The adenine nucleotide translocator: a target of nitric oxide, peroxynitrite, and 4-hydroxynonenal
Abstract
Nitric oxide (NO), peroxynitrite, and 4-hydroxynonenal (HNE) may be involved in the pathological demise of cells via apoptosis. Apoptosis induced by these agents is inhibited by Bcl-2, suggesting the involvement of mitochondria in the death pathway. In vitro, NO, peroxynitrite and HNE can cause direct permeabilization of mitochondrial membranes, and this effect is inhibited by cyclosporin A, indicating involvement of the permeability transition pore complex (PTPC) in the permeabilization event. NO, peroxynitrite and HNE also permeabilize proteoliposomes containing the adenine nucleotide translocator (ANT), one of the key components of the PTPC, yet have no or little effects on protein-free control liposomes. ANT-dependent, NO-, peroxynitrite- or HNE-induced permeabilization is at least partially inhibited by recombinant Bcl-2 protein, as well as the antioxidants trolox and butylated hydroxytoluene. In vitro, none of the tested agents (NO, peroxynitrite, HNE, and tert-butylhydroperoxide) causes preferential carbonylation HNE adduction, or nitrotyrosylation of ANT. However, all these agents induced ANT to undergo thiol oxidation/derivatization. Peroxynitrite and HNE also caused significant lipid peroxidation, which was antagonized by butylated hydroxytoluene but not by recombinant Bcl-2. Transfection-enforced expression of vMIA, a viral apoptosis inhibitor specifically targeted to ANT, largely reduces the mitochondrial and nuclear signs of apoptosis induced by NO, peroxynitrite and HNE in intact cells. Taken together these data suggest that NO, peroxynitrite, and HNE may directly act on ANT to induce mitochondrial membrane permeabilization and apoptosis.
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The redox-sensitive thiols of ANT are targets for modification by nitric oxide, peroxynitrite, thiol crosslinkers, and other thiol-reactive reagents.
“In contrast, the redox-sensitive thiols of ANT have been well studied as targets for modification by nitric oxide, peroxynitrite, thiol crosslinkers, and other thiol-reactive reagents (101, 435).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [435]
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Galluzzi, L., Larochette, N., Zamzami, N., & Kroemer, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209598 · Cited by 342 · see citing works
Self-citationMitochondria-targeted peptide antioxidants: Novel neuroprotective agents
Szeto, H. H. (2006) · The AAPS Journal · doi:10.1208/aapsj080362 · Cited by 332 · see citing works
Mitochondria as a Therapeutic Target in Heart Failure
Bayeva, M., Gheorghiade, M., & Ardehali, H. (2012) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2012.08.1021 · Cited by 336 · see citing works
“NO was also shown o activate mitochondrial permeability transition pore openng and to induce apoptosis (71).”
BackgroundThe Role of Oxidative Stress in Myocardial Ischemia and Reperfusion Injury and Remodeling: Revisited
Kurian, G. A., Rajagopal, R., Vedantham, S., & Rajesh, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1656450 · Cited by 331 · see citing works
Arterial ageing: from endothelial dysfunction to vascular calcification
Tesauro, M., Mauriello, A., Rovella, V., Annicchiarico‐Petruzzelli, M., Cardillo, C., Melino, G., & Daniele, N. D. (2017) · Journal of Internal Medicine · doi:10.1111/joim.12605 · Cited by 325 · see citing works
Self-citationCell signalling by reactive lipid species: new concepts and molecular mechanisms
Higdon, A. N., Diers, A. R., Oh, J. Y., Landar, A. L., & Darley-Usmar, V. M. (2012) · Biochemical Journal · doi:10.1042/bj20111752 · Cited by 320 · see citing works
Cell-permeable, mitochondrial-targeted, peptide antioxidants
Szeto, H. H. (2006) · The AAPS Journal · doi:10.1007/bf02854898 · Cited by 316 · see citing works
Free radicals, mitochondria, and hypoxia–ischemia in the developing brain
Blomgren, K., & Hagberg, H. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.040 · Cited by 310 · see citing works
Roles of Reactive Oxygen and Nitrogen Species in Pain
Salvemini, D., Little, J., Doyle, T., & Neumann, W. (2011) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2011.01.026 · Cited by 300 · see citing works
“P A A uthor M anuscript permeability transition pore complex (MPTPC) [352].”
