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Mitochondrial Dysfunction and Oxidative Damage

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (28 February 2019) | Viewed by 56769

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Dr. Iain P. Hargreaves

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Department of Pharmacy and Biomolecular Science, Liverpool John Moores University, Byrom Street, Liverpool L3 5UA, UK
Interests: mitochondrial dysfunction; oxidative stress; coenzyme Q10
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Special Issue Information

Dear Colleagues,

Mitochondrial dysfunction and oxidative stress have been implicated in the pathogenesis of a number of diseases and conditions. The mitochondrial electron transport chain (ETC) is particularly vulnerable to reactive oxygen (ROS) and nitrogen (RNS) species induced impairment either as the result free radical induced damage to the enzyme complexes, mitochondrial DNA or mitochondrial membrane phospholipids. Once impaired the ETC then becomes a major source of ROS generation, which results in further damage to the ETC, as well compounding the cellular oxidative stress. Although the cell possesses a number of antioxidant systems to combat ROS and RNS, during pathological conditions these defences can become overwhelmed resulting in oxidative damage to the biomolecules of the cell and resulting in cellular and consequently, organ dysfunction. Therefore, the use of appropriate antioxidant strategies, especially those that target the mitochondria may be particularly important in the treatment of diseases associated with oxidative stress. Clinical management of oxidative stress and mitochondrial dysfunction is hampered by a lack of consensus on appropriate treatment strategies together with an absence of reliable non-invasive surrogates to monitor disease progression and the treatment response following therapeutic invention

This Special Issue requests original research, mini and full reviews, and perspectives that address the progress and current standing in the field of mitochondrial dysfunction and oxidative stress.

Dr. Iain P. Hargreaves
Guest Editor

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Keywords

Metabolic disease
Oxidative stress,
Antioxidants strategies
Coenzyme Q10
Glutathione
Mitochondrial diseases
Disease markers of mitochondrial respiratory chain disorders
Secondary causes of mitochondrial respiratory chain disorders

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Published Papers (11 papers)

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Research

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13 pages, 1379 KiB

Open AccessCommunication

The Effect of Methylmalonic Acid Treatment on Human Neuronal Cell Coenzyme Q₁₀ Status and Mitochondrial Function

by Emma C. Proctor, Nadia Turton, Elle Jo Boan, Emily Bennett, Suzannah Philips, Robert A. Heaton and Iain P. Hargreaves

Int. J. Mol. Sci. 2020, 21(23), 9137; https://doi.org/10.3390/ijms21239137 - 30 Nov 2020

Cited by 10 | Viewed by 3360

Abstract

Methylmalonic acidemia is an inborn metabolic disease of propionate catabolism, biochemically characterized by accumulation of methylmalonic acid (MMA) to millimolar concentrations in tissues and body fluids. However, MMA’s role in the pathophysiology of the disorder and its status as a “toxic intermediate” is unclear, despite evidence for its ability to compromise antioxidant defenses and induce mitochondrial dysfunction. Coenzyme Q₁₀ (CoQ₁₀) is a prominent electron carrier in the mitochondrial respiratory chain (MRC) and a lipid-soluble antioxidant which has been reported to be deficient in patient-derived fibroblasts and renal tissue from an animal model of the disease. However, at present, it is uncertain which factors are responsible for inducing this CoQ₁₀ deficiency or the effect of this deficit in CoQ₁₀ status on mitochondrial function. Therefore, in this study, we investigated the potential of MMA, the principal metabolite that accumulates in methylmalonic acidemia, to induce a cellular CoQ₁₀ deficiency. In view of the severe neurological presentation of patients with this condition, human neuroblastoma SH-SY5Y cells were used as a neuronal cell model for this investigation. Following treatment with pathological concentrations of MMA (>0.5 mM), we found a significant (p = 0.0087) ~75% reduction in neuronal cell CoQ₁₀ status together with a significant (p = 0.0099) decrease in MRC complex II–III activity at higher concentrations (>2 mM). The deficits in neuronal CoQ₁₀ status and MRC complex II–III activity were associated with a loss of cell viability. However, no significant impairment of mitochondrial membrane potential (ΔΨm) was detectable. These findings indicate the potential of pathological concentrations of MMA to induce a neuronal cell CoQ₁₀ deficiency with an associated loss of MRC complex II–III activity. However, in the absence of an impairment of ΔΨm, the contribution this potential deficit in cellular CoQ₁₀ status makes towards the disease pathophysiology methylmalonic acidemia has yet to be fully elucidated. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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22 pages, 2491 KiB

