone reductase/complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death

Ralph, Stephen J.; Moreno-Sánchez, Rafael; Neuzil, Jiri; Rodríguez-Enríquez, Sara

doi:10.1007/s11095-011-0566-7

Cited by 126Mitochondrial Function and PathologyBioactive Compounds and Antitumor AgentsRedox biology and oxidative stress

Inhibitors of succinate: quinone reductase/complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death

Ralph, Stephen J., Moreno-Sánchez, Rafael, Neuzil, Jiri, Rodríguez-Enríquez, Sara·2011·Pharmaceutical Research

DOI 10.1007/s11095-011-0566-7

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Abstract

Succinate:quinone reductase (SQR) of Complex II occupies a unique central point in the mitochondrial respiratory system as a major source of electrons driving reactive oxygen species (ROS) production. It is an ideal pharmaceutical target for modulating ROS levels in normal cells to prevent oxidative stress-induced damage or alternatively,increase ROS in cancer cells, inducing cell death.The value of drugs like diazoxide to prevent ROS production,protecting normal cells, whereas vitamin E analogues promote ROS in cancer cells to kill them is highlighted. As pharmaceuticals these agents may prevent degenerative disease and their modes of action are presently being fully explored. The evidence that SDH/Complex II is tightly coupled to the NADH/NAD+ ratio in all cells,impacted by the available supplies of Krebs cycle intermediates as essential NAD-linked substrates, and the NAD+-dependent regulation of SDH/Complex II are reviewed, as are links to the NAD+-dependent dehydrogenases, Complex I and the E3 dihiydrolipoamide dehydrogenase to produce ROS. This review collates and discusses diverse sources of information relating to ROS production in different biological systems, focussing on evidence for SQR as the main source of ROS production in mitochondria, particularly its relevance to protection from oxidative stress and to the mitochondrial-targeted anti cancer drugs (mitocans) as novel cancer therapies [corrected].

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Mutations in complex II subunits C and D near the Qp site are associated with hereditary paragangliomas and pheochromocytomas, and SdhA mutations can cause Leigh syndrome.
“This seems to be especially the case for mutations in complex II subunits C and D located in the vicinity of the Qp site that have been associated with specific forms of cancer such as hereditary paragangliomas and pheochromocytomas (overview in [13,14,36]) and in SdhA that can cause Leigh syndrome, a progressive neurodegenerative disease [14,94].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [36]
The increased succinate pool under hypoxia may come from glutamate via alpha-ketoglutarate by transamination or from partial reversal of the TCA cycle from malate through fumarate, which would require complex II to act as a fumarate reductase.
“This increased succinate pool under hypoxia might be supplied either from glutamate through α-ketoglutarate by transamination [76,77] or by a partial reversal of the TCA cycle from malate through fumarate, which requires that complex II would become a fumarate reductase under hypoxia [36,79].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [36]
Loss of complex II function can cause succinate accumulation and increased ROS generation in mammalian cells.
“It has been observed that loss of function of complex II can lead to the accumulation of succinate and increased ROS generation in mammalian cells (overview in [14,36]).”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [36]
The prevalent view is that under these conditions ROS are produced by complex I due to reverse electron transfer from complex II, although alternative explanations have been proposed.
“While alternative explanations for the source or mechanism of ROS production under these conditions have been proposed [34,36], the prevalent view is that under these conditions ROS are produced by complex I due to RET from complex II [18][19][20]23].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [36]
Recent publications challenging the existence of reverse electron transfer from complex II into complex I have not considered the requirement of complexes III and IV for high membrane potential.
“This has not been considered in recent publications that have challenged the existence of a reverse electron transfer from complex II into complex I [36,110].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [36]

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Self-citation
Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction
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Authors: Ralph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S.
Affiliations: Griffith University (AU)
Corresponding author: Ralph, Stephen J.
ORCID: Ralph, Stephen J.
Venue: Pharmaceutical Research
Publisher: Springer Science and Business Media LLC
Published: 2011-08-24
Volume: 28
Issue: 11
Pages: 2695-2730
ISSN: 0724-8741 (ISSN-L)
1573-904X
DOI: 10.1007/s11095-011-0566-7
OpenAlex: W1983521123
Cited by: 126
References: 292
Citations by year: 2026: 2 · 2025: 4 · 2024: 12 · 2023: 12 · 2022: 6 · 2021: 12 · 2020: 11 · 2019: 8 · 2018: 9 · 2017: 9 · 2016: 5 · 2015: 9 · 2014: 12 · 2013: 6 · 2012: 9
FWCI: 0.78
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Pharmaceutical Research (publishedVersion)
PubMed (publishedVersion)
ASEP (submittedVersion, public-domain)
Griffith Research Online (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: succinate dehydrogenase, mitochondrial reactive oxygen species, oxidative stress, ischemic injury, cancer cell death, diazoxide, vitamin E analogues, NAD+/NADH ratio, Krebs cycle intermediates, NAD-dependent dehydrogenase, mitocans
MeSH terms: Coenzyme A, Fatty Acids, Nonesterified, Humans, Dihydrolipoamide Dehydrogenase, Mitochondria, Neoplasms, Organophosphorus Compounds, Ubiquinone, NAD(P)H Dehydrogenase (Quinone), Cell Death, Reactive Oxygen Species, Succinic Acid, Protective Agents, alpha-Tocopherol

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Inhibitors of succinate: quinone reductase/complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death

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