[1]
Davis, S.S. Biomedical applications of nanotechnology--implications for drug targeting and gene therapy. Trends Biotechnol., 1997, 15(6), 217-224.
[2]
Keservani, R.K.; Sharma, A.K.; Kesharwani, R.K. Drug
Delivery Approaches and Nanosystems, Volume 2: Drug Targeting
Aspects of Nanotechnology. CRC Press: , 2017.
[3]
Burns, R.J.; Smith, R.A.; Murphy, M.P. Synthesis and characterization of thiobutyltriphenylphosphonium bromide, a novel thiol reagent targeted to the mitochondrial matrix. Arch. Biochem. Biophys., 1995, 322(1), 60-68.
[4]
Wallace, D.C.; Fan, W. Energetics, epigenetics, mitochondrial genetics. Mitochondrion, 2010, 10(1), 12-31.
[5]
Nicholls, D.G.; Bernson, V.S.; Heaton, G.M. The identification of the component in the inner membrane of brown adipose tissue mitochondria responsible for regulating energy dissipation. Experientia Suppl., 1978, 32, 89-93.
[6]
Bagur, R.; Hajnóczky, G. Intracellular Ca2+ Sensing: Its Role in Calcium Homeostasis and Signaling. Mol. Cell, 2017, 66(6), 780-788.
[7]
Clapham, D.E. Calcium signaling. Cell, 2007, 131(6), 1047-1058.
[8]
Lemasters, J.J. Molecular Mechanisms of Cell Death. In Molecular Pathology; Elsevier, 2018, pp. 1-24.
[9]
Kim, J-S.; He, L.; Lemasters, J.J. Mitochondrial permeability transition: a common pathway to necrosis and apoptosis. Biochem. Biophys. Res. Commun., 2003, 304(3), 463-470.
[10]
Kalkavan, H.; Green, D.R. MOMP, cell suicide as a BCL-2 family business. Cell Death Differ., 2018, 25(1), 46-55.
[11]
Chautan, M.; Chazal, G.; Cecconi, F.; Gruss, P.; Golstein, P. Interdigital cell death can occur through a necrotic and caspase-independent pathway. Curr. Biol., 1999, 9(17), 967-970.
[12]
Angelova, P.R.; Abramov, A.Y. Functional role of mitochondrial reactive oxygen species in physiology. Free Radic. Biol. Med., 2016, 100, 81-85.
[13]
Zorov, D.B.; Juhaszova, M.; Sollott, S.J. Mitochondrial ROS-induced ROS release: an update and review. Biochim. Biophys. Acta (BBA)-. Bioenergetics, 2006, 1757(5-6), 509-517.
[14]
Orrenius, S.; Gogvadze, V.; Zhivotovsky, B. Mitochondrial oxidative stress: implications for cell death. Annu. Rev. Pharmacol. Toxicol., 2007, 47, 143-183.
[15]
Zhou, R.; Yazdi, A.S.; Menu, P.; Tschopp, J. A role for mitochondria in NLRP3 inflammasome activation. Nature, 2011, 469(7329), 221-225.
[16]
Angelova, P.R.; Kasymov, V.; Christie, I.; Sheikhbahaei, S.; Turovsky, E.; Marina, N.; Korsak, A.; Zwicker, J.; Teschemacher, A.G.; Ackland, G.L.; Funk, G.D.; Kasparov, S.; Abramov, A.Y.; Gourine, A. V Functional Oxygen Sensitivity of Astrocytes. J. Neurosci., 2015, 35(29), 10460-10473.
[17]
Bedard, K.; Krause, K-H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev., 2007, 87(1), 245-313.
[18]
Klebanoff, S.J. Myeloperoxidase: friend and foe. J. Leukoc. Biol., 2005, 77(5), 598-625.
[19]
Kellogg, E.W.; Fridovich, I. Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system. J. Biol. Chem., 1975, 250(22), 8812-8817.
[20]
Pizzinat, N.; Copin, N.; Vindis, C.; Parini, A.; Cambon, C. Reactive oxygen species production by monoamine oxidases in intact cells. Naunyn Schmiedebergs Arch. Pharmacol., 1999, 359(5), 428-431.
[21]
Montezano, A.C.; Touyz, R.M. Reactive oxygen species and endothelial function--role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases. Basic Clin. Pharmacol. Toxicol., 2012, 110(1), 87-94.
[22]
Sahoo, S.; Meijles, D.N.; Pagano, P.J. NADPH oxidases: key modulators in aging and age-related cardiovascular diseases? Clin. Sci. (Lond.), 2016, 130(5), 317-335.
[23]
Nauseef, W.M. Biological roles for the NOX family NADPH oxidases. J. Biol. Chem., 2008, 283(25), 16961-16965.
[24]
Rastogi, R.; Geng, X.; Li, F.; Ding, Y. NOX Activation by Subunit Interaction and Underlying Mechanisms in Disease. Front. Cell. Neurosci., 2016, 10, 301.
[25]
Vorobjeva, N.; Prikhodko, A.; Galkin, I.; Pletjushkina, O.; Zinovkin, R.; Sud’ina, G.; Chernyak, B.; Pinegin, B. Mitochondrial reactive oxygen species are involved in chemoattractant-induced oxidative burst and degranulation of human neutrophils in vitro. Eur. J. Cell Biol., 2017, 96(3), 254-265.
