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Journal articles on the topic 'Pore de transition de perméabilité mitochondrial'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Cour, M., J. Loufouat, M. Palliard, L. Gomez, A. Gharib, M. Ovize, and L. Argaud. "F013 Inhibition de l’ouverture du pore de transition de perméabilité mitochondrial et protection cellulaire dans l’arrêt cardio-circulatoire." Archives of Cardiovascular Diseases 102 (March 2009): S58. http://dx.doi.org/10.1016/s1875-2136(09)72266-1.

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2

Lablanche, S., C. Cottet, S. Halimi, and P. Y. Benhamou. "P164 Rôle du Pore de transition de perméabilité mitochondriale dans la mort cellulaire béta induite par l’ischémie-reperfusion." Diabetes & Metabolism 38 (March 2012): A70. http://dx.doi.org/10.1016/s1262-3636(12)71266-1.

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3

Li, B., D. De Paulis, E. Couture-Lepetit, A. Gharib, and M. Ovize. "C021 Effets in vitro des inhibiteurs de la chaîne respiratoire sur l’inhibition du pore de transition de perméabilité mitochondrial par la cyclosporine A." Archives of Cardiovascular Diseases 102 (March 2009): S35. http://dx.doi.org/10.1016/s1875-2136(09)72208-9.

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4

Lablanche, S., C. Cottet, F. Lamarche, S. Halimi, P. Y. Benhamou, X. Leverve, and E. Fontaine. "P161 - Rôle du pore de transition de perméabilité mitochondriale dans l’apoptose des cellules béta induite par l’hyperglycémie et l’hyperfructosémie." Diabetes & Metabolism 37, no. 1 (March 2011): A72—A73. http://dx.doi.org/10.1016/s1262-3636(11)70787-x.

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5

Lablanche, S., C. Cottet, M. J. Richard, S. Halimi, and E. Fontaine. "P163 Implication du pore de transition de perméabilité mitochondriale dans l’apoptose des îlots pancréatiques humains induite par l’hyperglycémie et l’hyperfructosémie." Diabetes & Metabolism 38 (March 2012): A70. http://dx.doi.org/10.1016/s1262-3636(12)71265-x.

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6

Crompton, Martin, Sukaina Virji, Veronica Doyle, Nicholas Johnson, and John M. Ward. "The mitochondrial permeability transition pore." Biochemical Society Symposia 66 (September 1, 1999): 167–79. http://dx.doi.org/10.1042/bss0660167.

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This chapter reviews recent advances in the identification of the structural elements of the permeability transition pore. The discovery that cyclosporin A (CsA) inhibits the pore proved instrumental. Various approaches indicate that CsA blocks the pore by binding to cyclophilin (CyP)-D. In particular, covalent labelling of CyP-D in situ by a photoactive CsA derivative has shown that pore ligands have the same effects on the degree to which CsA both blocks the pore and binds to CyP-D. The recognition that CyP-D is a key component has enabled the other constituents to be resolved. Use of a CyP-D fusion protein as affinity matrix has revealed that CyP-D binds very strongly to 1:1 complexes of the voltage-dependent anion channel (from the outer membrane) and adenine nucleotide translocase (inner membrane). Our current model envisages that the pore arises as a complex between these three components at contact sites between the mitochondrial inner and outer membranes. This is in line with recent reconstitutions of pore activity from protein fractions containing these proteins. The strength of interaction between these proteins suggests that it may be a permanent feature rather than assembled only under pathological conditions. Calcium, the key activator of the pore, does not appear to affect pore assembly; rather, an allosteric action allowing pore flicker into an open state is indicated. CsA inhibits pore flicker and lowers the binding affinity for calcium. Whether adenine nucleotide translocase or the voltage-dependent anion channel (via inner membrane insertion) provides the inner membrane pore has not been settled, and data relevant to this issue are also documented.

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7

GATEAUROESCH, O., L. ARGAUD, and M. OVIZE. "Mitochondrial permeability transition pore and postconditioning." Cardiovascular Research 70, no. 2 (May 1, 2006): 264–73. http://dx.doi.org/10.1016/j.cardiores.2006.02.024.

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8

Jonas, Elizabeth, Nelli Mnatsakanyan, Kambiz N. Alavian, and Rongmin Chen. "Mitochondrial (ATP Synthase) Permeability Transition Pore." Biophysical Journal 118, no. 3 (February 2020): 16a. http://dx.doi.org/10.1016/j.bpj.2019.11.269.

