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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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Cites
[30] Microsomal lipid peroxidation
Buege, J. A., & Aust, S. D. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)52032-6 · Cited by 13,564
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 9,051
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Self-citationBcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,402
Mitochondrial control of cell death
Kroemer, G., & Reed, J. C. (2000) · Nature Medicine · doi:10.1038/74994 · Cited by 3,103
Self-citationThe mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432
Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product.
Evan, G. I., Lewis, G. K., Ramsay, G. M., & Bishop, J. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3610 · Cited by 2,412
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
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Items 101–200 of 245
Winger, A. M., Taylor, N. L., Heazlewood, J. L., Day, D. A., & Millar, A. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702385200 · Cited by 83
UCP1 and Defense against Oxidative Stress
Shabalina, I. G., Petrovič, N., Kramarova, T. V., Hoeks, J., Cannon, B., & Nedergaard, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601387200 · Cited by 82
Feugang, J. M., Roover, R. D., Moens, A., Leonard, S., Dessy, F., & Donnay, I. (2003) · Theriogenology · doi:10.1016/s0093-691x(03)00191-2 · Cited by 82
“The mechanism of Trolox embryotoxicity is unknown, but it can be hypothesized that it affects the structure of cell membranes, impairing the cell polarization that characterizes TE cells [57–59].”
BackgroundElucidation of Thioredoxin Target Protein Networks in Mouse
Fu, C., Wu, C., Liu, T., Ago, T., Zhai, P., Sadoshima, J., & Hong Li, A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800580-mcp200 · Cited by 80
“There are four cysteines within mouse ANT1, several of which have been shown to be prone to oxidation (37, 38).”
McCormick, A. L., Meiering, C. D., Smith, G. B., & Mocarski, E. S. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12205-12217.2005 · Cited by 78
“vMIA is a potent suppressor of cell death (6, 8, 9, 25, 30, 51, 59) and can block apoptosis induced by proteasome inhibitors.”
BackgroundKoshkin, V., Dai, F. F., Doucette, C. A., Chan, C. B., & Wheeler, M. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705652200 · Cited by 79
Martin, L. J. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.009 · Cited by 80
Control of Apoptosis by Human Cytomegalovirus
McCormick, A. L. (2008) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-77349-8_16 · Cited by 69
“To date, vMIA is the most broadly antiapoptotic CMV protein known and analogous to the cellular Bcl-2 proteins, is highly effective against a myriad of stimuli including intrinsic stresses as well as extrinsic, immune-regulated signals (Goldmacher et al. 1999; Belzacq et al. 2001; Vieira et al. 2001; Jan et al. 2002;…”
BackgroundCell death suppression by cytomegaloviruses
Goldmacher, V. S. (2005) · APOPTOSIS · doi:10.1007/s10495-005-0800-z · Cited by 67
Self-citationBouaziz, C., Martel, C., Dein, O. S. E., Abid‐Essefi, S., Brenner, C., Lemaire, C., & Bacha, H. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp117 · Cited by 64
Self-citationChang, A., Sancheti, H., Garcia, J., Kaplowitz, N., Cadenas, E., & Han, D. (2014) · Chemical Research in Toxicology · doi:10.1021/tx400462r · Cited by 65
Armas, M. I. D., Esteves, R., Viera, N., Reyes, A. M., Mastrogiovanni, M., Alegria, T. G. P., Netto, L. E. S., Tórtora, V., Radí, R., & Trujillo, M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.451 · Cited by 65
Ceramide-induced formation of ROS and ATP depletion trigger necrosis in lymphoid cells
Villena, J., Henríquez, M., Torres, V. A., Moraga, F., Díaz‐Elizondo, J., Arredondo, C., Chiong, M., Olea‐Azar, C., Stutzin, A., Lavandero, S., et al. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.017 · Cited by 63
Huang, H., Ou, H., Xu, H., Chen, H., Fowler, C., & Gibson, G. E. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10756 · Cited by 64
“The MPT can be regulated by the disulfide redox state (Bernadi et al., 1994; Costantini et al., 2000; Vieira et al., 2001; Chen et al., 2002).”