[26]
Zinovkin, R.A.; Romaschenko, V.P.; Galkin, I.I.; Zakharova, V.V.; Pletjushkina, O.Y.; Chernyak, B.V.; Popova, E.N. Role of mitochondrial reactive oxygen species in age-related inflammatory activation of endothelium. Aging (Albany NY), 2014, 6(8), 661-674.
[27]
Mukhopadhyay, P.; Horváth, B.; Zsengellér, Z.; Zielonka, J.; Tanchian, G.; Holovac, E.; Kechrid, M.; Patel, V.; Stillman, I.E.; Parikh, S.M.; Joseph, J.; Kalyanaraman, B.; Pacher, P. Mitochondrial-targeted antioxidants represent a promising approach for prevention of cisplatin-induced nephropathy. Free Radic. Biol. Med., 2012, 52(2), 497-506.
[28]
Tuppen, H.A.L.; Blakely, E.L.; Turnbull, D.M.; Taylor, R.W. Mitochondrial DNA mutations and human disease. Biochim. Biophys. Acta - Bioenerg., 2010, 1797(2), 113-128.
[29]
Lightowlers, R.N.; Taylor, R.W.; Turnbull, D.M. Mutations causing mitochondrial disease: What is new and what challenges remain? Science, 2015, 349(6255), 1494-1499.
[30]
Phielix, E.; Schrauwen-Hinderling, V.B.; Mensink, M.; Lenaers, E.; Meex, R.; Hoeks, J.; Kooi, M.E.; Moonen-Kornips, E.; Sels, J-P.; Hesselink, M.K.C.; Schrauwen, P. Lower intrinsic ADP-stimulated mitochondrial respiration underlies in vivo mitochondrial dysfunction in muscle of male type 2 diabetic patients. Diabetes, 2008, 57(11), 2943-2949.
[31]
Kelley, D.E.; He, J.; Menshikova, E.V.; Ritov, V.B. Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes, 2002, 51(10), 2944-2950.
[32]
Ritov, V.B.; Menshikova, E.V.; Azuma, K.; Wood, R.; Toledo, F.G.S.; Goodpaster, B.H.; Ruderman, N.B.; Kelley, D.E. Deficiency of electron transport chain in human skeletal muscle mitochondria in type 2 diabetes mellitus and obesity. Am. J. Physiol. Endocrinol. Metab., 2010, 298(1), E49-E58.
[33]
Mihalik, S.J.; Goodpaster, B.H.; Kelley, D.E.; Chace, D.H.; Vockley, J.; Toledo, F.G.S.; DeLany, J.P. Increased levels of plasma acylcarnitines in obesity and type 2 diabetes and identification of a marker of glucolipotoxicity. Obesity (Silver Spring), 2010, 18(9), 1695-1700.
[34]
Newgard, C.B.; An, J.; Bain, J.R.; Muehlbauer, M.J.; Stevens, R.D.; Lien, L.F.; Haqq, A.M.; Shah, S.H.; Arlotto, M.; Slentz, C.A.; Rochon, J.; Gallup, D.; Ilkayeva, O.; Wenner, B.R.; Yancy, W.S.; Eisenson, H.; Musante, G.; Surwit, R.S.; Millington, D.S.; Butler, M.D.; Svetkey, L.P. A branched-chain amino acid-related metabolic signature that differentiates obese and lean humans and contributes to insulin resistance. Cell Metab., 2009, 9(4), 311-326.
[35]
Adams, S.H.; Hoppel, C.L.; Lok, K.H.; Zhao, L.; Wong, S.W.; Minkler, P.E.; Hwang, D.H.; Newman, J.W.; Garvey, W.T. Plasma acylcarnitine profiles suggest incomplete long-chain fatty acid beta-oxidation and altered tricarboxylic acid cycle activity in type 2 diabetic African-American women. J. Nutr., 2009, 139(6), 1073-1081.
[36]
Anderson, E.J.; Lustig, M.E.; Boyle, K.E.; Woodlief, T.L.; Kane, D.A.; Lin, C-T.; Price, J.W.; Kang, L.; Rabinovitch, P.S.; Szeto, H.H.; Houmard, J.A.; Cortright, R.N.; Wasserman, D.H.; Neufer, P.D. Mitochondrial H2O2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans. J. Clin. Invest., 2009, 119(3), 573-581.
[37]
Brown, D.A.; Perry, J.B.; Allen, M.E.; Sabbah, H.N.; Stauffer, B.L.; Shaikh, S.R.; Cleland, J.G.F.; Colucci, W.S.; Butler, J.; Voors, A.A.; Anker, S.D.; Pitt, B.; Pieske, B.; Filippatos, G.; Greene, S.J.; Gheorghiade, M. Expert consensus document: Mitochondrial function as a therapeutic target in heart failure. Nat. Rev. Cardiol., 2017, 14(4), 238-250.
[38]
Halestrap, A.P.; Pasdois, P. The role of the mitochondrial permeability transition pore in heart disease. Biochim. Biophys. Acta, 2009, 1787(11), 1402-1415.
[39]
Boudina, S.; Sena, S.; O’Neill, B.T.; Tathireddy, P.; Young, M.E.; Abel, E.D. Reduced mitochondrial oxidative capacity and increased mitochondrial uncoupling impair myocardial energetics in obesity. Circulation, 2005, 112(17), 2686-2695.
[40]
Rontoyanni, V.G.; Nunez Lopez, O.; Fankhauser, G.T.; Cheema, Z.F.; Rasmussen, B.B.; Porter, C. Mitochondrial Bioenergetics in the Metabolic Myopathy Accompanying Peripheral Artery Disease. Front. Physiol., 2017, 8, 141.