InfluentialLove, S. (2003) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/s0278-5846(03)00022-8 · Cited by 290 · see citing works
Mitotic catastrophe constitutes a special case of apoptosis whose suppression entails aneuploidy
Castedo, M., Perfettini, J., Roumier, T., Valent, A., Raslová, H., Yakushijin, K., Horne, D. A., Feunteun, J., Lenoir, G., Medema, R. H., et al. (2004) · Oncogene · doi:10.1038/sj.onc.1207572 · Cited by 291 · see citing works
“…(Vogelstein et al., 2000), caspases (baculovirus-derived p35) (Bump et al., 1995) or MMP (cytomegalovirus-derived vMIA) (Goldmacher et al., 1999; Vieira et al., 2001), and syncytia were generated either in the absence of DBH (which leads to spontaneous prophase-associated apoptosis) or in the…”
BackgroundSelf-citationAmyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis
Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287 · see citing works
Hill, B. G., Dranka, B. P., Zou, L., Chatham, J. C., & Darley-Usmar, V. M. (2009) · Biochemical Journal · doi:10.1042/bj20090934 · Cited by 284 · see citing works
Mitochondria-Targeted Cytoprotective Peptides for Ischemia–Reperfusion Injury
Szeto, H. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1892 · Cited by 269 · see citing works
“ROS can further promote MPT by causing oxidation of thiol groups on the ANT (104).”
Daiber, A., Lisa, F. D., Oelze, M. W., Kröller‐Schön, S., Steven, S., Schulz, E., & Münzel, T. F. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13403 · Cited by 271 · see citing works
“For instance, peroxynitrite leads tomPTP opening (Vieira et al., 2001).”
BackgroundNeuronal Death and Oxidative Stress in the Developing Brain
Ikonomidou, C., & Kaindl, A. M. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3581 · Cited by 255 · see citing works
“…the capacity of a cell and its mitochondria to scavenge and render them harmless, the resulting oxidative stress may initiate mitochondrial permeability transition (mtPT; i.e ., an increase in mitochondrial membrane permeability through opening of mitochondrial permeability transition pores) (182).”
No death without life: vital functions of apoptotic effectors
Galluzzi, L., Joza, N. A., Tasdemir, E., Maiuri, M. C., Hengartner, M. O., Abrams, J., Tavernarakis, N., Penninger, J. M., Madeo, F., & Kroemer, G. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.28 · Cited by 256 · see citing works
“dent anion channel (VDAC, in the OM), cyclophilin D (CypD, in the mitochondrial matrix), creatine kinase (CK, in the IMS), the peripheral-type benzodiazepine receptor (PBR, in OM) as well as hexokinase isoforms (HKI and HKII, in the cytosol).(128,129)”
BackgroundSelf-citationH+ transport is an integral function of the mitochondrial ADP/ATP carrier
Bertholet, A. M., Chouchani, E. T., Kazak, L., Angelin, A., Fedorenko, A., Long, J. Z., Vidoni, S., Garrity, R., Cho, J., Terada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1400-3 · Cited by 256 · see citing works
Zhao, K., Luo, G., Giannelli, S., & Szeto, H. H. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.08.022 · Cited by 251 · see citing works
The many roads to mitochondrial dysfunction in neuroimmune and neuropsychiatric disorders
Morris, G., & Berk, M. (2015) · BMC Medicine · doi:10.1186/s12916-015-0310-y · Cited by 245 · see citing works
“The subsequent depletion of NADPH impairs the ability of mitochondria to further regenerate reduced GSH, exacerbating the preexisting oxidative stress within the organelle [457,458].”