BackgroundMitochondrial pathobiology in ALS
Martin, L. J. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9395-y · Cited by 65
Salidroside protects against MPP+-induced apoptosis in PC12 cells by inhibiting the NO pathway
Li, X., Ye, X., Li, X., Sun, X., Liang, Q., Tao, L., Kang, X., & Chen, J. (2011) · Brain Research · doi:10.1016/j.brainres.2011.01.015 · Cited by 63
“Excessive mitochondrial Ca2+ accumulation may impair mitochondrial function and activate certain phospholipases, proteases and endonucleases, leading to irreversiblemembrane, organelle and chromatindamageand eventually to cell death (Brown, 1999; Vieira et al., 2001).”
BackgroundHuang, H.-M., Zhang, H., Xu, H., & Gibson, G. E. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(02)00222-3 · Cited by 61
Mechanisms of Apoptosis Induced by Cisplatin in Marginal Cells in Mouse Stria Vascularis
Lee, J., Nakagawa, T., Kita, T., Kim, T. S., Iguchi, F., Endo, T., Shiga, A., Lee, S. H., & Ito, J. (2004) · ORL · doi:10.1159/000079329 · Cited by 62
Thornton, C., Baburamani, A. A., Kichev, A., & Hagberg, H. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170017 · Cited by 64
Access of viral proteins to mitochondria via mitochondria‐associated membranes
Williamson, C. D., & Colberg‐Poley, A. M. (2009) · Reviews in Medical Virology · doi:10.1002/rmv.611 · Cited by 63
“In addition, there is evidence that pUL37x1\vMIA interacts with ANT and the mitochondrial PiC, reducing ATP generation in transfected cells [68,86,91,92].”
Mitochondria as Targets of Apoptosis Regulation by Nitric Oxide
Vieira, H. L. A., & Kroemer, G. (2003) · IUBMB Life · doi:10.1080/15216540310001639652 · Cited by 60
“NO and peroxitrate can induce the permeabilization of proteoliposomes that contain ANT, suggesting that ANT is (one of) the NO targets within the PTPC ( 44, 45 ).”
BackgroundSelf-citationMitochondrial permeability transition as a novel principle of hepatorenal toxicity in vivo
Haouzi, D., COHEN, I. R., Vieira, H. L. A., Poncet, D., Boya, P., Castedo, M., Vadrot, N., Belzacq, A.-S., Fau, D., Brenner, C., et al. (2002) · APOPTOSIS · doi:10.1023/a:1020026923038 · Cited by 61
Self-citationCahuana, G. M., Tejedo, J. R., Jiménez, J., Ramı́rez, R., Sobrino, F., & Bedoya, F. J. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.004 · Cited by 57
Mitochondrion-targeted apoptosis regulators of viral origin
Boya, P., Roumier, T., Andréau, K., González‐Polo, R. A., Zamzami, N., Castedo, M., & Kroemer, G. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00630-2 · Cited by 59
Self-citationPauleau, A.-L., Larochette, N., Giordanetto, F., Scholz, S. R., Poncet, D., Zamzami, N., Goldmacher, V. S., & Kroemer, G. (2007) · Oncogene · doi:10.1038/sj.onc.1210511 · Cited by 53
“In addition to cell death suppression, there is evidence that vMIA interacts with the adenosine triphosphate (ATP) synthasome composed by the adenine nucleotide translocase, the F1F0 ATP synthase and the mitochondrial phosphate carrier (Goldmacher et al., 1999; Vieira et al., 2001).”
Self-citationInsights into the mechanisms of CMV‐mediated interference with cellular apoptosis
Andoniou, C. E., & Degli‐Esposti, M. A. (2006) · Immunology and Cell Biology · doi:10.1111/j.1440-1711.2005.01412.x · Cited by 52
Cavalieri, B., Perrelli, M.-G., Aragno, M., Mastrocola, R., Corvetti, G., Durazzo, M., Poli, G., & Cutrìn, J. C. (2002) · Liver Transplantation · doi:10.1053/jlts.2002.35549 · Cited by 51
Kharaziha, P., Raeve, H. D., Fristedt, C., Li, Q., Gruber, A., Johnsson, P., Kokaraki, G., Panzar, M., Laane, E., Österborg, A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0658 · Cited by 49
“The importance of Mcl-1 for multiple myeloma survival is well described (35).”