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9

Halestrap, Andrew P. "What is the mitochondrial permeability transition pore?" Journal of Molecular and Cellular Cardiology 46, no. 6 (June 2009): 821–31. http://dx.doi.org/10.1016/j.yjmcc.2009.02.021.

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10

Naryzhnaya, Natalia V., Leonid N. Maslov, and Peter R. Oeltgen. "Pharmacology of mitochondrial permeability transition pore inhibitors." Drug Development Research 80, no. 8 (August 24, 2019): 1013–30. http://dx.doi.org/10.1002/ddr.21593.

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11

Chernyak, B. V. "Redox Regulation of the Mitochondrial Permeability Transition Pore." Bioscience Reports 17, no. 3 (June 1, 1997): 293–302. http://dx.doi.org/10.1023/a:1027384628678.

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The recent data on redox regulation of the mitochondrial cyclosporin-sensitive pore are reviewed here. They indicate that the pore is modulated by the redox state of pyridine nucleotides and glutathione at two independent sites. Special attention is paid to experimental approaches for studying this phenomenon in isolated mitochondria. The relation between oxidative stress and the opening of the mitochondrial pore in some cases of cell injury and in programmed cell death (apoptosis) is discussed.

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12

Morota, Saori, Magnus-J. Hansson, Roland Mansson, Yoshihisa Kudo, Nagao Ishii, Eskil Elmer, and Hiroyuki Uchino. "Mitochondrial permeability transition: Evaluation of putative “pore blockers”." Neuroscience Research 58 (January 2007): S240. http://dx.doi.org/10.1016/j.neures.2007.06.583.

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13

Gautier, Clement A., Emilie Giaime, Erica Caballero, Lucía Núñez, Zhiyin Song, David Chan, Carlos Villalobos, and Jie Shen. "Regulation of mitochondrial permeability transition pore by PINK1." Molecular Neurodegeneration 7, no. 1 (2012): 22. http://dx.doi.org/10.1186/1750-1326-7-22.

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14

Amodeo, Giuseppe F., Nelli Mnatsakanyan, Maria E. Solesio, Magdalena Klim, Piotr Kurcok, Eleonora Zakharian, Elizabeth A. Jonas, and Evgeny V. Pavlov. "Molecular Assembly of the Mitochondrial Permeability Transition Pore." Biophysical Journal 114, no. 3 (February 2018): 658a. http://dx.doi.org/10.1016/j.bpj.2017.11.3554.

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15

Mnatsakanyan, Nelli, Gisela Beutner, George A. Porter, Kambiz N. Alavian, and Elizabeth A. Jonas. "Physiological roles of the mitochondrial permeability transition pore." Journal of Bioenergetics and Biomembranes 49, no. 1 (February 11, 2016): 13–25. http://dx.doi.org/10.1007/s10863-016-9652-1.

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16

Varanyuwatana, Pinadda, and Andrew P. Halestrap. "The mitochondrial permeability transition pore and its modulators." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1797 (July 2010): 130–31. http://dx.doi.org/10.1016/j.bbabio.2010.04.388.

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17

Szab�, Ildik�, and Mario Zoratti. "The mitochondrial megachannel is the permeability transition pore." Journal of Bioenergetics and Biomembranes 24, no. 1 (February 1992): 111–17. http://dx.doi.org/10.1007/bf00769537.

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18

Afzal, Nasrin, W. Jonathan Lederer, and M. Saleet Jafri. "Mitochondrial Permeability Transition Pore and Number of Openings." Biophysical Journal 112, no. 3 (February 2017): 440a. http://dx.doi.org/10.1016/j.bpj.2016.11.2350.

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19

Villa-Abrille, María C., Eugenio Cingolani, Horacio E. Cingolani, and Bernardo V. Alvarez. "Silencing of cardiac mitochondrial NHE1 prevents mitochondrial permeability transition pore opening." American Journal of Physiology-Heart and Circulatory Physiology 300, no. 4 (April 2011): H1237—H1251. http://dx.doi.org/10.1152/ajpheart.00840.2010.