Open AccessArticle

Deferasirox-Dependent Iron Chelation Enhances Mitochondrial Dysfunction and Restores p53 Signaling by Stabilization of p53 Family Members in Leukemic Cells

by Chiara Calabrese, Cristina Panuzzo, Serena Stanga, Giacomo Andreani, Silvia Ravera, Alessandro Maglione, Lucrezia Pironi, Jessica Petiti, Muhammad Shahzad Ali, Patrizia Scaravaglio, Francesca Napoli, Carmen Fava, Marco De Gobbi, Francesco Frassoni, Giuseppe Saglio, Enrico Bracco, Barbara Pergolizzi and Daniela Cilloni

Int. J. Mol. Sci. 2020, 21(20), 7674; https://doi.org/10.3390/ijms21207674 - 16 Oct 2020

Cited by 15 | Viewed by 3688

Abstract

Iron is crucial to satisfy several mitochondrial functions including energy metabolism and oxidative phosphorylation. Patients affected by Myelodysplastic Syndromes (MDS) and acute myeloid leukemia (AML) are frequently characterized by iron overload (IOL), due to continuous red blood cell (RBC) transfusions. This event impacts the overall survival (OS) and it is associated with increased mortality in lower-risk MDS patients. Accordingly, the oral iron chelator Deferasirox (DFX) has been reported to improve the OS and delay leukemic transformation. However, the molecular players and the biological mechanisms laying behind remain currently mostly undefined. The aim of this study has been to investigate the potential anti-leukemic effect of DFX, by functionally and molecularly analyzing its effects in three different leukemia cell lines, harboring or not p53 mutations, and in human primary cells derived from 15 MDS/AML patients. Our findings indicated that DFX can lead to apoptosis, impairment of cell growth only in a context of IOL, and can induce a significant alteration of mitochondria network, with a sharp reduction in mitochondrial activity. Moreover, through a remarkable reduction of Murine Double Minute 2 (MDM2), known to regulate the stability of p53 and p73 proteins, we observed an enhancement of p53 transcriptional activity after DFX. Interestingly, this iron depletion-triggered signaling is enabled by p73, in the absence of p53, or in the presence of a p53 mutant form. In conclusion, we propose a mechanism by which the increased p53 family transcriptional activity and protein stability could explain the potential benefits of iron chelation therapy in terms of improving OS and delaying leukemic transformation. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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13 pages, 1619 KiB

Open AccessArticle

Assessment of Mitochondrial Dysfunction in Experimental Autoimmune Encephalomyelitis (EAE) Models of Multiple Sclerosis

by Xiulin Ng, Mona Sadeghian, Simon Heales and Iain P. Hargreaves

Int. J. Mol. Sci. 2019, 20(20), 4975; https://doi.org/10.3390/ijms20204975 - 9 Oct 2019

