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Mitochondrial Redox Regulations

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A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Health Outcomes of Antioxidants and Oxidative Stress".

Deadline for manuscript submissions: closed (31 August 2021) | Viewed by 53577

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Prof. Dr. Petr Ježek

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Department of Mitochondrial Physiology, No. 75, Institute of Physiology, The Czech Academy of Sciences, Prague, Czech Republic
Interests: mitochondria; redox signaling; pancreatic beta cells; specific cancer metabolism; mitochondrial ultrastructure

Special Issue Information

Dear Colleagues,

Mitochondria are recognized as a metabolic hub, but also as the redox hub, controlling cell fate and emanating superoxide/H₂O₂, which in a regulated form can be regarded as redox signaling. Retrograde redox signaling from the mitochondrion can be directed towards the cell cytosol, nucleus, plasma membrane or other cell components. It is executed via the H₂O₂ diffusion or by redox relaying enzymes, such as peroxiredoxins. In addition to redox-sensitive kinases and phosphatases, prominent receivers of the redox signal are extracellular matrix metaloproteinases, redox-sensitive channels and, upon hypoxia, also inhibitable proline hydroxylase domain enzymes (PHD/EglN, plus FIH), leading to HIF-1α accumulation and resulting transcriptome reprogramming. An opposite redox signaling direction is represented by the external redox signaling from the cell towards the mitochondrion, including H₂O₂ activation of kinases within the intracristal space, likewise leading to, e.g., sulfenylation of critical cysteines in mitochondrial proteins. Finally, intra-mitochondrial redox signaling exists just within the interior of the outer mitochondrial membrane, exemplified by acetylation of MnSOD making it inactive, or by the H₂O₂-activated phospholipase iPLA2γ; and by a plethora of situations of elevated superoxide leading to the initiation of apoptosis. Coverage of these topics is welcome for this Special Issue, including both reviews and experimental articles.

Prof. Dr. Petr Ježek
Guest Editor

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Keywords

Redox signaling to and from mitochondrion
Physiological mitochondrial redox homeostasis
Mitochondrial redox biology of diseases

Published Papers (12 papers)

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Editorial

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2 pages, 176 KiB

Open AccessEditorial

Mitochondrial Redox Regulations and Redox Biology of Mitochondria

by Petr Ježek

Antioxidants 2021, 10(12), 1921; https://doi.org/10.3390/antiox10121921 - 29 Nov 2021

Cited by 5 | Viewed by 1595

Abstract

Mitochondria undoubtedly represent a metabolic hub, but also act as a redox hub, controlling cell fate and emanating superoxide/H₂O₂, which in a regulated form and timing provide redox signaling [...] Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

Research

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17 pages, 4075 KiB

Open AccessArticle

FRI-1 Is an Anti-Cancer Isoquinolinequinone That Inhibits the Mitochondrial Bioenergetics and Blocks Metabolic Shifts by Redox Disruption in Breast Cancer Cells

by Miguel Córdova-Delgado, Sebastián Fuentes-Retamal, Charlotte Palominos, Camila López-Torres, Daniela Guzmán-Rivera, Oney Ramírez-Rodríguez, Ramiro Araya-Maturana and Félix A. Urra

Antioxidants 2021, 10(10), 1618; https://doi.org/10.3390/antiox10101618 - 14 Oct 2021