BackgroundRegulation of the apoptosis–necrosis switch
Nicotera, P., & Melino, G. (2004) · Oncogene · doi:10.1038/sj.onc.1207559 · Cited by 238 · see citing works
“NO can directly regulate the activity of the ANT mitochondrial protein, crucial for the activation of mitochondrial depolarization in certain apoptosis models (Vieira et al., 2001).”
BackgroundSelf-citationNitric oxide as a modulator of apoptosis
Li, C., & Wogan, G. N. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.10.021 · Cited by 237 · see citing works
van Golen, R. F., van Gulik, T. M., & Heger, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.013 · Cited by 221 · see citing works
The permeability transition pore complex in cancer cell death
Brenner, C., & Grimm, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209609 · Cited by 220 · see citing works
Self-citationNitric oxide and mitochondrial respiration in the heart
Brown, G. C., & Borutaite, V. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.022 · Cited by 213 · see citing works
“In vitro, peroxynitrite and S-nitrosothiols can cause direct permeabilisation of mitochondrial membranes, and this effect is inhibited by cyclosporin A, indicating involvement of the mitochondrial permeability transition pore (MPT) in the permeabilisation event [48] [49] [50].”
Oxidatively damaged proteins of heart mitochondrial electron transport complexes
Choksi, K. B., Boylston, W. H., Rabek, J. P., Widger, W. R., & Papaconstantinou, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2003.11.007 · Cited by 212 · see citing works
Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases
Martin, L. J. (2010) · Pharmaceuticals · doi:10.3390/ph3040839 · Cited by 208 · see citing works
“sensitive manner [488].”
Curtis, J., Grimsrud, P. A., Hahn, W. S., Xu, X. M., Foncea, R. E., Graham, D. W., Brestoff, J. R., Wiczer, B. M., Ilkayeva, O., Cianflone, K., et al. (2010) · Diabetes · doi:10.2337/db09-1105 · Cited by 207 · see citing works
“Indeed, under certain conditions 4-HNE can facilitate proton leak in other cell types through adenine nucleotide translocator or uncoupling proteins (45,46).”
BackgroundBelzacq, A.-S., Hamel, C. E., Vieira, H. L. A., Cohen, I., Haouzi, D., Métivier, D., Marchetti, P., Brenner, C., & Kroemer, G. (2001) · Oncogene · doi:10.1038/sj.onc.1204953 · Cited by 194 · see citing works
“…Bcl-2 antagonist Bax, p53-Apl, proline oxidase etc.) (Vogelstein et al., 2000), as well as the generation of small second messengers including Ca2+, ganglioside GD3 (Rippo et al., 2000), reactive oxygen species (ROS) (Costantini et al., 2000a), nitric oxide and peroxynitrite (Vieira et al., 2001).”
BackgroundSelf-citationMitochondrial permeability transition in acute neurodegeneration
Friberg, H., & Wieloch, T. W. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01381-0 · Cited by 185 · see citing works
Uncoupling proteins: A role in protection against reactive oxygen species—or not?
Cannon, B., Shabalina, I. G., Kramarova, T. V., Petrovic, N., & Nedergaard, J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.016 · Cited by 182 · see citing works
Martin, L. J., Gertz, B., Pan, Y. H., Price, A. C., Molkentin, J. D., & Chang, Q. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.02.015 · Cited by 181 · see citing works
“4F). mPTP proteins in spinal cords of mSOD1 mice were examined for nitration because peroxynitrite (ONOO−), a biologically significant oxidant formed by the reaction of nitric oxide (NO) with O2− (Beckman et al., 1993; Pacher et al., 2007) can induce permeability transition (Vieira et al., 2001).”