[41]
Swerdlow, R.H.; Burns, J.M.; Khan, S.M. The Alzheimer’s disease mitochondrial cascade hypothesis. J. Alzheimers Dis., 2010, 20(Suppl. 2), S265-S279.
[42]
Onyango, I.G.; Dennis, J.; Khan, S.M. Mitochondrial Dysfunction in Alzheimer’s Disease and the Rationale for Bioenergetics Based Therapies. Aging Dis., 2016, 7(2), 201-214.
[43]
Lustbader, J.W.; Cirilli, M.; Lin, C.; Xu, H.W.; Takuma, K.; Wang, N.; Caspersen, C.; Chen, X.; Pollak, S.; Chaney, M.; Trinchese, F.; Liu, S.; Gunn-Moore, F.; Lue, L-F.; Walker, D.G.; Kuppusamy, P.; Zewier, Z.L.; Arancio, O.; Stern, D.; Yan, S.S.; Wu, H. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer’s disease. Science, 2004, 304(5669), 448-452.
[44]
Manczak, M.; Anekonda, T.S.; Henson, E.; Park, B.S.; Quinn, J.; Reddy, P.H. Mitochondria are a direct site of A beta accumulation in Alzheimer’s disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet., 2006, 15(9), 1437-1449.
[45]
Moreira, P.I.; Zhu, X.; Wang, X.; Lee, H-G.; Nunomura, A.; Petersen, R.B.; Perry, G.; Smith, M.A. Mitochondria: a therapeutic target in neurodegeneration. Biochim. Biophys. Acta, 2010, 1802(1), 212-220.
[46]
Beal, M.F. Mitochondria and neurodegeneration. Novartis Found. Symp., 2007, 287, 183-192.
[47]
Ekstrand, M.I.; Terzioglu, M.; Galter, D.; Zhu, S.; Hofstetter, C.; Lindqvist, E.; Thams, S.; Bergstrand, A.; Hansson, F.S.; Trifunovic, A.; Hoffer, B.; Cullheim, S.; Mohammed, A.H.; Olson, L.; Larsson, N-G. Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons. Proc. Natl. Acad. Sci. USA, 2007, 104(4), 1325-1330.
[48]
Galter, D.; Pernold, K.; Yoshitake, T.; Lindqvist, E.; Hoffer, B.; Kehr, J.; Larsson, N-G.; Olson, L. MitoPark mice mirror the slow progression of key symptoms and L-DOPA response in Parkinson’s disease. Genes Brain Behav., 2010, 9(2), 173-181.
[49]
Carmo, C.; Naia, L.; Lopes, C.; Rego, A.C. Mitochondrial Dysfunction in Huntington’s Disease. Adv. Exp. Med. Biol., 2018, 1049, 59-83.
[50]
Beal, M.F.; Brouillet, E.; Jenkins, B.G.; Ferrante, R.J.; Kowall, N.W.; Miller, J.M.; Storey, E.; Srivastava, R.; Rosen, B.R.; Hyman, B.T. Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid. J. Neurosci., 1993, 13(10), 4181-4192.
[51]
Shi, P.; Gal, J.; Kwinter, D.M.; Liu, X.; Zhu, H. Mitochondrial dysfunction in amyotrophic lateral sclerosis. Biochim. Biophys. Acta, 2010, 1802(1), 45-51.
[52]
Igoudjil, A.; Magrané, J.; Fischer, L.R.; Kim, H.J.; Hervias, I.; Dumont, M.; Cortez, C.; Glass, J.D.; Starkov, A.A.; Manfredi, G. In vivo pathogenic role of mutant SOD1 localized in the mitochondrial intermembrane space. J. Neurosci., 2011, 31(44), 15826-15837.
[53]
Hoffman, E.P.; Brown, R.H.; Kunkel, L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell, 1987, 51(6), 919-928.
[54]
Sperl, W.; Skladal, D.; Gnaiger, E.; Wyss, M.; Mayr, U.; Hager, J.; Gellerich, F.N. High resolution respirometry of permeabilized skeletal muscle fibers in the diagnosis of neuromuscular disorders. Mol. Cell. Biochem., 1997, 174(1-2), 71-78.
[55]
Vila, M.C.; Rayavarapu, S.; Hogarth, M.W.; Meulen, J.H. Van der; Horn, A.; Defour, A.; Takeda, S.; Brown, K.J.; Hathout, Y.; Nagaraju, K.; Jaiswal, J.K. Mitochondria mediate cell membrane repair and contribute to Duchenne muscular dystrophy. Cell Death Differ., 2017, 24(2), 330-342.
[56]
Kelly-Worden, M.; Thomas, E. Mitochondrial Dysfunction in Duchenne Muscular Dystrophy. Open J. Endocr. Metab. Dis., 2014, 4(8), 211-218.
[57]
Rygiel, K.A.; Miller, J.; Grady, J.P.; Rocha, M.C.; Taylor, R.W.; Turnbull, D.M. Mitochondrial and inflammatory changes in sporadic inclusion body myositis. Neuropathol. Appl. Neurobiol., 2015, 41(3), 288-303.
[58]
Balk, R.A. Systemic inflammatory response syndrome (SIRS): where did it come from and is it still relevant today? Virulence, 2014, 5(1), 20-26.
[59]
Rangel-Frausto, M.S.; Pittet, D.; Costigan, M.; Hwang, T.; Davis, C.S.; Wenzel, R.P. The natural history of the systemic inflammatory response syndrome (SIRS): A prospective study. Jama, 1995, 273(2), 117-123.