Cited by 11 | Viewed by 2625

Abstract

Since breast cancer (BC) cells are dependent on mitochondrial bioenergetics for promoting proliferation, survival, and metastasis, mitochondria highlight as an important target for anticancer drug discovery. FRI-1, methyl 1, 3-dimethyl-5, 8-dioxo-5, 8-dihydro-4-isoquinolinecarboxylate, was previously described as a selective cytotoxic compound on cancer cell lines, however, details on the mechanism of action remain unknown. In this work, we describe that FRI-1 inhibits mitochondrial bioenergetics, producing apoptosis in MCF7 and MDA-MB-231 BC cell lines. FRI-1 decreases the maximal oxygen consumption rate (OCR), Δψm, NADH, and ATP levels, with a notable increase of mitochondrial reactive oxygen species (ROS) production, promoting AMPK activation with pro-survival effects. Moreover, FRI-1 inhibits the metabolic remodeling to glycolysis induced by oligomycin. In isolated tumoral mitochondria, FRI-1 increases Complex I and III-dependent OCR state 2, and this is sensitive to rotenone and antimycin A inhibitor additions, suggesting a redox cycling event. Remarkably, α-ketoglutarate and lipoic acid supplementation reversed and promoted, respectively, the FRI-1-induced apoptosis, suggesting that mitochondrial redox disruption affects 2-oxoglutarate dehydrogenase (OGDH) activity, and this is involved in their anticancer mechanism. Consistent with this, the combination of FRI-1 and CPI-613, a dual inhibitor of redox-sensible tricarboxylic acid (TCA) cycle enzymes PDH and OGDH, produced extensive BC cell death. Taken together, our results suggest that FRI-1 exhibits anticancer effects through inhibition of mitochondrial bioenergetics by redox disruption in BC cells. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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14 pages, 1385 KiB

Open AccessArticle

Effect of Chronic Stress Present in Fibroblasts Derived from Patients with a Sporadic Form of AD on Mitochondrial Function and Mitochondrial Turnover

by Karolina Drabik, Dominika Malińska, Karolina Piecyk, Grażyna Dębska-Vielhaber, Stefan Vielhaber, Jerzy Duszyński and Joanna Szczepanowska

Antioxidants 2021, 10(6), 938; https://doi.org/10.3390/antiox10060938 - 10 Jun 2021

Cited by 10 | Viewed by 2623

Abstract

Although the sporadic form of Alzheimer’s disease (AD) is the prevalent form, the cellular events underlying the disease pathogenesis have not been fully characterized. Accumulating evidence points to mitochondrial dysfunction as one of the events responsible for AD progression. We investigated mitochondrial function in fibroblasts collected from patients diagnosed with the sporadic form of AD (sAD), placing a particular focus on mitochondrial turnover. We measured mitochondrial biogenesis and autophagic clearance, and evaluated the presence of bioenergetic stress in sAD cells. The mitochondrial turnover was clearly lower in the fibroblasts from sAD patients than in the fibroblasts from the control subjects, and the levels of many proteins regulating mitochondrial biogenesis, autophagy and mitophagy were decreased in patient cells. Additionally, the sAD fibroblasts had slightly higher mitochondrial superoxide levels and impaired antioxidant defense. Mitochondrial turnover undergoes feedback regulation through mitochondrial retrograde signaling, which is responsible for the maintenance of optimal mitochondrial functioning, and mitochondria-derived ROS participate as signaling molecules in this process. Our results showed that in sAD patients cells, there is a shift in the balance of mitochondrial function, possibly in response to the presence of cellular stress related to disease development. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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12 pages, 2050 KiB

Open AccessArticle

Antiplatelet Activity of Isorhamnetin via Mitochondrial Regulation

by Lyanne Rodríguez, Lina Badimon, Diego Méndez, Teresa Padró, Gemma Vilahur, Esther Peña, Basilio Carrasco, Hermine Vogel, Iván Palomo and Eduardo Fuentes

Antioxidants 2021, 10(5), 666; https://doi.org/10.3390/antiox10050666 - 25 Apr 2021