Cited by 14 | Viewed by 2998

Abstract

Multiple sclerosis (MS) is an inflammatory demyelinating disease of the central nervous system (CNS) that involves the autoreactive T-cell attack on axonal myelin sheath. Lesions or plaques formed as a result of repeated damage and repair mechanisms lead to impaired relay of electrical impulses along the nerve, manifesting as clinical symptoms of MS. Evidence from studies in experimental autoimmune encephalomyelitis (EAE) models of MS strongly suggests that mitochondrial dysfunction presents at the onset of disease and throughout the disease course. The aim of this study was to determine if mitochondrial dysfunction occurs before clinical symptoms arise, and whether this is confined to the CNS. EAE was induced in C57B/L6 mice, and citrate synthase and mitochondrial respiratory chain (MRC) complex I–IV activities were assayed at presymptomatic (3 or 10 days post first immunisation (3 or 10 DPI)) and asymptomatic (17 days post first immunisation (17 DPI) time-points in central nervous system (CNS; spinal cord) and peripheral (liver and jaw muscle) tissues. Samples from animals immunised with myelin oligodendrocyte glycoprotein (MOG) as EAE models were compared with control animals immunised with adjuvant (ADJ) only. Significant changes in MOG compared to control ADJ animals in MRC complex I activity occurred only at presymptomatic stages, with an increase in the spinal cord at 10 DPI (87.9%), an increase at 3 DPI (25.6%) and decrease at 10 DPI (22.3%) in the jaw muscle, and an increase in the liver at 10 DPI (71.5%). MRC complex II/III activity changes occurred at presymptomatic and the asymptomatic stages of the disease, with a decrease occurring in the spinal cord at 3 DPI (87.6%) and an increase at 17 DPI (36.7%), increase in the jaw muscle at 10 DPI (25.4%), and an increase at 3 DPI (75.2%) and decrease at 17 DPI (95.7%) in the liver. Citrate synthase activity was also significantly decreased at 10 DPI (27.3%) in the liver. No significant changes were observed in complex IV across all three tissues assayed. Our findings reveal evidence that mitochondrial dysfunction is present at the asymptomatic stages in the EAE model of MS, and that the changes in MRC enzyme activities are tissue-specific and are not confined to the CNS. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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15 pages, 1997 KiB

Open AccessArticle

Exogenous Iron Increases Fasciocidal Activity and Hepatocellular Toxicity of the Synthetic Endoperoxides OZ78 and MT04

by Karin Brecht, Carla Kirchhofer, Jamal Bouitbir, Francesca Trapani, Jennifer Keiser and Stephan Krähenbühl

Int. J. Mol. Sci. 2019, 20(19), 4880; https://doi.org/10.3390/ijms20194880 - 1 Oct 2019

Cited by 10 | Viewed by 2347

Abstract

The synthetic peroxides OZ78 and MT04 recently emerged as fasciocidal drug candidates. However, the effect of iron on fasciocidal activity and hepatocellular toxicity of these compounds is unknown. We investigated the in vitro fasciocidal activity and hepatocellular toxicity of OZ78 and MT04 in absence and presence of Fe(II)chloride and hemin, and conducted a toxicological study in mice. Studies were performed in comparison with the antimalarial artesunate (AS), a semisynthetic peroxide. Fasciocidal effects of OZ78 and MT04 were confirmed and enhanced by Fe²⁺ or hemin. In HepG2 cells, AS reduced cellular ATP and impaired membrane integrity concentration-dependently. In comparison, OZ78 or MT04 were not toxic at 100 µM and reduced the cellular ATP by 13% and 19%, respectively, but were not membrane-toxic at 500 µM. The addition of Fe²⁺ or hemin increased the toxicity of OZ78 and MT04 significantly. AS inhibited complex I, II, and IV of the mitochondrial electron transport chain, and MT04 impaired complex I and II, whereas OZ78 was not toxic. All three compounds increased cellular reactive oxygen species (ROS) concentration-dependently, with a further increase by Fe²⁺ or hemin. Mice treated orally with up to 800 mg OZ78, or MT04 showed no relevant hepatotoxicity. In conclusion, we confirmed fasciocidal activity of OZ78 and MT04, which was increased by Fe²⁺ or hemin. OZ78 and MT04 were toxic to HepG2 cells, which was explained by mitochondrial damage associated with ROS generation in the presence of iron. No relevant hepatotoxicity was observed in mice in vivo, possibly due to limited exposure and/or high antioxidative hepatic capacity. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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14 pages, 1928 KiB