Study of PTPC Composition during Apoptosis for Identification of Viral Protein Target
Verrier, F., Mignotte, B., Jan, G., & Brenner, C. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1299.022 · Cited by 49
Self-citationBufalin Induces Reactive Oxygen Species Dependent Bax Translocation and Apoptosis in ASTC‐a‐1 Cells
Sun, L., Chen, T., Wang, X., Chen, Y., & Wei, X. (2009) · Evidence-based Complementary and Alternative Medicine · doi:10.1093/ecam/nep082 · Cited by 44
“ROS may promote MPT by causing the oxidation of thiol groups on the adenine nucleotide translocator, which is believed to form part of the MPT pore [29].”
BackgroundRole of Peroxynitrite in the Cardiovascular Dysfunction of Septic Shock
Liaudet, L., Rosenblatt‐Velin, N., & Pacher, P. (2013) · Current Vascular Pharmacology · doi:10.2174/1570161111311020009 · Cited by 43
Timuçin, A. C., & Başağa, H. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.010 · Cited by 43
“Another evidence towards the possibility of HNE based inhibition of overexpressed Bcl-2 was obtained in Jurkat T cells, where overexpression of Bcl-2 only partially prevented HNE induced ANT dependent mitochondrial permeabilization (Table 2) [121].”
Cytofluorometric quantitation of apoptosis-driven inner mitochondrial membrane permeabilization
Poncet, D., Boya, P., Métivier, D., Zamzami, N., & Kroemer, G. (2003) · APOPTOSIS · doi:10.1023/a:1025546525894 · Cited by 42
Self-citationMor, D., Bembrick, A. L., Austin, P. J., & Keay, K. A. (2011) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2011.01.004 · Cited by 40
“This in turn increases mitochondrial permeability and triggers the release of apoptotic factors into the cytoplasm (Vieira et al., 2001; Pacher et al., 2007).”
BackgroundProtein Carbonylation in Neurodegenerative and Demyelinating CNS Diseases
Bizzozero, O. A. (2008) · Springer eBooks · doi:10.1007/978-0-387-30375-8_23 · Cited by 43
“Also, carbonylation of ANTwith 4-HNE in vitro enhances permeability transition pore opening in proteoliposomes, suggesting that this modification may have some regulatory function in vivo (Vieira et al., 2001).”
BackgroundSmith, G. B., & Mocarski, E. S. (2005) · Journal of Virology · doi:10.1128/jvi.79.23.14923-14932.2005 · Cited by 40
“Human CMV vMIA is a potent suppressor of cell death induced by mitochondrial membrane-permeabilizing agents, reactive oxygen species, and preapoptotic chromatin condensation (3, 7, 55), providing insight into apoptotic signaling and cellular pathways integrating DNA damage with apoptosis checkpoints.”
BackgroundIschemic Preconditioning Reduces Intestinal Epithelial Apoptosis in Rats
Cinel, İ., Avlan, D., Cinel, L., Polat, G., Atici, S., Mavioğlu, İ., Serinol, H., Aksöyek, S., & Oral, U. (2003) · Shock · doi:10.1097/01.shk.0000055817.40894.84 · Cited by 39
“(27) have also shown that apoptosis by lipid peroxidation products, such as 4-hydroxynonenal, can also be inhibited by bcl-2, which may be considered as a supporting finding for our results.”