Cited by 22 | Viewed by 2752

Abstract

With the diet, we ingest nutrients capable of modulating platelet function, which plays a crucial role in developing cardiovascular events, one of the leading causes of mortality worldwide. Studies that demonstrate the antiplatelet and antithrombotic potential of bioactive compounds are vital to maintaining good cardiovascular health. In this work, we evaluate the flavonol isorhamnetin’s antiplatelet effect on human platelets, using collagen, thrombin receptor activator peptide 6 (TRAP-6), and phorbol myristate acetate (PMA) as agonists. Isorhamnetin induced a significant inhibition on collagen- and TRAP-6-induced platelet aggregation, with half-maximum inhibitory concentration (IC₅₀) values of 8.1 ± 2.6 and 16.1 ± 11.1 µM, respectively; while it did not show cytotoxic effect. Isorhamnetin reduced adenosine triphosphate levels (ATP) in platelets stimulated by collagen and TRAP-6. We also evidenced that isorhamnetin’s antiplatelet activity was related to the inhibition of mitochondrial function without effect on reactive oxygen species (ROS) levels. Additionally, we investigated isorhamnetin’s effect on thrombus formation in vitro under flow conditions on the damaged vessel wall. In this context, we demonstrate that isorhamnetin at 20 µM induced a significant inhibition on platelet deposition, confirming its antithrombotic effect. Our findings corroborate the antiplatelet and antithrombotic potential of isorhamnetin present in many foods of daily consumption. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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11 pages, 1595 KiB

Open AccessArticle

The Relationship between Mitochondrial Reactive Oxygen Species Production and Mitochondrial Energetics in Rat Tissues with Different Contents of Reduced Coenzyme Q

by Karolina Dominiak and Wieslawa Jarmuszkiewicz

Antioxidants 2021, 10(4), 533; https://doi.org/10.3390/antiox10040533 - 29 Mar 2021

Cited by 12 | Viewed by 2089

Abstract

We investigated the relationship between mitochondrial production of reactive oxygen species (ROS) and mitochondrial energetics in various rat tissues with different contents of the reduced coenzyme Q (Q) pool (Q9 + Q10). Our results indicate that similar to the tissue level, mitochondrial H₂O₂ release under nonphosphorylating conditions was strongly dependent on the amount of the reduced Q pool. Namely, in brain and lung mitochondria, less H₂O₂ release corresponded to a less reduced Q pool, while in liver and heart mitochondria, higher H₂O₂ release corresponded to a more reduced Q pool. We can conclude that the differences observed in rat tissues in the size of the reduced Q pool reflect different levels of ROS production and hence may reflect different demands for reduced Q as an antioxidant. Moreover, differences in mitochondrial H₂O₂ release were observed in different types of rat mitochondria during the oxidation of succinate (complex II substrate), malate plus glutamate (complex I substrate), and their mixture under phosphorylating and nonphosphorylating conditions. Our results indicate the existence of a tissue-specific maximum respiratory chain capacity in ROS production, possibly related to the membrane potential-mediated control of oxidative phosphorylation. We propose the use of a new parameter for the study of isolated mitochondria, RCR_ROS, the ratio between the formation of mitochondrial ROS under nonphosphorylating and phosphorylating conditions, which represents the maximum factorial increase in mitochondrial ROS formation that can be achieved after all ADP is phosphorylated. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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Review

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25 pages, 4338 KiB

Open AccessReview

Antioxidant Synergy of Mitochondrial Phospholipase PNPLA8/iPLA2γ with Fatty Acid–Conducting SLC25 Gene Family Transporters

by Martin Jabůrek, Pavla Průchová, Blanka Holendová, Alexander Galkin and Petr Ježek

Antioxidants 2021, 10(5), 678; https://doi.org/10.3390/antiox10050678 - 26 Apr 2021