Open AccessArticle

Inhibition of Mitochondrial Complex I Impairs Release of α-Galactosidase by Jurkat Cells

by Jonathan R. A. Lambert, Steven J. Howe, Ahad A. Rahim, Derek G. Burke and Simon J. R. Heales

Int. J. Mol. Sci. 2019, 20(18), 4349; https://doi.org/10.3390/ijms20184349 - 5 Sep 2019

Cited by 2 | Viewed by 3431

Abstract

Fabry disease (FD) is caused by mutations in the GLA gene that encodes lysosomal α-galactosidase-A (α-gal-A). A number of pathogenic mechanisms have been proposed and these include loss of mitochondrial respiratory chain activity. For FD, gene therapy is beginning to be applied as a treatment. In view of the loss of mitochondrial function reported in FD, we have considered here the impact of loss of mitochondrial respiratory chain activity on the ability of a GLA lentiviral vector to increase cellular α-gal-A activity and participate in cross correction. Jurkat cells were used in this study and were exposed to increasing viral copies. Intracellular and extracellular enzyme activities were then determined; this in the presence or absence of the mitochondrial complex I inhibitor, rotenone. The ability of cells to take up released enzyme was also evaluated. Increasing transgene copies was associated with increasing intracellular α-gal-A activity but this was associated with an increase in Km. Release of enzyme and cellular uptake was also demonstrated. However, in the presence of rotenone, enzyme release was inhibited by 37%. Excessive enzyme generation may result in a protein with inferior kinetic properties and a background of compromised mitochondrial function may impair the cross correction process. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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20 pages, 2651 KiB

Open AccessArticle

Integrated Approach Reveals Role of Mitochondrial Germ-Line Mutation F18L in Respiratory Chain, Oxidative Alterations, Drug Sensitivity, and Patient Prognosis in Glioblastoma

by Kathleen Keatley, Samuel Stromei-Cleroux, Tammy Wiltshire, Nina Rajala, Gary Burton, William V. Holt, D. Timothy J. Littlewood, Andrew G. Briscoe, Josephine Jung, Keyoumars Ashkan, Simon J. Heales, Geoffrey J. Pilkington, Brigitte Meunier, John E. McGeehan, Iain P. Hargreaves and Rhiannon E. McGeehan

Int. J. Mol. Sci. 2019, 20(13), 3364; https://doi.org/10.3390/ijms20133364 - 9 Jul 2019

Cited by 10 | Viewed by 4544

Abstract

Glioblastoma is the most common and malignant primary brain tumour in adults, with a dismal prognosis. This is partly due to considerable inter- and intra-tumour heterogeneity. Changes in the cellular energy-producing mitochondrial respiratory chain complex (MRC) activities are a hallmark of glioblastoma relative to the normal brain, and associate with differential survival outcomes. Targeting MRC complexes with drugs can also facilitate anti-glioblastoma activity. Whether mutations in the mitochondrial DNA (mtDNA) that encode several components of the MRC contribute to these phenomena remains underexplored. We identified a germ-line mtDNA mutation (m. 14798T > C), enriched in glioblastoma relative to healthy controls, that causes an amino acid substitution F18L within the core mtDNA-encoded cytochrome b subunit of MRC complex III. F18L is predicted to alter corresponding complex III activity, and sensitivity to complex III-targeting drugs. This could in turn alter reactive oxygen species (ROS) production, cell behaviour and, consequently, patient outcomes. Here we show that, despite a heterogeneous mitochondrial background in adult glioblastoma patient biopsy-derived cell cultures, the F18L substitution associates with alterations in individual MRC complex activities, in particular a 75% increase in MRC complex II_III activity, and a 34% reduction in CoQ10, the natural substrate for MRC complex III, levels. Downstream characterisation of an F18L-carrier revealed an 87% increase in intra-cellular ROS, an altered cellular distribution of mitochondrial-specific ROS, and a 64% increased sensitivity to clomipramine, a repurposed MRC complex III-targeting drug. In patients, F18L-carriers that received the current standard of care treatment had a poorer prognosis than non-carriers (373 days vs. 415 days, respectively). Single germ-line mitochondrial mutations could predispose individuals to differential prognoses, and sensitivity to mitochondrial targeted drugs. Thus, F18L, which is present in blood could serve as a useful non-invasive biomarker for the stratification of patients into prognostically relevant groups, one of which requires a lower dose of clomipramine to achieve clinical effect, thus minimising side-effects. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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15 pages, 4263 KiB