[60]
Zakharova, V.V.; Pletjushkina, O.Y.; Zinovkin, R.A.; Popova, E.N.; Chernyak, B. V Mitochondria-Targeted Antioxidants and Uncouplers of Oxidative Phosphorylation in Treatment of the Systemic Inflammatory Response Syndrome (SIRS). J. Cell. Physiol., 2017, 232(5), 904-912.
[61]
Jo, E-K.; Kim, J.K.; Shin, D-M.; Sasakawa, C. Molecular mechanisms regulating NLRP3 inflammasome activation. Cell. Mol. Immunol., 2016, 13(2), 148-159.
[62]
Zhong, Z.; Liang, S.; Sanchez-Lopez, E.; He, F.; Shalapour, S.; Lin, X.; Wong, J.; Ding, S.; Seki, E.; Schnabl, B.; Hevener, A.L.; Greenberg, H.B.; Kisseleva, T.; Karin, M. New mitochondrial DNA synthesis enables NLRP3 inflammasome activation. Nature, 2018, 560(7717), 198-203.
[63]
Zhang, Q.; Raoof, M.; Chen, Y.; Sumi, Y.; Sursal, T.; Junger, W.; Brohi, K.; Itagaki, K.; Hauser, C.J. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature, 2010, 464(7285), 104-107.
[64]
Prikhodko, A.S.; Vitushkina, M.V.; Zinovkina, L.A.; Popova, E.N.; Zinovkin, R.A. Priming of human neutrophils is necessary for their activation by extracellular DNA. Biochem., 2016, 81(6), 609-614.
[65]
Chakraborty, K.; Raundhal, M.; Chen, B.B.; Morse, C.; Tyurina, Y.Y.; Khare, A.; Oriss, T.B.; Huff, R.; Lee, J.S.; St Croix, C.M.; Watkins, S.; Mallampalli, R.K.; Kagan, V.E.; Ray, A.; Ray, P. The mito-DAMP cardiolipin blocks IL-10 production causing persistent inflammation during bacterial pneumonia. Nat. Commun., 2017, 8, 13944.
[66]
Raoof, M.; Zhang, Q.; Itagaki, K.; Hauser, C.J. Mitochondrial Peptides Are Potent Immune Activators That Activate Human Neutrophils Via FPR-1. J. Trauma Inj. Infect. Crit. Care, 2010, 68(6), 1328-1334.
[67]
Mitochondrial Biology and Experimental Therapeutics; Oliveira, P.J., Ed. Springer: Cham, 2018.
[68]
Sun, N.; Youle, R.J.; Finkel, T. The Mitochondrial Basis of Aging. Mol. Cell, 2016, 61(5), 654-666.
[69]
Harman, D. The biologic clock: the mitochondria? J. Am. Geriatr. Soc., 1972, 20(4), 145-147.
[70]
Trifunovic, A.; Wredenberg, A.; Falkenberg, M.; Spelbrink, J.N.; Rovio, A.T.; Bruder, C.E.; Bohlooly-Y, M.; Gidlöf, S.; Oldfors, A.; Wibom, R.; Törnell, J.; Jacobs, H.T.; Larsson, N-G. Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature, 2004, 429(6990), 417-423.
[71]
Schriner, S.E.; Linford, N.J.; Martin, G.M.; Treuting, P.; Ogburn, C.E.; Emond, M.; Coskun, P.E.; Ladiges, W.; Wolf, N.; Remmen, H. Van; Wallace, D.C.; Rabinovitch, P.S. Extension of murine life span by overexpression of catalase targeted to mitochondria. Science, 2005, 308(5730), 1909-1911.
[72]
Kennedy, S.R.; Salk, J.J.; Schmitt, M.W.; Loeb, L.A. Ultra-sensitive sequencing reveals an age-related increase in somatic mitochondrial mutations that are inconsistent with oxidative damage. PLoS Genet., 2013, 9(9)e1003794
[73]
Chung, H.Y.; Cesari, M.; Anton, S.; Marzetti, E.; Giovannini, S.; Seo, A.Y.; Carter, C.; Yu, B.P.; Leeuwenburgh, C. Molecular inflammation: underpinnings of aging and age-related diseases. Ageing Res. Rev., 2009, 8(1), 18-30.
[74]
Judge, S.; Jang, Y.M.; Smith, A.; Hagen, T.; Leeuwenburgh, C. Age-associated increases in oxidative stress and antioxidant enzyme activities in cardiac interfibrillar mitochondria: implications for the mitochondrial theory of aging. FASEB J., 2005, 19(3), 419-421.
[75]
Ungvari, Z.; Orosz, Z.; Labinskyy, N.; Rivera, A.; Xiangmin, Z.; Smith, K.; Csiszar, A. Increased mitochondrial H2O2 production promotes endothelial NF-kappaB activation in aged rat arteries. Am. J. Physiol. Heart Circ. Physiol., 2007, 293(1), H37-H47.
[76]
Dai, D-F.; Rabinovitch, P.S.; Ungvari, Z. Mitochondria and cardiovascular aging. Circ. Res., 2012, 110(8), 1109-1124.
[77]
Sanada, F.; Taniyama, Y.; Muratsu, J.; Otsu, R.; Shimizu, H.; Rakugi, H.; Morishita, R. Source of Chronic Inflammation in Aging. Front. Cardiovasc. Med., 2018, 5, 12.