ResultMitochondrion-dependent caspase activation by the HIV-1 envelope
Roumier, T., Castedo, M., Perfettini, J., Andréau, K., Métivier, D., Zamzami, N., & Kroemer, G. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00480-5 · Cited by 38
Self-citationAging is a deprivation syndrome driven by a germ–soma conflict
Heininger, K. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00015-6 · Cited by 40
Colell, A., García‐Ruiz, C., Marı́, M., & Fernández-Checa, J. C. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00071-7 · Cited by 38
Jat, D., Parihar, P., Kothari, S., & Parihar, M. S. (2013) · PubMed · Cited by 38
Intersection between Mitochondrial Permeability Pores and Mitochondrial Fusion/Fission
Gazaryan, I. G., & Brown, A. M. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9252-2 · Cited by 37
“For example, chemical modification or crosslinking of certain protein thiols are known to alter susceptibility to iMPT [31].”
BackgroundKlumpe, I., Savvatis, K., Westermann, D., Tschöpe, C., Rauch, U., Landmesser, U., Schultheiss, H.-P., & Dörner, A. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1413-4 · Cited by 35
“In addition, HNE has been found to increase the membrane permeability of proteoliposomes containing ANT, suggesting that HNE modification is an indicator of enhanced mitochondrial permeability [26].”
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Ryans, K., Omosun, Y., McKeithen, D. N., Simoneaux, T., Mills, C. C., Bowen, N. J., Eko, F. O., Black, C. M., Igietseme, J. U., & He, Q. (2017) · BMC Immunology · doi:10.1186/s12865-017-0212-1 · Cited by 35
Effects of 4-epianhydrotetracycline on oxidative stress in zebrafish (Danio rerio) embryos
Wang, M., Zhao, J., Wu, L., & Ma, T. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.149047 · Cited by 32
Fukami, T., Nakasu, S., Baba, K., Nakajima, M., & Matsuda, M. (2004) · Journal of Neuro-Oncology · doi:10.1007/s11060-004-9168-0 · Cited by 34
“Many kinds of cytotoxic injuries that induce AIF translocation to the nucleus have been reported [24,29–41], but the role of AIF in response to the hyperthermal stimulation in human tumor cell lines is not known.”
BackgroundTang, Q., Murphy, E. A., & Maul, G. G. (2006) · Journal of Virology · doi:10.1128/jvi.00275-06 · Cited by 34
“The viral mitochondrial inhibitor of apoptosis (vMIA) is apparently a strong inhibitor of apoptosis induced by HCMV infection (3, 6, 7, 15, 18, 22, 31, 39) and also inhibits apoptosis induced by proteosome inhibitors.”
BackgroundResveratrol disrupts peroxynitrite-triggered mitochondrial apoptotic pathway: a role for Bcl-2
de Brito, P. M., Simões, N. F., Almeida, L. M., & Dinis, T. C. P. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0235-4 · Cited by 32
“In other studies, Bcl-2 overexpression has been shown to prevent apoptosis but not necrosis elicited by peroxynitrite [37, 40, 41].”
BackgroundMitochondrial Pathobiology in Parkinson's Disease and Amyotrophic Lateral Sclerosis
Martin, L. J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100348 · Cited by 32
“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 A-sensitive manner [196].”
Effects of 4-hydroxynonenal on mitochondrial 3-hydroxy-3-methylglutaryl (HMG-CoA) synthase
Patel, V. B., Spencer, C. H., Young, T. A., Lively, M. O., & CUNNINGHAM, C. C. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.004 · Cited by 32
Nitric-oxide-induced depolarization of neuronal mitochondria: implications for neuronal cell death
Solenski, N. J., Kostecki, V. K., Dovey, S. L., & Periasamy, A. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2003.08.011 · Cited by 32
“, 1999) in causing evidence that it can react with the mitochondrial ETS and with constituents of the mitochondrial transition pore with the induction of a mitochondrial permeability transition (MPT) (Cassina and Radi, 1996; Radi et al., 1994; Aulak et al., 2001; Brookes et al., 2000; Vieira et al., 2001).”
BackgroundZhao, L., Deng, X., Li, Y., Hu, J., Xie, L., Shi, F., Tang, M., Bode, A. M., Zhang, X., Liao, W., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202114072 · Cited by 31
“…inhibit the opening of mPTP by interacting with ANTs, and the human immunodeficiency virus-1 (HIV-1) encoding viral protein R (Vpr) can bind to ANTs to induce mPTPdriven apoptosis (Jacotot et al, 2001; Vieira et al, 2001; Sabbah et al, 2006; Tanaka et al, 2008; Green et al, 2011; Wang et al, 2017).”