Cited by 13 | Viewed by 3433

Abstract

Patatin-like phospholipase domain-containing protein PNPLA8, also termed Ca²⁺-independent phospholipase A2γ (iPLA2γ), is addressed to the mitochondrial matrix (or peroxisomes), where it may manifest its unique activity to cleave phospholipid side-chains from both sn-1 and sn-2 positions, consequently releasing either saturated or unsaturated fatty acids (FAs), including oxidized FAs. Moreover, iPLA2γ is directly stimulated by H₂O₂ and, hence, is activated by redox signaling or oxidative stress. This redox activation permits the antioxidant synergy with mitochondrial uncoupling proteins (UCPs) or other SLC25 mitochondrial carrier family members by FA-mediated protonophoretic activity, termed mild uncoupling, that leads to diminishing of mitochondrial superoxide formation. This mechanism allows for the maintenance of the steady-state redox status of the cell. Besides the antioxidant role, we review the relations of iPLA2γ to lipid peroxidation since iPLA2γ is alternatively activated by cardiolipin hydroperoxides and hypothetically by structural alterations of lipid bilayer due to lipid peroxidation. Other iPLA2γ roles include the remodeling of mitochondrial (or peroxisomal) membranes and the generation of specific lipid second messengers. Thus, for example, during FA β-oxidation in pancreatic β-cells, H₂O₂-activated iPLA2γ supplies the GPR40 metabotropic FA receptor to amplify FA-stimulated insulin secretion. Cytoprotective roles of iPLA2γ in the heart and brain are also discussed. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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19 pages, 2601 KiB

Open AccessReview

The Mia40/CHCHD4 Oxidative Folding System: Redox Regulation and Signaling in the Mitochondrial Intermembrane Space

by Eleanor Dickson-Murray, Kenza Nedara, Nazanine Modjtahedi and Kostas Tokatlidis

Antioxidants 2021, 10(4), 592; https://doi.org/10.3390/antiox10040592 - 12 Apr 2021

Cited by 15 | Viewed by 4430

Abstract

Mitochondria are critical for several cellular functions as they control metabolism, cell physiology, and cell death. The mitochondrial proteome consists of around 1500 proteins, the vast majority of which (about 99% of them) are encoded by nuclear genes, with only 13 polypeptides in human cells encoded by mitochondrial DNA. Therefore, it is critical for all the mitochondrial proteins that are nuclear-encoded to be targeted precisely and sorted specifically to their site of action inside mitochondria. These processes of targeting and sorting are catalysed by protein translocases that operate in each one of the mitochondrial sub-compartments. The main protein import pathway for the intermembrane space (IMS) recognises proteins that are cysteine-rich, and it is the only import pathway that chemically modifies the imported precursors by introducing disulphide bonds to them. In this manner, the precursors are trapped in the IMS in a folded state. The key component of this pathway is Mia40 (called CHCHD4 in human cells), which itself contains cysteine motifs and is subject to redox regulation. In this review, we detail the basic components of the MIA pathway and the disulphide relay mechanism that underpins the electron transfer reaction along the oxidative folding mechanism. Then, we discuss the key protein modulators of this pathway and how they are interlinked to the small redox-active molecules that critically affect the redox state in the IMS. We present also evidence that the mitochondrial redox processes that are linked to iron–sulfur clusters biogenesis and calcium homeostasis coalesce in the IMS at the MIA machinery. The fact that the MIA machinery and several of its interactors and substrates are linked to a variety of common human diseases connected to mitochondrial dysfunction highlight the potential of redox processes in the IMS as a promising new target for developing new treatments for some of the most complex and devastating human diseases. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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13 pages, 5484 KiB

Open AccessFeature PaperReview

Mitochondria and the Frozen Frog

by Janet M. Storey, Shaobo Wu and Kenneth B. Storey

Antioxidants 2021, 10(4), 543; https://doi.org/10.3390/antiox10040543 - 1 Apr 2021