[78]
Merkwirth, C.; Jovaisaite, V.; Durieux, J.; Matilainen, O.; Jordan, S.D.; Quiros, P.M.; Steffen, K.K.; Williams, E.G.; Mouchiroud, L.; Tronnes, S.U.; Murillo, V.; Wolff, S.C.; Shaw, R.J.; Auwerx, J.; Dillin, A. Two Conserved Histone Demethylases Regulate Mitochondrial Stress-Induced Longevity. Cell, 2016, 165(5), 1209-1223.
[79]
Tian, Y.; Garcia, G.; Bian, Q.; Steffen, K.K.; Joe, L.; Wolff, S.; Meyer, B.J.; Dillin, A. Mitochondrial Stress Induces Chromatin Reorganization to Promote Longevity and UPR mt. Cell, 2016, 165(5), 1197-1208.
[80]
Gray, M.W.; Burger, G.; Lang, B.F. Mitochondrial evolution. Science, 1999, 283(5407), 1476-1481.
[81]
Adam-Vizi, V.; Chinopoulos, C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol. Sci., 2006, 27(12), 639-645.
[82]
Kagan, V.E.; Borisenko, G.G.; Tyurina, Y.Y.; Tyurin, V.A.; Jiang, J.; Potapovich, A.I.; Kini, V.; Amoscato, A.A.; Fujii, Y. Oxidative lipidomics of apoptosis: redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine. Free Radic. Biol. Med., 2004, 37(12), 1963-1985.
[83]
Pfanner, N.; Geissler, A. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol., 2001, 2(5), 339-349.
[84]
Liberman, E.A.; Topaly, V.P.; Tsofina, L.M.; Jasaitis, A.A.; Skulachev, V.P. Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria. Nature, 1969, 222(5198), 1076-1078.
[85]
Smith, R.A.; Porteous, C.M.; Coulter, C.V.; Murphy, M.P. Selective targeting of an antioxidant to mitochondria. Eur. J. Biochem., 1999, 263(3), 709-716.
[86]
Amorim, R.; Benfeito, S.; Teixeira, J.; Cagide, F.; Oliveira, P.J.; Borges, F. In:. Mitochondrial Biology and Experimental Therapeutics; Oliveira, P.J., Ed.; Springer: Cham, 2018, pp. 333-358.
[87]
Weissig, V. In: In: Mitochondrial Medicine; Weissig, V.; Edeas, M., Eds.; Humana Press, 2015; Vol. II, pp. 1-11.
[88]
D’Souza, G.G.M.; Boddapati, S.V.; Weissig, V. Mitochondrial leader sequence-plasmid DNA conjugates delivered into mammalian cells by DQAsomes co-localize with mitochondria. Mitochondrion, 2005, 5(5), 352-358.
[89]
Zhao, K.; Zhao, G-M.; Wu, D.; Soong, Y.; Birk, A.V.; Schiller, P.W.; Szeto, H.H. Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury. J. Biol. Chem., 2004, 279(33), 34682-34990.
[90]
Birk, A.V.; Liu, S.; Soong, Y.; Mills, W.; Singh, P.; Warren, J.D.; Seshan, S.V.; Pardee, J.D.; Szeto, H.H. The mitochondrial-targeted compound SS-31 re-energizes ischemic mitochondria by interacting with cardiolipin. J. Am. Soc. Nephrol., 2013, 24(8), 1250-1261.
[91]
Szeto, H.H. Cell-permeable, mitochondrial-targeted, peptide antioxidants. AAPS J., 2006, 8(2), E277-E283.
[92]
Cerrato, C.P.; Langel, Ü. Cell-Penetrating Peptides Targeting Mitochondria. In Mitochondrial Biology and Experimental Therapeutics; Springer International Publishing: Cham, 2018, pp. 593-611.
[93]
Szeto, H.H.; Birk, A.V. Serendipity and the discovery of novel compounds that restore mitochondrial plasticity. Clin. Pharmacol. Ther., 2014, 96(6), 672-683.
[94]
Heijne, G. von Mitochondrial targeting sequences may form amphiphilic helices. EMBO J., 1986, 5(6), 1335-1342.
[95]
Neupert, W.; Herrmann, J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem., 2007, 76, 723-749.
[96]
Flierl, A.; Jackson, C.; Cottrell, B.; Murdock, D.; Seibel, P.; Wallace, D.C. Targeted delivery of DNA to the mitochondrial compartment via import sequence-conjugated peptide nucleic acid. Mol. Ther., 2003, 7(4), 550-557.
[97]
Yu, H.; Koilkonda, R.D.; Chou, T-H.; Porciatti, V.; Ozdemir, S.S.; Chiodo, V.; Boye, S.L.; Boye, S.E.; Hauswirth, W.W.; Lewin, A.S.; Guy, J. Gene delivery to mitochondria by targeting modified adenoassociated virus suppresses Leber’s hereditary optic neuropathy in a mouse model. Proc. Natl. Acad. Sci. USA, 2012, 109(20), E1238-E1247.
[98]
Cha, M-Y.; Han, S-H.; Son, S.M.; Hong, H-S.; Choi, Y-J.; Byun, J.; Mook-Jung, I. Mitochondria-specific accumulation of amyloid β induces mitochondrial dysfunction leading to apoptotic cell death. PLoS One, 2012, 7(4)e34929
[99]
Korshunov, S.S.; Skulachev, V.P.; Starkov, A.A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett., 1997, 416(1), 15-18.