BackgroundModulation of apoptosis by nitric oxide: implications in myocardial ischemia and heart failure
Razavi, H. M., HAMILTON, J., & Feng, Q. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.11.006 · Cited by 181 · see citing works
“Both NO and peroxynitrite have been shown to oxidize the adenine nucleotide translocator, one of the key components of the permeability transition pore complex and thus accelerate its pro-apoptotic function (Vieira et al., 2001).”
BackgroundPathological apoptosis in the developing brain
Blomgren, K., Leist, M., & Groc, L. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0754-4 · Cited by 181 · see citing works
“sition (mtPT) [207], which then in turn potentiates the oxidative stress.”
BackgroundNitric Oxide, Mitochondria, and Cell Death
Brown, G. C., & Borutaitė, V. (2001) · IUBMB Life · doi:10.1080/15216540152845993 · Cited by 179 · see citing works
“RNS may directly oxidise thiols of the adenine nucleotide translocator, a key component of the MPT pore (48).”
BackgroundPhysiological Roles of the Permeability Transition Pore
Brenner, C., & Moulin, M. (2012) · Circulation Research · doi:10.1161/circresaha.112.265942 · Cited by 179 · see citing works
Self-citationMarzetti, E., Wohlgemuth, S. E., Lees, H. A., Chung, H.-Y., Giovannini, S., & Leeuwenburgh, C. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.05.005 · Cited by 172 · see citing works
“2001) and to promote mPTP opening (Vieira et al. 2001).”
BackgroundGuy, C. B. (2006) · Frontiers in bioscience · doi:10.2741/2122 · Cited by 173 · see citing works
“NO/RNS may also directly oxidise the protein thiols that regulate opening of the MPT pore (52).”
BackgroundBiology of Mitochondria in Neurodegenerative Diseases
Martin, L. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00005-9 · Cited by 162 · see citing works
“In vitro cell-free and cell experiments have shown that NO and ONOO can act directly on the ANT to induce mitochondrial permeabilization in a cyclosporine Asensitive manner.(363) Oxidative stress enhances the binding of CyPD to ANT.”
Viral proteins targeting mitochondria: controlling cell death
Boya, P., Pauleau, A., Poncet, D., González‐Polo, R. A., Zamzami, N., & Kroemer, G. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.08.007 · Cited by 162 · see citing works
“Many different cell lines overexpressing vMIA are protected against CD95 ligation [55] and oxidant stress-induced cell death [60,61], as well as staurosporine [57] or overexpression of Bid [58].”
BackgroundSelf-citationChen, Y., Cai, J.-Y., Murphy, T., & Jones, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202026200 · Cited by 166 · see citing works
Mitochondrial Permeability Transition and Cell Death: The Role of Cyclophilin D
Javadov, S. A., & Kuznetsov, A. V. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00076 · Cited by 157 · see citing works
“In vitro studies using proteins and cells revealed that both NO and ONOO can affect ANT and increase mPT in a CsA-sensitive manner (Vieira et al., 2001), suggesting a key role of nitrosylation in the activation of pore opening.”
Acrolein induces oxidative stress in brain mitochondria
Luo, J., & Shi, R. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2004.09.001 · Cited by 157 · see citing works
“To further demonstrate the role of ANT in acroleininduced oxidative stress, the mitochondrial production of ROS was monitored and the effects of different conditions were tested.”
BackgroundInfluentialThe role of free radicals in cerebral hypoxia and ischemia
Rodrigo, J., Fernández, A. P., Serrano, J., Peinado, M. Á., & Martı́nez, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.010 · Cited by 150 · see citing works
Sansbury, B. E., Jones, S. P., Riggs, D. W., Darley-Usmar, V. M., & Hill, B. G. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.002 · Cited by 150 · see citing works
“This damage phase is associated with cell death, as described in [18], which has been shown to occur via Ca2+ overload [29] and by causing mitochondrial permeability transition [38].”