BackgroundAdenine Nucleotide Translocase in the Focus of Cardiovascular Diseases
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Therapeutic peptides: Targeting the mitochondrion to modulate apoptosis
Jacotot, E. D., Deniaud, A., Borgne‐Sanchez, A., Touat-Hamici, Z., Briand, J., Bras, M. L., & Brenner, C. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.07.002 · Cited by 30
Self-citationMahmoud, A. M., Germoush, M. O., & Soliman, A. S. (2014) · International Journal of Pharmacology · doi:10.3923/ijp.2014.451.460 · Cited by 29
Mitochondria as targets in angiogenesis inhibition
Park, D., & Dilda, P. J. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.12.005 · Cited by 32
Viral modulators of cell death provide new links to old pathways
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“In the absence of other viral proteins, overexpression of vMIA protects cells from apoptosis induced by a variety of death stimuli including ligation of death receptors, DNA damage, reactive oxygen species, respiration poisons, and infection with an adenovirus mutant lacking its anti-apoptotic factor E1B 19K [27–29].”
BackgroundGuidarelli, A., Cerioni, L., Tommasini, I., Fiorani, M., Brüne, B., & Cantoni, O. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.016 · Cited by 29
Gao, Y., Zhang, H., Qiao, H., Wang, W., & Chang, J. (2010) · Brain Research · doi:10.1016/j.brainres.2010.08.043 · Cited by 28
“Formation of ROS in the brain after various insults is respirationdependent, mitochondria in vitro are sensitive to ROS, and most data suggest that oxidative stress contributes to the post-ischemic impairment of mitochondrial respiration (Vieira et al., 2001).”
BackgroundIlmarinen, P., Moilanen, E., Kinnula, V. L., & Kankaanranta, H. (2012) · Respiratory Research · doi:10.1186/1465-9921-13-73 · Cited by 28
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BackgroundComputational Insights on the Competing Effects of Nitric Oxide in Regulating Apoptosis
Bagci, E. Z., Yoram Vodovotz, B., Billiar, T. R., Ermentrout, B., & Bahar, İ. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002249 · Cited by 28
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Szeto, H. (2006) · The AAPS Journal · doi:10.1208/aapsj080232 · Cited by 25
Rodrigues, F. P., Pestana, C. R., Polizello, A. C. M., Pardo‐Andreu, G. L., Uyemura, S. A., dos Santos, A. C., Alberici, L. C., da Silva, R. S., & Curti, C. (2012) · Nitric Oxide · doi:10.1016/j.niox.2012.02.001 · Cited by 24
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Cinel, İ. (2002) · Pharmacological Research · doi:10.1016/s1043-6618(02)00075-0 · Cited by 23
Brain mitochondrial alterations after chronic alcohol consumption
Almansa, I., Fernández, A., García‐Ruiz, C., Muriach, M., Barcia, J. M., Miranda, M., Fernández-Checa, J. C., & Romero, F. J. (2009) · Journal of Physiology and Biochemistry · doi:10.1007/bf03180583 · Cited by 22
Winter, J., Klumpe, I., Heger, J., Rauch, U., Schultheiß, H., Landmesser, U., & Dörner, A. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.11.002 · Cited by 22
Daiber, A., Oelze, M. W., Daub, S., Steven, S., Schuff, A., Kröller‐Schön, S., Hausding, M., Wenzel, P., Schulz, E., Gori, T., et al. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_48 · Cited by 21
Murakami, T. (2019) · Scientific Reports · doi:10.1038/s41598-019-53219-w · Cited by 21
4-Hydroxynonenal (HNE) and hepatic injury related to chronic oxidative stress
Bekyarova, G. Y., Tzaneva, M. A., Bratoeva, K. Z., Иванова, И., Kotzev, A. I., Hristova, M., Krastev, D. S., Kindekov, I., & Mileva, M. M. (2019) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2019.1674690 · Cited by 20