[100]
Antonenko, Y.N.; Avetisyan, A.V.; Bakeeva, L.E.; Chernyak, B.V.; Chertkov, V.A.; Domnina, L.V.; Ivanova, O.Y.; Izyumov, D.S.; Khailova, L.S.; Klishin, S.S.; Korshunova, G.A.; Lyamzaev, K.G.; Muntyan, M.S.; Nepryakhina, O.K.; Pashkovskaya, A.A.; Pletjushkina, O.Y.; Pustovidko, A.V.; Roginsky, V.A.; Rokitskaya, T.I.; Ruuge, E.K.; Saprunova, V.B.; Severina, I.I.; Simonyan, R.A.; Skulachev, I.V.; Skulachev, M.V.; Sumbatyan, N.V.; Sviryaeva, I.V.; Tashlitsky, V.N.; Vassiliev, J.M.; Vyssokikh, M.Y.; Yaguzhinsky, L.S.; Zamyatnin, A.A.; Skulachev, V.P. Mitochondria-targeted plastoquinone derivatives as tools to interrupt execution of the aging program. 1. Cationic plastoquinone derivatives: synthesis and in vitro studies. Biochemistry (Mosc.), 2008, 73(12), 1273-1287.
[101]
Fink, B.D.; Herlein, J.A.; Yorek, M.A.; Fenner, A.M.; Kerns, R.J.; Sivitz, W.I. Bioenergetic effects of mitochondrial-targeted coenzyme Q analogs in endothelial cells. J. Pharmacol. Exp. Ther., 2012, 342(3), 709-719.
[102]
Rossman, M.J.; Santos-Parker, J.R.; Steward, C.A.C.; Bispham, N.Z.; Cuevas, L.M.; Rosenberg, H.L.; Woodward, K.A.; Chonchol, M.; Gioscia-Ryan, R.A.; Murphy, M.P.; Seals, D.R. Chronic
Supplementation With a Mitochondrial Antioxidant (MitoQ)
Improves Vascular Function in Healthy Older Adults. Hypertens (Dallas, Tex. 1979). 2018, 71(6), 1056-1063.
[103]
Snow, B.J.; Rolfe, F.L.; Lockhart, M.M.; Frampton, C.M.; O’Sullivan, J.D.; Fung, V.; Smith, R.A.J.; Murphy, M.P.; Taylor, K.M. Protect Study Group A double-blind, placebo-controlled study to assess the mitochondria-targeted antioxidant MitoQ as a disease-modifying therapy in Parkinson’s disease. Mov. Disord., 2010, 25(11), 1670-1674.
[104]
Gane, E.J.; Weilert, F.; Orr, D.W.; Keogh, G.F.; Gibson, M.; Lockhart, M.M.; Frampton, C.M.; Taylor, K.M.; Smith, R.A.J.; Murphy, M.P. The mitochondria-targeted anti-oxidant mitoquinone decreases liver damage in a phase II study of hepatitis C patients. Liver Int., 2010, 30(7), 1019-1026.
[105]
Petrov, A.; Perekhvatova, N.; Skulachev, M.; Stein, L.; Ousler, G. SkQ1 Ophthalmic Solution for Dry Eye Treatment: Results of a Phase 2 Safety and Efficacy Clinical Study in the Environment and During Challenge in the Controlled Adverse Environment Model. Adv. Ther., 2016, 33(1), 96-115.
[106]
Sies, H. Total antioxidant capacity: appraisal of a concept. J. Nutr., 2007, 137(6), 1493-1495.
[107]
Gasparovic, A.C.; Jaganjac, M.; Mihaljevic, B.; Sunjic, S.B.; Zarkovic, N. Assays for the measurement of lipid peroxidation. Methods Mol. Biol., 2013, 965, 283-296.
[108]
Kelso, G.F.; Porteous, C.M.; Coulter, C.V.; Hughes, G.; Porteous, W.K.; Ledgerwood, E.C.; Smith, R.A.; Murphy, M.P. Selective targeting of a redox-active ubiquinone to mitochondria within cells: antioxidant and antiapoptotic properties. J. Biol. Chem., 2001, 276(7), 4588-4596.
[109]
Skulachev, V.P.; Antonenko, Y.N.; Cherepanov, D.A.; Chernyak, B.V.; Izyumov, D.S.; Khailova, L.S.; Klishin, S.S.; Korshunova, G.A.; Lyamzaev, K.G.; Pletjushkina, O.Y.; Roginsky, V.A.; Rokitskaya, T.I.; Severin, F.F.; Severina, I.I.; Simonyan, R.A.; Skulachev, M.V.; Sumbatyan, N.V.; Sukhanova, E.I.; Tashlitsky, V.N.; Trendeleva, T.A.; Vyssokikh, M.Y.; Zvyagilskaya, R.A. Prevention of cardiolipin oxidation and fatty acid cycling as two antioxidant mechanisms of cationic derivatives of plastoquinone (SkQs). Biochim. Biophys. Acta Bioenerg., 2010, 1797(6-7), 878-889.
[110]
Severin, F.F.; Severina, I.I.; Antonenko, Y.N.; Rokitskaya, T.I.; Cherepanov, D.A.; Mokhova, E.N.; Vyssokikh, M.Y.; Pustovidko, A.V.; Markova, O.V.; Yaguzhinsky, L.S.; Korshunova, G.A.; Sumbatyan, N.V.; Skulachev, M.V.; Skulachev, V.P. Penetrating cation/fatty acid anion pair as a mitochondria-targeted protonophore. Proc. Natl. Acad. Sci. USA, 2010, 107(2), 663-668.