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Inhibition of Na+/H+ exchanger 1 (NHE1) reduces cardiac ischemia-reperfusion (I/R) injury and also cardiac hypertrophy and failure. Although the mechanisms underlying these NHE1-mediated effects suggest delay of mitochondrial permeability transition pore (MPTP) opening, and reduction of mitochondrial-derived superoxide production, the possibility of NHE1 blockade targeting mitochondria has been incompletely explored. A short-hairpin RNA sequence mediating specific knock down of NHE1 expression was incorporated into a lentiviral vector (shRNA-NHE1) and transduced in the rat myocardium. NHE1 expression of mitochondrial lysates revealed that shRNA-NHE1 transductions reduced mitochondrial NHE1 (mNHE1) by ∼60%, supporting the expression of NHE1 in mitochondria membranes. Electron microscopy studies corroborate the presence of NHE1 in heart mitochondria. Immunostaining of rat cardiomyocytes also suggests colocalization of NHE1 with the mitochondrial marker cytochrome c oxidase. To examine the functional role of mNHE1, mitochondrial suspensions were exposed to increasing concentrations of CaCl2 to induce MPTP opening and consequently mitochondrial swelling. shRNA-NHE1 transduction reduced CaCl2-induced mitochondrial swelling by 64 ± 4%. Whereas the NHE1 inhibitor HOE-642 (10 μM) decreased mitochondrial Ca2+-induced swelling in rats transduced with nonsilencing RNAi (37 ± 6%), no additional HOE-642 effects were detected in mitochondria from rats transduced with shRNA-NHE1. We have characterized the expression and function of NHE1 in rat heart mitochondria. Because mitochondria from rats injected with shRNA-NHE1 present a high threshold for MPTP formation, the beneficial effects of NHE1 inhibition in I/R resulting from mitochondrial targeting should be considered.

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20

Yehuda-Shnaidman, Einav, Bella Kalderon, and Jacob Bar-Tana. "Modulation of Mitochondrial Transition Pore Components by Thyroid Hormone." Endocrinology 146, no. 5 (May 1, 2005): 2462–72. http://dx.doi.org/10.1210/en.2004-1161.

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Abstract Thyroid hormone (TH) modulates metabolic efficiency by controlling the coupling of mitochondrial oxidative phosphorylation. However, its uncoupling mode of action is still enigmatic. Treatment of Jurkat or GH3 cells with T3 is reported here to result in limited, Cyclosporin A-sensitive mitochondrial depolarization, conforming to low conductance gating of the mitochondrial transition pore (MTP). MTP protein components induced by T3 treatment were verified in T3-treated and hypothyroid rat liver as well as in Jurkat cells. T3 treatment resulted in increase in mitochondrial Bax and Bak together with decreased mitochondrial Bcl2. T3-induced mitochondrial depolarization was aborted by overexpression of Bcl2. In contrast to Bax-Bcl2 family proteins, some other MTP components were either not induced by T3 (e.g. voltage-dependent anion channel) or were induced, but were not involved in Cyclosporin A-sensitive MTP gating (e.g. Cyclophilin D and adenine nucleotide translocase-2) Hence, TH-induced mitochondrial uncoupling may be ascribed to low conductance MTP gating mediated by TH-induced increase in mitochondrial proapoptotic combined with a decrease in mitochondrial antiapoptotic proteins of the Bax-Bcl2 family.

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21

Hirsch, Tamara, Isabel Marzo, and Guido Kroemer. "Role of the Mitochondrial Permeability Transition Pore in Apoptosis." Bioscience Reports 17, no. 1 (February 1, 1997): 67–76. http://dx.doi.org/10.1023/a:1027339418683.

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Mitochondrial permeability transition (PT) involves the formation of proteaceous, regulated pores, probably by apposition of inner and outer mitochondrial membrane proteins which cooperate to form the mitochondrial megachannel (=mitochondrial PT pore). PT has important metabolic consequences, namely the collapse of the mitochondrial transmembrane potential, uncoupling of the respiratory chain, hyperproduction of superoxide anions, disruption of mitochondrial biogenesis, outflow of matrix calcium and glutathione, and release of soluble intermembrane proteins. Recent evidence suggests that PT is a critical, rate limiting event of apoptosis (programmed cell death): (i) induction of PT suffices to cause apoptosis; (ii) one of the immediate consequences of PT, disruption of the mitochondrial transmembrane potential (ΔΨm), is a constant feature of early apoptosis; (iii) prevention of PT impedes the ΔΨm collapse as well as all other features of apoptosis at the levels of the cytoplasma, the nucleus, and the plasma membrane; (iv) PT is modulated by members of the apoptosis-regulatory bcl-2 gene family. Recent data suggest that the acquisition of the apoptotic phenotype, including characteristic changes in nuclear morphology and biochemistry (chromatin condensation and DNA fragmentation), depends on the action of apoptogenic proteins released from the mitochondrial intermembrane space.