BackgroundMcCormick, A. L., Smith, V. L., Chow, D. C., & Mocarski, E. S. (2002) · Journal of Virology · doi:10.1128/jvi.77.1.631-641.2003 · Cited by 147 · see citing works
“The activity of vMIA, which is also conserved in two larger glycoproteins encoded by UL37, gpUL37, and gpUL37M, prevents release of cytochrome c from mitochondria. vMIA may function via an association with an adenine nucleotide translocator (ANT) (19, 20), a component of the mitochondrial membrane permeability transit…”
BackgroundInfluentialMitochondria and ischemic reperfusion damage in the adult and in the developing brain
Blomgren, K., Zhu, C., Hallin, U., & Hagberg, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00628-4 · Cited by 143 · see citing works
Morris, G., & Maes, M. H. J. (2014) · Current Neuropharmacology · doi:10.2174/1570159x11666131120224653 · Cited by 139 · see citing works
Viruses as Modulators of Mitochondrial Functions
Anand, S. K., & Tikoo, S. K. (2013) · Advances in Virology · doi:10.1155/2013/738794 · Cited by 141 · see citing works
“It protects the cells against CD95 ligation [211] and oxidative stress-induced cell death [214, 215] and prevents mitochondrial fusion [216] thus promoting cell survival.”
BackgroundEndoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
Boya, P., COHEN, I. R., Zamzami, N., Vieira, H. L. A., & Kroemer, G. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401006 · Cited by 139 · see citing works
Self-citationIsom, A., Barnes, S., Wilson, L. S., KIRK, M. C., Coward, L. U., & Darley-Usmar, V. M. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.03.013 · Cited by 140 · see citing works
“Studies concerning the covalent adduction of 4HNE to cellular target proteins have demonstrated that 4HNE can interact with and in some cases inhibit a variety of enzymes, including the adenine nucleotide translocator and Complex III of the mitochondrial electron transport chain [14–16].”
Redox Regulatory Mechanism of Transnitrosylation by Thioredoxin
Wu, C., Liu, T., Chen, W., Oka, S., Fu, C., Jain, M. R., Parrott, A. M., Baykal, A. T., Sadoshima, J., & Hong Li, A. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000034 · Cited by 132 · see citing works
Hansen, J. M., Zhang, H., & Jones, D. P. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfj175 · Cited by 131 · see citing works
“The adenine translocator is a critical component of the membrane permeability transition (MPT) pore and contains redox-sensitive cysteines that are susceptible to oxidation (Costantini et al., 2000; Vieira et al., 2001).”
BackgroundDysfunctional mitochondrial bioenergetics and the pathogenesis of hepatic disorders
Auger, C., Alhasawi, A. A., Contavadoo, M., & Appanna, V. D. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00040 · Cited by 129 · see citing works
Obrador, E., Palmer, R. S., López‐Blanch, R., Jihad-Jebbar, A., Vallés, S. L., & Estrela, J. M. (2020) · Antioxidants · doi:10.3390/antiox9090901 · Cited by 129 · see citing works
“In vitro cell experiments have shown that NO and ONOO‐ can act directly on the ANT to induce mitochondrial permeabilization [83].”
BackgroundStructural organization of mitochondrial ATP synthase
Wittig, I., & Schägger, H. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.027 · Cited by 128 · see citing works
Fatty Acid Oxidation and Signaling in Apoptosis
Tang, D. G., La, E., Kern, J. C., & Kehrer, J. P. (2002) · Biological Chemistry · doi:10.1515/bc.2002.046 · Cited by 125 · see citing works
An Anti-apoptotic Viral Protein That Recruits Bax to Mitochondria
Poncet, D., Larochette, N., Pauleau, A., Boya, P., Jalil, A., Cartron, P., Vallette, F. M., Schnebelen, C., Bartle, L. M., Skaletskaya, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308408200 · Cited by 124 · see citing works
Self-citationSanvicens, N., Gómez‐Vicente, V., Masip, I., Messeguer, Á., & Cotter, T. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402202200 · Cited by 123 · see citing works
Mitochondria: Redox Metabolism and Dysfunction
Kang, J., & Pervaiz, S. (2012) · Biochemistry Research International · doi:10.1155/2012/896751 · Cited by 121 · see citing works
“An electrogenic transporter, adenine nucleotide translocase (ANT), then transports ATP out of the mitochondria to places where energy demanding cellular processes occur [1].”