Peroxynitrite-induced mitochondrial translocation of PKCα causes U937 cell survival
Cerioni, L., Palomba, L., Brüne, B., & Cantoni, O. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.193 · Cited by 19
Whaley, J. G., Tharakan, B., Smith, B., Hunter, F. A., & Childs, E. W. (2009) · Journal of Burn Care & Research · doi:10.1097/bcr.0b013e3181bfb825 · Cited by 18
Modulation of myocardial contraction by peroxynitrite
Kohr, M. J., Roof, S. R., Zweier, J. L., & Ziolo, M. T. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00468 · Cited by 18
“Additional mitochondrial targets of peroxynitrite include the adenine nucleotide translocase (Vieira et al., 2001), nicotinamide nucleotide transhydrogenase (Forsmark-Andree et al., 1996), and Complex I, II, and V of the electron transport chain (Radi et al., 1994; Cassina and Radi, 1996; Riobo et…”
BackgroundYao, H., Xiang, X., Chen, L., Guo, A.-Q., Fang-qing, H., Lan, L.-P., Lu, X., & Wu, X. (2008) · Bioscience Reports · doi:10.1042/bsr20080144 · Cited by 18
Boengler, K., Gres, P., Dodoni, G., Konietzka, I., Lisa, F. D., Heusch, G., & Schulz, R. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.08.004 · Cited by 18
Oliveira, P. J. (2005) · Current Diabetes Reviews · doi:10.2174/1573399052952578 · Cited by 17
“In the same line, compounds with proapoptotic activities were shown to specifically address the ANT [50-53].”
BackgroundNitric oxide plays a dual role in the oxidative injury of cultured rat microglia but not astroglia
Wang, J., Lee, C.-T., & Wang, J. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.048 · Cited by 17
“NO exerts inhibition on mitochondrial permeability transition pore (MPTP) and cytochrome c release (Vieira et al., 2001) and induces expression of cytoprotective genes, such as HSP70 and HO-1 (Kim et al.”
The antioxidant effect of the mesoionic compound SYD-1 in mitochondria
Gozzi, G. J., Pires, A. D. R. A., Martinez, G. R., Rocha, M. E. M., Noleto, G. R., Echevarrı́a, A., Canuto, A. V. D. S., & Cadena, S. M. S. C. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.07.004 · Cited by 17
Ji, B., Ito, K., & Horie, T. (2004) · Chemical Research in Toxicology · doi:10.1021/tx034067m · Cited by 17
Vimentin intermediate filaments protect mitochondria from oxidative stress
Matveeva, E. A., Chernoivanenko, I. S., & Minin, A. А. (2010) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s199074781004001x · Cited by 16
Reactive Oxygen Species: Friends and Foes of Signal Transduction
Retta, S. F., Chiarugi, P., Trabalzini, L., Pinton, P., & Belkin, A. M. (2012) · Journal of Signal Transduction · doi:10.1155/2012/534029 · Cited by 16
Chen, Y., Stanford, A., Simmons, R. L., Ford, H. R., & Hoffman, R. A. (2001) · Cellular Immunology · doi:10.1006/cimm.2001.1880 · Cited by 15
Imaizumi, N., & Aniya, Y. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.10.012 · Cited by 14
Depletion of Toxoplasma adenine nucleotide translocator leads to defects in mitochondrial morphology
Wu, Y., Ying, Z., Liu, J., Sun, Z., Li, S., & Liu, Q. (2022) · Parasites & Vectors · doi:10.1186/s13071-022-05295-7 · Cited by 13
“Helena and colleagues found that nitric oxide (NO), peroxynitrite, and 4-hydroxynonenal could directly act on ANT to induce mPTP opening and apoptosis [9].”
BackgroundHa, S. C., Han, A. R., Kim, D. W., Kim, E.-A. L., Kim, D., Choi, S. Y., & Cho, S. (2013) · BMB Reports · doi:10.5483/bmbrep.2013.46.7.018 · Cited by 13
“of ROS in the brain after various insults is respiration dependent, and mitochondria in vitro are sensitive to ROS (31).”