Open AccessArticle

Proteomics Analysis of Tangeretin-Induced Apoptosis through Mitochondrial Dysfunction in Bladder Cancer Cells

by Jen-Jie Lin, Chun-Chieh Huang, Yu-Li Su, Hao-Lun Luo, Nai-Lun Lee, Ming-Tse Sung and Yu-Jen Wu

Int. J. Mol. Sci. 2019, 20(5), 1017; https://doi.org/10.3390/ijms20051017 - 26 Feb 2019

Cited by 19 | Viewed by 4813

Abstract

Tangeretin is one of the most abundant compounds in citrus peel, and studies have shown that it possesses anti-oxidant and anti-cancer properties. However, no study has been conducted on bladder cancer cells. Bladder cancer has the second highest mortality rate among urological cancers and is the fifth most common malignancy in the world. Currently, combination chemotherapy is the most common approach by which to treat patients with bladder cancer, and thus identifying more effective chemotherapeutic agents that can be safely administered to patients is a very important research issue. Therefore, this study investigated whether tangeretin can induce apoptosis and identified the signaling pathways of tangeretin-induced apoptosis in human bladder cancer cells using two-dimensional gel electrophoresis (2DGE). The results of the study demonstrated that 60 μM tangeretin reduced the cell survival of a BFTC-905 bladder carcinoma cell line by 42%, and induced early and late apoptosis in the cells. In this study 2DGE proteomics technology identified 41 proteins that were differentially-expressed in tangeretin-treated cells, and subsequently LC–MS/MS analysis was performed to identify the proteins. Based on the functions of the differentially-expressed proteins, the results suggested that tangeretin caused mitochondrial dysfunction and further induced apoptosis in bladder cancer cells. Moreover, western blotting analysis demonstrated that tangeretin treatment disturbed calcium homeostasis in the mitochondria, triggered cytochrome C release, and activated caspase-3 and caspase-9, which led to apoptosis. In conclusion, our results showed that tangeretin-induced apoptosis in human bladder cancer cells is mediated by mitochondrial inactivation, suggesting that tangeretin has the potential to be developed as a new drug for the treatment of bladder cancer. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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17 pages, 2324 KiB

Open AccessArticle

Interaction of Diet and Ozone Exposure on Oxidative Stress Parameters within Specific Brain Regions of Male Brown Norway Rats

by Joseph M. Valdez, Andrew F. M. Johnstone, Judy E. Richards, Judith E. Schmid, Joyce E. Royland and Prasada Rao S. Kodavanti

Int. J. Mol. Sci. 2019, 20(1), 11; https://doi.org/10.3390/ijms20010011 - 20 Dec 2018

Cited by 11 | Viewed by 3658

Abstract

Oxidative stress (OS) contributes to the neurological and cardio/pulmonary effects caused by adverse metabolic states and air pollutants such as ozone (O₃). This study explores the interactive effects of O₃ and diet (high-fructose (FRUC) or high–fat (FAT)) on OS in different rat brain regions. In acute exposure, there was a decrease in markers of reactive oxygen species (ROS) production in some brain regions by diet and not by O₃. Total antioxidant substances (TAS) were increased in the cerebellum (CER) and frontal cortex (FC) and decreased in the striatum (STR) by both diets irrespective of O₃ exposure. Protein carbonyls (PC) and total aconitase decreased in some brain regions irrespective of exposure. Following subacute exposure, an increase in markers of ROS was observed in both diet groups. TAS was increased in the FC (FAT only) and there was a clear O₃ effect where TAS was increased in the FC and STR. Diet increased PC formation within the CER in the FAT group, while the hippocampus showed a decrease in PC after O₃ exposure in controls. In general, these results indicate that diet/O₃ did not have a global effect on brain OS parameters, but showed some brain region- and OS parameter-specific effects by diets. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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Review