BackgroundThe adenine nucleotide translocator in apoptosis
Belzacq, A.-S., Vieira, H. L. A., Kroemer, G., & Brenner, C. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01366-4 · Cited by 117 · see citing works
Self-citationThe Mitochondrial Death Pathway
Chalah, A., & Khosravi‐Far, R. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-1-4020-6554-5_3 · Cited by 116 · see citing works
“It is believed that the release mechanism might involve the opening of mitochondrial PTPs (Vieira et al., 2001).”
Viral and bacterial proteins regulating apoptosis at the mitochondrial level
Boya, P., Roques, B. P., & Kroemer, G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4325 · Cited by 115 · see citing works
Self-citationEngland, K., & Cotter, T. G. (2005) · Redox Report · doi:10.1179/135100005x70224 · Cited by 113 · see citing works
Mitochondrial Thioredoxin System
Patenaude, A., Murthy, M. R. V., & Mirault, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402496200 · Cited by 140 · see citing works
Nitric oxide synthase regulation and diversity: Implications in Parkinson’s disease
Kavya, R., Saluja, R., Singh, S., & Dikshit, M. (2006) · Nitric Oxide · doi:10.1016/j.niox.2006.07.003 · Cited by 110 · see citing works
Disruption of the hexokinase–VDAC complex for tumor therapy
Galluzzi, L., Kepp, O., Tajeddine, N., & Kroemer, G. (2008) · Oncogene · doi:10.1038/onc.2008.114 · Cited by 106 · see citing works
“Although several ANT isoforms facilitate MOMP (Vieira et al., 2001), others, such as ANT2, stabilize mitochondrial membranes (Le Bras et al., 2006).”
BackgroundSelf-citationWu, J., Zhang, M., Hao, S., Jia, M., Ji, M., Qiu, L., Sun, X., Yang, J., & Li, K. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8918-z · Cited by 104 · see citing works
“For instance, mitochondrial dysfunction triggers cell death pathways and inflammatory signaling pathways [33, 34].”
BackgroundHow do reactive oxygen species and calcium trigger mitochondrial membrane permeabilisation?
Tajeddine, N. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.02.013 · Cited by 101 · see citing works
Marriott, H. M., Bingle, C. D., Read, R. C., Braley, K. E., Kroemer, G., Hellewell, P. G., Craig, R. W., Whyte, M. K. B., & Dockrell, D. H. (2005) · Journal of Clinical Investigation · doi:10.1172/jci200521766 · Cited by 101 · see citing works
Self-citationCytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA
Poncet, D., Pauleau, A., Szabadkai, G., Vozza, A., Scholz, S. R., Bras, M. L., Brière, J.-J., Jalil, A., Moigne, R. L., Brenner, C., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604069 · Cited by 100 · see citing works
“The ATP synthasome is a multiprotein ensemble composed of complex V (F1F0ATP synthase), ANT, and phosphate inorganic carrier (PiC; Chen et al., 2004).”
BackgroundInfluentialSelf-citationJavadov, S. A., Jang, S., Parodi‐Rullán, R. M., Khuchua, Z. A., & Kuznetsov, A. V. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2502-4 · Cited by 97 · see citing works
“Nitric oxide and ONOO− also attacked ANT, a PTP regulator that binds CypD, to permeabilize ANT-containing proteoliposomes [92].”