[111]
Feniouk, B.A.; Skulachev, V.P. Cellular and Molecular Mechanisms of Action of Mitochondria-Targeted Antioxidants. Curr. Aging Sci., 2017, 10(1), 41-48.
[112]
Asin-Cayuela, J.; Manas, A-R.B.; James, A.M.; Smith, R.A.J.; Murphy, M.P. Fine-tuning the hydrophobicity of a mitochondria-targeted antioxidant. FEBS Lett., 2004, 571(1-3), 9-16.
[113]
Pond, S.M.; Tozer, T.N. First-pass elimination. Basic concepts and clinical consequences. Clin. Pharmacokinet., 9(1), 1-25.
[114]
Murphy, M.P.; Smith, R.A.J. Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol., 2007, 47, 629-656.
[115]
Smith, R.A.J.; Porteous, C.M.; Gane, A.M.; Murphy, M.P. Delivery of bioactive molecules to mitochondria in vivo. Proc. Natl. Acad. Sci. USA, 2003, 100(9), 5407-5412.
[116]
Kezic, A.; Spasojevic, I.; Lezaic, V.; Bajcetic, M. Mitochondria-Targeted Antioxidants: Future Perspectives in Kidney Ischemia Reperfusion Injury. Oxid. Med. Cell. Longev., 2016, 2016, 1-12.
[117]
Silva, F.S.G.; Simoes, R.F.; Couto, R.; Oliveira, P.J. Targeting Mitochondria in Cardiovascular Diseases. Curr. Pharm. Des., 2016, 22(37), 5698-5717.
[118]
Braakhuis, A.J.; Nagulan, R.; Somerville, V. The Effect of MitoQ on Aging-Related Biomarkers: A Systematic Review and Meta-Analysis. Oxid. Med. Cell. Longev., 2018, 20188575263
[119]
Shabalina, I.G.; Vyssokikh, M.Y.; Gibanova, N.; Csikasz, R.I.; Edgar, D.; Hallden-Waldemarson, A.; Rozhdestvenskaya, Z.; Bakeeva, L.E.; Vays, V.B.; Pustovidko, A.V.; Skulachev, M.V.; Cannon, B.; Skulachev, V.P.; Nedergaard, J. Improved health-span and lifespan in mtDNA mutator mice treated with the mitochondrially targeted antioxidant SkQ1. Aging (Albany NY), 2017, 9(2), 315-339.
[120]
Ng, L.F.; Gruber, J.; Cheah, I.K.; Goo, C.K.; Cheong, W.F.; Shui, G.; Sit, K.P.; Wenk, M.R.; Halliwell, B. The mitochondria-targeted antioxidant MitoQ extends lifespan and improves healthspan of a transgenic Caenorhabditis elegans model of Alzheimer disease. Free Radic. Biol. Med., 2014, 71, 390-401.
[121]
Shill, D.D.; Southern, W.M.; Willingham, T.B.; Lansford, K.A.; McCully, K.K.; Jenkins, N.T. Mitochondria-specific antioxidant supplementation does not influence endurance exercise training-induced adaptations in circulating angiogenic cells, skeletal muscle oxidative capacity or maximal oxygen uptake. J. Physiol., 2016, 594(23), 7005-7014.
[122]
Gioscia-Ryan, R.A.; LaRocca, T.J.; Sindler, A.L.; Zigler, M.C.; Murphy, M.P.; Seals, D.R. Mitochondria-targeted antioxidant (MitoQ) ameliorates age-related arterial endothelial dysfunction in mice. J. Physiol., 2014, 592(12), 2549-2561.
[123]
Loo B. , van der; Labugger, R.; Skepper, J.N.; Bachschmid, M.; Kilo, J.; Powell, J.M.; Palacios-Callender, M.; Erusalimsky, J.D.; Quaschning, T.; Malinski, T.; Gygi, D.; Ullrich, V.; Lüscher, T.F. Enhanced peroxynitrite formation is associated with vascular aging. J. Exp. Med., 2000, 192(12), 1731-1744.
[124]
Bachschmid, M.M.; Schildknecht, S.; Matsui, R.; Zee, R.; Haeussler, D.; Cohen, R.A.; Pimental, D.; Loo, B. van der Vascular aging: chronic oxidative stress and impairment of redox signaling-consequences for vascular homeostasis and disease. Ann. Med., 2013, 45(1), 17-36.
[125]
Weidinger, A.; Müllebner, A.; Paier-Pourani, J.; Banerjee, A.; Miller, I.; Lauterböck, L.; Duvigneau, J.C.; Skulachev, V.P.; Redl, H.; Kozlov, A.V. Vicious inducible nitric oxide synthase-mitochondrial reactive oxygen species cycle accelerates inflammatory response and causes liver injury in rats. Antioxid. Redox Signal., 2015, 22(7), 572-586.
[126]
Manskikh, V.N.; Gancharova, O.S.; Nikiforova, A.I.; Krasilshchikova, M.S.; Shabalina, I.G.; Egorov, M.V.; Karger, E.M.; Milanovsky, G.E.; Galkin, I.I.; Skulachev, V.P.; Zinovkin, R.A. Age-associated murine cardiac lesions are attenuated by the mitochondria-targeted antioxidant SkQ1. Histol. Histopathol., 2015, 30(3), 353-360.