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22

Matsumoto, Shohei, Hans Friberg, Michel Ferrand-Drake, and Tadeusz Wieloch. "Blockade of the Mitochondrial Permeability Transition Pore Diminishes Infarct Size in the Rat after Transient Middle Cerebral Artery Occlusion." Journal of Cerebral Blood Flow & Metabolism 19, no. 7 (July 1999): 736–41. http://dx.doi.org/10.1097/00004647-199907000-00002.

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The mitochondrial permeability transition pore is an inducer of cell death. During the reperfusion phase after cerebral ischemia, calcium accumulates in mitochondria, and a burst of free radical formation occurs, conditions that favor the activation of the mitochondrial permeability transition pore. Here the authors demonstrate that a blocker of the mitochondrial permeability transition pore, the nonimmunosuppressive cyclosporin A analogue N-methyl-Val-4-cyclosporin A (10 mg/kg intraperitoneally), administered during reperfusion and at 24 hours of reperfusion, diminishes infarct size in a rat model of transient focal ischemia of 2 hours' duration. The mitochondrial permeability transition pore may be an important target for drugs against stroke.

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23

Quinsay, Melissa N., Robert L. Thomas, Youngil Lee, and Åsa B. Gustafsson. "Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore." Autophagy 6, no. 7 (October 2010): 855–62. http://dx.doi.org/10.4161/auto.6.7.13005.

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24

Shintani-Ishida, Kaori, and Ken-ichi Yoshida. "Mitochondrial m-calpain opens the mitochondrial permeability transition pore in ischemia–reperfusion." International Journal of Cardiology 197 (October 2015): 26–32. http://dx.doi.org/10.1016/j.ijcard.2015.06.010.

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25

Hassoun, Sidi Mohamed, Steve Lancel, Patrice Petillot, Brigitte Decoster, Raphael Favory, Philippe Marchetti, and Remi Neviere. "Sphingosine impairs mitochondrial function by opening permeability transition pore." Mitochondrion 6, no. 3 (June 2006): 149–54. http://dx.doi.org/10.1016/j.mito.2006.05.001.

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26

Chinopoulos, Christos. "Mitochondrial permeability transition pore: Back to the drawing board." Neurochemistry International 117 (July 2018): 49–54. http://dx.doi.org/10.1016/j.neuint.2017.06.010.

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27

Gerle, Christoph. "Mitochondrial F-ATP synthase as the permeability transition pore." Pharmacological Research 160 (October 2020): 105081. http://dx.doi.org/10.1016/j.phrs.2020.105081.

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28

Baines, Christopher P. "The molecular composition of the mitochondrial permeability transition pore." Journal of Molecular and Cellular Cardiology 46, no. 6 (June 2009): 850–57. http://dx.doi.org/10.1016/j.yjmcc.2009.02.007.

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29

Torrezan-Nitao, Elis, Regina Celia Bressan Queiroz Figueiredo, and Luis Fernando Marques-Santos. "Mitochondrial permeability transition pore in sea urchin female gametes." Mechanisms of Development 154 (December 2018): 208–18. http://dx.doi.org/10.1016/j.mod.2018.07.008.

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30

Mareninova, Olga A., Irina V. Odinokova, Moses A. Lee, Ilya Gukovsky, and Anna S. Gukovskaya. "370 Role of Mitochondrial Permeability Transition Pore in Pancreatitis." Gastroenterology 136, no. 5 (May 2009): A—60. http://dx.doi.org/10.1016/s0016-5085(09)60273-0.

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31

Savino, Costanza, PierGiuseppe Pelicci, and Marco Giorgio. "The P66Shc/Mitochondrial Permeability Transition Pore Pathway Determines Neurodegeneration." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/719407.