BackgroundAdenine nucleotide translocase: a component of the phylogenetically conserved cell death machinery
Zhivotovsky, B., Galluzzi, L., Kepp, O., & Kroemer, G. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.118 · Cited by 99 · see citing works
Self-citationMartin, L. J., Adams, N. A., Pan, Y., Price, A., & Wong, M. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2225-10.2011 · Cited by 96 · see citing works
“, 2002), and thiol modification of ANT can cause mPTP opening (Costantini et al., 2000; Vieira et al., 2001; García et al., 2007).”
BackgroundCell permeable BH3-peptides overcome the cytoprotective effect of Bcl-2 and Bcl-XL
Vieira, H. L. A., Boya, P., Cohen, I., Hamel, C. E., Haouzi, D., Druillennec, S., Belzacq, A.-S., Brenner, C., Roques, B. P., & Kroemer, G. (2002) · Oncogene · doi:10.1038/sj.onc.1205270 · Cited by 89 · see citing works
“…MMP. BaxBH3 and Bcl2BH3-induced MMP is not inhibited by ANT ligands The viral mitochondrial inhibitor of apoptosis (vMIA) encoded by cytomegalovirus speci®cally interacts with ANT (Goldmacher et al., 1999; Vieira et al., 2001) and this property is thought to account for its MMPstabilizing activity.”
BackgroundSelf-citationvMIA, a viral inhibitor of apoptosis targeting mitochondria
Goldmacher, V. S. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01367-6 · Cited by 88 · see citing works
Self-citationZhang, S., Ong, C. N., & Shen, H. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.03.033 · Cited by 87 · see citing works
Roumier, T., Vieira, H. L. A., Castedo, M., Ferri, K. F., Boya, P., Andréau, K., Druillennec, S., Joza, N. A., Penninger, J. M., Roques, B. P., et al. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401089 · Cited by 87 · see citing works
Self-citationChen, H., Qi, S., & Shen, J. (2016) · Current Neuropharmacology · doi:10.2174/1570159x14666160620102055 · Cited by 86 · see citing works
Mitochondrial Protein Targets of Thiol-Reactive Electrophiles
Wong, H. L., & Liebler, D. C. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700433m · Cited by 82 · see citing works
- Authors
- Vieira, H. L., Belzacq, A.-S., Haouzi, D., Bernassola, F., Cohen, I., Jacotot, E., Ferri, K. F., El Hamel, C., Bartle, L. M., Melino, G., Brenner, C., Goldmacher, V., & Kroemer, G.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Université de Technologie de Compiègne (FR)
- University of Rome Tor Vergata (IT)
- Corresponding author
- Kroemer, Guido
- ORCID
- Venue
- Oncogene
- Published
- 2001-07-19
- Volume
- 20
- Issue
- 32
- Pages
- 4305-4316
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2005480061
- Cited by
- 244
- References
- 67
- Citations by year
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- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion)
- Funders
- Agence Nationale de la Recherche
- Ligue Contre le Cancer
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- adenine nucleotide translocase, nitric oxide, peroxynitrite, 4-hydroxynonenal, apoptosis, mitochondrial permeability transition pore, mitochondrial membrane permeabilization, Bcl-2, lipid peroxidation, thiol oxidation, Trolox, butylated hydroxytoluene, cyclosporine, oxidative stress
- MeSH terms
- Mitochondrial Permeability Transition Pore, Mitochondrial ADP, ATP Translocases, Aldehydes, Animals, Cell Nucleus, HeLa Cells, Humans, Intracellular Membranes, Ion Channels, Membrane Proteins, Mitochondria, Nitrates, Nitric Oxide, Permeability, Proteins, Proteolipids, Lipid Peroxidation, Oxidants, Apoptosis, Jurkat Cells, Proto-Oncogene Proteins c-bcl-2, Mitochondrial Membrane Transport Proteins, Inhibitor of Apoptosis Proteins, Mice
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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