BackgroundCantoni, O., Guidarelli, A., Palomba, L., & Fiorani, M. (2005) · Molecular Pharmacology · doi:10.1124/mol.104.009498 · Cited by 13
“An effect of peroxynitrite on the adenine nucleotide translocator was recently identified in Kroemer’s laboratory (Vieira et al., 2001), and this event, in conjunction with alterations in the redox state (Costantini et al., 1996), may well be involved in the commitment to MPT, critically regulated…”
BackgroundCen, J., Liu, L., He, L., Liu, M., Wang, C., & Ji, B. (2012) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2012.08.008 · Cited by 12
“Mitochondria is considered to be a major site of the ROS production in mammalian cells through electron leakage from the electron transport chain and also appears to be the major target of ROS attack (Turrens, 2003; Lizasoain et al., 1996; Vieira et al., 2001).”
BackgroundRole of solute carrier transporters in regulating dendritic cell maturation and function
Shao, L., Yang, M., Sun, T., Xia, H., Du, D., Li, X., & Jie, Z. (2023) · European Journal of Immunology · doi:10.1002/eji.202350385 · Cited by 11
“To form the mitochondrial permeability transition pore, ANTs play a significant role in regulating mitochondrial permeability, morphology, and homeostasis [105, 106].”
BackgroundReactivity of mitochondrial peroxiredoxins with biological hydroperoxides
Trujillo, M., Piacenza, L., & Radí, R. (2023) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2023.100017 · Cited by 10
Kravenska, Y., Ganzha, V. V., Yavorskaya, E. N., & Lukyanetz, E. A. (2016) · Neurophysiology · doi:10.1007/s11062-016-9595-5 · Cited by 10
“of the MPTPs due to the direct interaction of this agent with a structural component of these pores, adenine nucleotide translocase [31].”
CMV modulation of the host response to infection
McCormick, A. L., & Mocarski, E. S. (2007) · Cambridge University Press eBooks · doi:10.1017/cbo9780511545313.022 · Cited by 10
Involvement of the mitochondrial permeability transition pore in angiotensin II-mediated apoptosis.
Ricci, C., Pastukh, V. M., & Schaffer, S. W. (2005) · PubMed Central · Cited by 10
Chen, H., Guan, B., & Shen, J. (2016) · Integrative Medicine International · doi:10.1159/000442468 · Cited by 8
Vieira, H. L. A., Pereira, A. C., Carrondo, M. J. T., & Alves, P. M. (2006) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-006-0093-9 · Cited by 8
“In mammalian cell systems the use of antioxidants to prevent cell death at the mitochondrial level has been described [6, 14].”
BackgroundSelf-citationMitochondrial Regulation of Cell Death
Liu, D., Perfettini, J., & Brenner, C. (2018) · Springer eBooks · doi:10.1007/978-3-319-73344-9_6 · Cited by 8
Self-citationMitochondrial Dysfunction in Reproductive and Developmental Toxicity
Palmeira, C. M., & Ramalho‐Santos, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804239-7.00053-6 · Cited by 6
Modeling Formalisms in Systems Biology of Apoptosis
Kallenberger, S. M., & Legewie, S. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4009-3_1 · Cited by 6
Cell Death Suppressors Encoded by Cytomegalovirus
Goldmacher, V. S. (2004) · Progress in molecular and subcellular biology · doi:10.1007/978-3-540-74264-7_1 · Cited by 6
“vMIA has affinity towards adenine nucleotide translocator (ANT), an integral protein of the inner mitochondrial membrane (Goldmacher et al. 1999; Vieira et al. 2001).”
BackgroundSelf-citationDennis, J., & Bennett, J. P. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10540 · Cited by 5
“, 2001), as well as the conformational state of the mitochondrial permeability transition pore (PTP; Vieira et al., 2001; Reichert et al., 2001) and the nitration of cytochrome c (Cassina et al.”
Background
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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