[127]
Galkin, I.I.; Pletjushkina, O.Y.; Zinovkin, R.A.; Zakharova, V.V.; Birjukov, I.S.; Chernyak, B.V.; Popova, E.N. Mitochondria-targeted antioxidants prevent TNFα-induced endothelial cell damage. Biochemistry (Mosc.), 2014, 79(2), 124-130.
[128]
Mao, P.; Manczak, M.; Shirendeb, U.P.; Reddy, P.H. MitoQ, a mitochondria-targeted antioxidant, delays disease progression and alleviates pathogenesis in an experimental autoimmune encephalomyelitis mouse model of multiple sclerosis. Biochim. Biophys. Acta, 2013, 1832(12), 2322-2331.
[129]
Korenaga, M.; Wang, T.; Li, Y.; Showalter, L.A.; Chan, T.; Sun, J.; Weinman, S.A. Hepatitis C virus core protein inhibits mitochondrial electron transport and increases reactive oxygen species (ROS) production. J. Biol. Chem., 2005, 280(45), 37481-37488.
[130]
Chacko, B.K.; Srivastava, A.; Johnson, M.S.; Benavides, G.A.; Chang, M.J.; Ye, Y.; Jhala, N.; Murphy, M.P.; Kalyanaraman, B.; Darley-Usmar, V.M. Mitochondria-targeted ubiquinone (MitoQ) decreases ethanol-dependent micro and macro hepatosteatosis. Hepatology, 2011, 54(1), 153-163.
[131]
Lukashev, A.N.; Skulachev, M.V.; Ostapenko, V.; Savchenko, A.Y.; Pavshintsev, V.V.; Skulachev, V.P. Advances in development of rechargeable mitochondrial antioxidants. Prog. Mol. Biol. Transl. Sci., 2014, 127, 251-265.
[132]
Skulachev, V.P.; Anisimov, V.N.; Antonenko, Y.N.; Bakeeva, L.E.; Chernyak, B.V.; Erichev, V.P.; Filenko, O.F.; Kalinina, N.I.; Kapelko, V.I.; Kolosova, N.G.; Kopnin, B.P.; Korshunova, G.A.; Lichinitser, M.R.; Obukhova, L.A.; Pasyukova, E.G.; Pisarenko, O.I.; Roginsky, V.A.; Ruuge, E.K.; Senin, I.I.; Severina, I.I.; Skulachev, M.V.; Spivak, I.M.; Tashlitsky, V.N.; Tkachuk, V.A.; Vyssokikh, M.Y.; Yaguzhinsky, L.S.; Zorov, D.B. An attempt to prevent senescence: a mitochondrial approach. Biochim. Biophys. Acta, 2009, 1787(5), 437-461.
[133]
Markovets, A.M.; Fursova, A.Z.; Kolosova, N.G. Therapeutic action of the mitochondria-targeted antioxidant SkQ1 on retinopathy in OXYS rats linked with improvement of VEGF and PEDF gene expression. PLoS One, 2011, 6(7)e21682
[134]
Iomdina, E.N.; Khoroshilova-Maslova, I.P.; Robustova, O.V.; Averina, O.A.; Kovaleva, N.A.; Aliev, G.; Reddy, V.P.; Zamyatnin, A.A.; Skulachev, M.V.; Senin, I.I.; Skulachev, V.P. Mitochondria-targeted antioxidant SkQ1 reverses glaucomatous lesions in rabbits. Front. Biosci. Landmark Ed., 2015, 20(1), 892-901.
[135]
Yani, E.V.; Katargina, L.A.; Chesnokova, N.B.; Beznos, O.V.; Savchenko, A.Y.; Vygodin, V.A.; Gudkova, E.Y.; Zamyatnin, J.A.A.; Skulachev, M.V. The first experience of using the drug Vizomitin in the treatment of dry eyes. Per. Med., 2012, 4(59), 134-137.
[136]
Brzheskiy, V.V.; Efimova, E.L.; Vorontsova, T.N.; Alekseev, V.N.; Gusarevich, O.G.; Shaidurova, K.N.; Ryabtseva, A.A.; Andryukhina, O.M.; Kamenskikh, T.G.; Sumarokova, E.S.; Miljudin, E.S.; Egorov, E.A.; Lebedev, O.I.; Surov, A.V.; Korol, A.R.; Nasinnyk, I.O.; Bezditko, P.A.; Muzhychuk, O.P.; Vygodin, V.A.; Yani, E.V.; Savchenko, A.Y.; Karger, E.M.; Fedorkin, O.N.; Mironov, A.N.; Ostapenko, V.; Popeko, N.A.; Skulachev, V.P.; Skulachev, M.V. Results of a Multicenter, Randomized, Double-Masked, Placebo-Controlled Clinical Study of the Efficacy and Safety of Visomitin Eye Drops in Patients with Dry Eye Syndrome. Adv. Ther., 2015, 32(12), 1263-1279.
[137]
Zernii, E.Y.; Gancharova, O.S.; Baksheeva, V.E.; Golovastova, M.O.; Kabanova, E.I.; Savchenko, M.S.; Tiulina, V.V.; Sotnikova, L.F.; Zamyatnin, A.A.; Philippov, P.P.; Senin, I.I. Mitochondria-Targeted Antioxidant SkQ1 Prevents Anesthesia-Induced Dry Eye Syndrome. Oxid. Med. Cell. Longev., 2017, 2017, 1-17.
[138]
Callender, S.P.; Mathews, J.A.; Kobernyk, K.; Wettig, S.D. Microemulsion utility in pharmaceuticals: Implications for multi-drug delivery. Int. J. Pharm., 2017, 526(1-2), 425-442.