Cited by 19 | Viewed by 7253

Abstract

The wood frog, Rana sylvatica, is the best-studied of a small group of amphibian species that survive whole body freezing during the winter months. These frogs endure the freezing of 65–70% of their total body water in extracellular ice masses. They have implemented multiple adaptations that manage ice formation, deal with freeze-induced ischemia/reperfusion stress, limit cell volume reduction with the production of small molecule cryoprotectants (glucose, urea) and adjust a wide variety of metabolic pathways for prolonged life in a frozen state. All organs, tissues, cells and intracellular organelles are affected by freeze/thaw and its consequences. This article explores mitochondria in the frozen frog with a focus on both the consequences of freezing (e.g., anoxia/ischemia, cell volume reduction) and mitigating defenses (e.g., antioxidants, chaperone proteins, upregulation of mitochondria-encoded genes, enzyme regulation, etc.) in order to identify adaptive strategies that defend and adapt mitochondria in animals that can be frozen for six months or more every year. A particular focus is placed on freeze-responsive genes in wood frogs that are encoded on the mitochondrial genome including ATP6/8, ND4 and 16S RNA. These were strongly up-regulated during whole body freezing (24 h at −2.5 °C) in the liver and brain but showed opposing responses to two component stresses: strong upregulation in response to anoxia but no response to dehydration stress. This indicates that freeze-responsive upregulation of mitochondria-encoded genes is triggered by declining oxygen and likely has an adaptive function in supporting cellular energetics under indeterminate lengths of whole body freezing. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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30 pages, 3135 KiB

Open AccessReview

Redox Homeostasis in Pancreatic β-Cells: From Development to Failure

by Štěpánka Benáková, Blanka Holendová and Lydie Plecitá-Hlavatá

Antioxidants 2021, 10(4), 526; https://doi.org/10.3390/antiox10040526 - 27 Mar 2021

Cited by 23 | Viewed by 4398

Abstract

Redox status is a key determinant in the fate of β-cell. These cells are not primarily detoxifying and thus do not possess extensive antioxidant defense machinery. However, they show a wide range of redox regulating proteins, such as peroxiredoxins, thioredoxins or thioredoxin reductases, etc., being functionally compartmentalized within the cells. They keep fragile redox homeostasis and serve as messengers and amplifiers of redox signaling. β-cells require proper redox signaling already in cell ontogenesis during the development of mature β-cells from their progenitors. We bring details about redox-regulated signaling pathways and transcription factors being essential for proper differentiation and maturation of functional β-cells and their proliferation and insulin expression/maturation. We briefly highlight the targets of redox signaling in the insulin secretory pathway and focus more on possible targets of extracellular redox signaling through secreted thioredoxin1 and thioredoxin reductase1. Tuned redox homeostasis can switch upon chronic pathological insults towards the dysfunction of β-cells and to glucose intolerance. These are characteristics of type 2 diabetes, which is often linked to chronic nutritional overload being nowadays a pandemic feature of lifestyle. Overcharged β-cell metabolism causes pressure on proteostasis in the endoplasmic reticulum, mainly due to increased demand on insulin synthesis, which establishes unfolded protein response and insulin misfolding along with excessive hydrogen peroxide production. This together with redox dysbalance in cytoplasm and mitochondria due to enhanced nutritional pressure impact β-cell redox homeostasis and establish prooxidative metabolism. This can further affect β-cell communication in pancreatic islets through gap junctions. In parallel, peripheral tissues losing insulin sensitivity and overall impairment of glucose tolerance and gut microbiota establish local proinflammatory signaling and later systemic metainflammation, i.e., low chronic inflammation prooxidative properties, which target β-cells leading to their dedifferentiation, dysfunction and eventually cell death. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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18 pages, 1916 KiB

Open AccessReview

Transcriptional Regulation of ROS Homeostasis by the ERR Subfamily of Nuclear Receptors

by Charlotte Scholtes and Vincent Giguère

Antioxidants 2021, 10(3), 437; https://doi.org/10.3390/antiox10030437 - 12 Mar 2021