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Mitochondrial-mediated oxidative stress and apoptosis play a crucial role in neurodegenerative disease and aging. Both mitochondrial permeability transition (PT) and swelling of mitochondria have been involved in neurodegeneration. Indeed, knockout mice for cyclophilin-D (Cyc-D), a key regulatory component of the PT pore (PTP) that triggers mitochondrial swelling, resulted to be protected in preclinical models of multiple sclerosis (MS), Parkinson’s disease (PD), and amyotrophic lateral sclerosis (ALS). However, how neuronal stress is transduced into mitochondrial oxidative stress and swelling is unclear. Recently, the aging determinant p66Shc that generates H2O2reacting with cytochrome c and induces oxidation of PTP and mitochondrial swelling was found to be involved in MS and ALS. To investigate the role of p66Shc/PTP pathway in neurodegeneration, we performed experimental autoimmune encephalomyelitis (EAE) experiments in p66Shc knockout mice (p66Shc−/−), knock out mice for cyclophilin-D (Cyc-D−/−), and p66Shc Cyc-D double knock out (p66Shc/Cyc-D−/−) mice. Results confirm that deletion of p66Shc protects from EAE without affecting immune response, whereas it is not epistatic to the Cyc-D mutation. These findings demonstrate that p66Shc contributes to EAE induced neuronal damage most likely through the opening of PTP suggesting that p66Shc/PTP pathway transduces neurodegenerative stresses.

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32

Batandier, Cécile, Laurent Poulet, Isabelle Hininger, Karine Couturier, Eric Fontaine, Anne-Marie Roussel, and Frédéric Canini. "Acute stress delays brain mitochondrial permeability transition pore opening." Journal of Neurochemistry 131, no. 3 (July 31, 2014): 314–22. http://dx.doi.org/10.1111/jnc.12811.

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33

Petronilli, Valeria, Giovanni Miotto, Marcella Canton, Raffaele Colonna, Paolo Bernardi, and Fabio Di Lisa. "Imaging the mitochondrial permeability transition pore in intact cells." BioFactors 8, no. 3-4 (1998): 263–72. http://dx.doi.org/10.1002/biof.5520080314.

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34

Szabó, Ildikó, and Mario Zoratti. "The mitochondrial permeability transition pore may comprise VDAC molecules." FEBS Letters 330, no. 2 (September 13, 1993): 201–5. http://dx.doi.org/10.1016/0014-5793(93)80273-w.

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35

Szabó, Ildikó, Vito De Pinto, and Mario Zoratti. "The mitochondrial permeability transition pore may comprise VDAC molecules." FEBS Letters 330, no. 2 (September 13, 1993): 206–10. http://dx.doi.org/10.1016/0014-5793(93)80274-x.

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36

Lerch, Markus M., Walter Halangk, and Julia Mayerle. "Preventing Pancreatitis by Protecting the Mitochondrial Permeability Transition Pore." Gastroenterology 144, no. 2 (February 2013): 265–69. http://dx.doi.org/10.1053/j.gastro.2012.12.010.

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37

Zorov, D. B., M. Juhaszova, Y. Yaniv, H. B. Nuss, S. Wang, and S. J. Sollott. "Regulation and pharmacology of the mitochondrial permeability transition pore." Cardiovascular Research 83, no. 2 (May 15, 2009): 213–25. http://dx.doi.org/10.1093/cvr/cvp151.

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38

Hurst, Stephen, Jan Hoek, and Shey-Shing Sheu. "Mitochondrial Ca2+ and regulation of the permeability transition pore." Journal of Bioenergetics and Biomembranes 49, no. 1 (August 6, 2016): 27–47. http://dx.doi.org/10.1007/s10863-016-9672-x.

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39

Montero, Mayte, Laura Vay, Esther Hernández-SanMiguel, Jaime SantoDomingo, Alfredo Moreno, Carmen D. Lobatón, and Javier Alvarez. "S3.19 Mitochondrial free [Ca2+] and the permeability transition pore." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1777 (July 2008): S29. http://dx.doi.org/10.1016/j.bbabio.2008.05.118.

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40

Baines, Christopher P. "The mitochondrial permeability transition pore and ischemia-reperfusion injury." Basic Research in Cardiology 104, no. 2 (February 26, 2009): 181–88. http://dx.doi.org/10.1007/s00395-009-0004-8.

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41

Piantadosi, Claude A., Martha S. Carraway, and Hagir B. Suliman. "Carbon monoxide, oxidative stress, and mitochondrial permeability pore transition." Free Radical Biology and Medicine 40, no. 8 (April 2006): 1332–39. http://dx.doi.org/10.1016/j.freeradbiomed.2005.11.020.

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42

Šileikytė, Justina, and Michael Forte. "The Mitochondrial Permeability Transition in Mitochondrial Disorders." Oxidative Medicine and Cellular Longevity 2019 (May 5, 2019): 1–11. http://dx.doi.org/10.1155/2019/3403075.