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23 pages, 682 KiB

Open AccessReview

Transcription, Processing, and Decay of Mitochondrial RNA in Health and Disease

by Arianna Barchiesi and Carlo Vascotto

Int. J. Mol. Sci. 2019, 20(9), 2221; https://doi.org/10.3390/ijms20092221 - 6 May 2019

Cited by 49 | Viewed by 13146

Abstract

Although the large majority of mitochondrial proteins are nuclear encoded, for their correct functioning mitochondria require the expression of 13 proteins, two rRNA, and 22 tRNA codified by mitochondrial DNA (mtDNA). Once transcribed, mitochondrial RNA (mtRNA) is processed, mito-ribosomes are assembled, and mtDNA-encoded proteins belonging to the respiratory chain are synthesized. These processes require the coordinated spatio-temporal action of several enzymes, and many different factors are involved in the regulation and control of protein synthesis and in the stability and turnover of mitochondrial RNA. In this review, we describe the essential steps of mitochondrial RNA synthesis, maturation, and degradation, the factors controlling these processes, and how the alteration of these processes is associated with human pathologies. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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18 pages, 1056 KiB

Open AccessReview

Dietary Macronutrient Management to Treat Mitochondrial Dysfunction in Parkinson’s Disease

by Rijan Bajracharya, Neil A. Youngson and J. William O. Ballard

Int. J. Mol. Sci. 2019, 20(8), 1850; https://doi.org/10.3390/ijms20081850 - 15 Apr 2019

Cited by 15 | Viewed by 7421

Abstract

Mitochondrial dysfunction has been demonstrated to play an important role in the pathogenesis of Parkinson’s disease (PD). The products of several PD-associated genes, including alpha-synuclein, parkin, pink1, protein deglycase DJ-1, and leucine rich repeat kinase 2, have important roles in mitochondrial biology. Thus, modifying mitochondrial function could be a potential therapeutic strategy for PD. Dietary management can alter mitochondrial function as shifts in dietary macronutrients and their ratios in food can alter mitochondrial energy metabolism, morphology and dynamics. Our studies have established that a low protein to carbohydrate (P:C) ratio can increase lifespan, motor ability and mitochondrial function in a parkin mutant Drosophila model of PD. In this review, we describe mitochondrial dysfunction in PD patients and models, and dietary macronutrient management strategies to reverse it. We focus on the effects of protein, carbohydrate, fatty acids, and their dietary ratios. In addition, we propose potential mechanisms that can improve mitochondrial function and thus reverse or delay the onset of PD. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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12 pages, 1457 KiB

Open AccessReview

Mitochondria Are Important Determinants of the Aging of Seeds

by Ewelina Ratajczak, Arleta Małecka, Iwona Ciereszko and Aleksandra M. Staszak

Int. J. Mol. Sci. 2019, 20(7), 1568; https://doi.org/10.3390/ijms20071568 - 28 Mar 2019

Cited by 51 | Viewed by 6590

Abstract

Seeds enable plant survival in harsh environmental conditions, and via seeds, genetic information is transferred from parents to the new generation; this stage provides an opportunity for sessile plants to settle in new territories. However, seed viability decreases over long-term storage due to seed aging. For the effective conservation of gene resources, e.g., in gene banks, it is necessary to understand the causes of decreases in seed viability, not only where the aging process is initiated in seeds but also the sequence of events of this process. Mitochondria are the main source of reactive oxygen species (ROS) production, so they are more quickly and strongly exposed to oxidative damage than other organelles. The mitochondrial antioxidant system is also less active than the antioxidant systems of other organelles, thus such mitochondrial ‘defects’ can strongly affect various cell processes, including seed aging, which we discuss in this paper. Full article

(This article belongs to the Special Issue Mitochondrial Dysfunction and Oxidative Damage)

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