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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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“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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“Abbreviations: AGER, advanced glycosylation end product-specific receptor; ALOX5, arachidonate 5-lipoxygenase; ANT, adenine nucleotide translocase; ASK1, apoptosis signal-regulating kinase 1; aSMase, acidic sphingomyelinase; ATF6, activating transcription factor 6; CFLAR, caspase-8 and FADD-like apoptosis regulator; C…”
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“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).”
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“Peroxynitrites can directly activate MPT (Vieira et al., 2001; Bernardi et al., 2006).”
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“…(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…”
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No death without life: vital functions of apoptotic effectors
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“…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).”
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“RNS may directly oxidise thiols of the adenine nucleotide translocator, a key component of the MPT pore (48).”
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“NO/RNS may also directly oxidise the protein thiols that regulate opening of the MPT pore (52).”
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“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.”
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“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
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“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.”
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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
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“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].”
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“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…”
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Viruses as Modulators of Mitochondrial Functions
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“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 140
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“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
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“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 130
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“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
Fatty Acid Oxidation and Signaling in Apoptosis
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An Anti-apoptotic Viral Protein That Recruits Bax to Mitochondria
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“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 118
Self-citationThe Mitochondrial Death Pathway
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“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
Self-citationEngland, K., & Cotter, T. G. (2005) · Redox Report · doi:10.1179/135100005x70224 · Cited by 113
Mitochondrial Thioredoxin System
Patenaude, A., Murthy, M. R. V., & Mirault, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402496200 · Cited by 140
Nitric oxide synthase regulation and diversity: Implications in Parkinson’s disease
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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
“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 105
“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 103
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 106
Self-citationCytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA
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“The ATP synthasome is a multiprotein ensemble composed of complex V (F1F0ATP synthase), ANT, and phosphate inorganic carrier (PiC; Chen et al., 2004).”
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“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
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“, 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
“…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
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Mitochondrial Protein Targets of Thiol-Reactive Electrophiles
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Metadata
- 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
- 2026: 1 · 2025: 1 · 2023: 2 · 2022: 7 · 2021: 2 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 9 · 2015: 5 · 2014: 7 · 2013: 10 · 2012: 16
- 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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