Cited by 16 | Viewed by 4084

Abstract

Reactive oxygen species (ROS) such as superoxide anion (O₂^•−) and hydrogen peroxide (H₂O₂) are generated endogenously by processes such as mitochondrial oxidative phosphorylation, or they may arise from exogenous sources like bacterial invasion. ROS can be beneficial (oxidative eustress) as signaling molecules but also harmful (oxidative distress) to cells when ROS levels become unregulated in response to physiological, pathological or pharmacological insults. Indeed, abnormal ROS levels have been shown to contribute to the etiology of a wide variety of diseases. Transcriptional control of metabolic genes is a crucial mechanism to coordinate ROS homeostasis. Therefore, a better understanding of how ROS metabolism is regulated by specific transcription factors can contribute to uncovering new therapeutic strategies. A large body of work has positioned the estrogen-related receptors (ERRs), transcription factors belonging to the nuclear receptor superfamily, as not only master regulators of cellular energy metabolism but, most recently, of ROS metabolism. Herein, we will review the role played by the ERRs as transcriptional regulators of ROS generation and antioxidant mechanisms and also as ROS sensors. We will assess how the control of ROS homeostasis by the ERRs can be linked to physiology and disease and the possible contribution of manipulating ERR activity in redox medicine. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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18 pages, 8819 KiB

Open AccessReview

Generation of Reactive Oxygen Species by Mitochondria

by Pablo Hernansanz-Agustín and José Antonio Enríquez

Antioxidants 2021, 10(3), 415; https://doi.org/10.3390/antiox10030415 - 9 Mar 2021

Cited by 129 | Viewed by 11582

Abstract

Reactive oxygen species (ROS) are series of chemical products originated from one or several electron reductions of oxygen. ROS are involved in physiology and disease and can also be both cause and consequence of many biological scenarios. Mitochondria are the main source of ROS in the cell and, particularly, the enzymes in the electron transport chain are the major contributors to this phenomenon. Here, we comprehensively review the modes by which ROS are produced by mitochondria at a molecular level of detail, discuss recent advances in the field involving signalling and disease, and the involvement of supercomplexes in these mechanisms. Given the importance of mitochondrial ROS, we also provide a schematic guide aimed to help in deciphering the mechanisms involved in their production in a variety of physiological and pathological settings. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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59 pages, 13996 KiB

Open AccessReview

The Pancreatic β-Cell: The Perfect Redox System

by Petr Ježek, Blanka Holendová, Martin Jabůrek, Jan Tauber, Andrea Dlasková and Lydie Plecitá-Hlavatá

Antioxidants 2021, 10(2), 197; https://doi.org/10.3390/antiox10020197 - 29 Jan 2021

Cited by 19 | Viewed by 5349

Abstract

Pancreatic β-cell insulin secretion, which responds to various secretagogues and hormonal regulations, is reviewed here, emphasizing the fundamental redox signaling by NADPH oxidase 4- (NOX4-) mediated H₂O₂ production for glucose-stimulated insulin secretion (GSIS). There is a logical summation that integrates both metabolic plus redox homeostasis because the ATP-sensitive K⁺ channel (K_ATP) can only be closed when both ATP and H₂O₂ are elevated. Otherwise ATP would block K_ATP, while H₂O₂ would activate any of the redox-sensitive nonspecific calcium channels (NSCCs), such as TRPM2. Notably, a 100%-closed K_ATP ensemble is insufficient to reach the −50 mV threshold plasma membrane depolarization required for the activation of voltage-dependent Ca²⁺ channels. Open synergic NSCCs or Cl⁻ channels have to act simultaneously to reach this threshold. The resulting intermittent cytosolic Ca²⁺-increases lead to the pulsatile exocytosis of insulin granule vesicles (IGVs). The incretin (e.g., GLP-1) amplification of GSIS stems from receptor signaling leading to activating the phosphorylation of TRPM channels and effects on other channels to intensify integral Ca²⁺-influx (fortified by endoplasmic reticulum Ca²⁺). ATP plus H₂O₂ are also required for branched-chain ketoacids (BCKAs); and partly for fatty acids (FAs) to secrete insulin, while BCKA or FA β-oxidation provide redox signaling from mitochondria, which proceeds by H₂O₂ diffusion or hypothetical SH relay via peroxiredoxin “redox kiss” to target proteins. Full article

(This article belongs to the Special Issue Mitochondrial Redox Regulations)

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