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Mitochondrial permeability transition pore (PTP), a (patho)physiological phenomenon discovered over 40 years ago, is still not completely understood. PTP activation results in a formation of a nonspecific channel within the inner mitochondrial membrane with an exclusion size of 1.5 kDa. PTP openings can be transient and are thought to serve a physiological role to allow quick Ca2+ release and/or metabolite exchange between mitochondrial matrix and cytosol or long-lasting openings that are associated with pathological conditions. While matrix Ca2+ and oxidative stress are crucial in its activation, the consequence of prolonged PTP opening is dissipation of the inner mitochondrial membrane potential, cessation of ATP synthesis, bioenergetic crisis, and cell death—a primary characteristic of mitochondrial disorders. PTP involvement in mitochondrial and cellular demise in a variety of disease paradigms has been long appreciated, yet the exact molecular entity of the PTP and the development of potent and specific PTP inhibitors remain areas of active investigation. In this review, we will (i) summarize recent advances made in elucidating the molecular nature of the PTP focusing on evidence pointing to mitochondrial FoF1-ATP synthase, (ii) summarize studies aimed at discovering novel PTP inhibitors, and (iii) review data supporting compromised PTP activity in specific mitochondrial diseases.

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43

Huber, Gavin, Sydney Priest, and Timothy Geisbuhler. "Cardioprotective Effect of Hydroxysafflor Yellow A via the Cardiac Permeability Transition Pore." Planta Medica 84, no. 08 (November 17, 2017): 507–18. http://dx.doi.org/10.1055/s-0043-122501.

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AbstractMyocardial ischemia damages cardiac myocytes in part via opening of the mitochondrial permeability transition pore. Preventing this poreʼs opening is therefore a useful therapeutic goal in treating cardiovascular disease. Hydroxysafflor yellow A has been proposed as a nontoxic alternative to other agents that modulate mitochondrial permeability transition pore opening. In this study, we proposed that hydroxysafflor yellow A prevents mitochondrial permeability transition pore formation in anoxic cardiac myocytes, and thus protects the cell from damage seen during reoxygenation of the cardiac myocytes. Experiments with hydroxysafflor yellow A transport in aerobic myocytes show that roughly 50% of the extracellular dye concentration crosses the cell membrane in a 2-h incubation. In our anoxia/reoxygenation protocol, hydroxysafflor yellow A modulated both the reduction of viability and the loss of rod-shaped cells that attend anoxia and reoxygenation. Hydroxysafflor yellow Aʼs protective effect was similar to that of cyclosporin A, an agent known to inhibit mitochondrial permeability transition pore opening. In additional experiments, plated myocytes were loaded with calcein/MitoTracker Red, then examined for intracellular dye distribution/morphology after anoxia/reoxygenation. Hydroxysafflor yellow A-containing cells showed a cardioprotective pattern similar to that of cyclosporin A (an agent known to close the mitochondrial permeability transition pore). We conclude that hydroxysafflor yellow A can enter the cardiac myocyte and is able to modulate anoxia/reoxygenation-induced damage by interacting with the mitochondrial permeability transition pore.

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44

CROMPTON, Martin. "The mitochondrial permeability transition pore and its role in cell death." Biochemical Journal 341, no. 2 (July 8, 1999): 233–49. http://dx.doi.org/10.1042/bj3410233.

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This article reviews the involvement of the mitochondrial permeability transition pore in necrotic and apoptotic cell death. The pore is formed from a complex of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase and cyclophilin-D (CyP-D) at contact sites between the mitochondrial outer and inner membranes. In vitro, under pseudopathological conditions of oxidative stress, relatively high Ca2+ and low ATP, the complex flickers into an open-pore state allowing free diffusion of low-Mr solutes across the inner membrane. These conditions correspond to those that unfold during tissue ischaemia and reperfusion, suggesting that pore opening may be an important factor in the pathogenesis of necrotic cell death following ischaemia/reperfusion. Evidence that the pore does open during ischaemia/reperfusion is discussed. There are also strong indications that the VDAC-adenine nucleotide translocase-CyP-D complex can recruit a number of other proteins, including Bax, and that the complex is utilized in some capacity during apoptosis. The apoptotic pathway is amplified by the release of apoptogenic proteins from the mitochondrial intermembrane space, including cytochrome c, apoptosis-inducing factor and some procaspases. Current evidence that the pore complex is involved in outer-membrane rupture and release of these proteins during programmed cell death is reviewed, along with indications that transient pore opening may provoke ‘accidental’ apoptosis.

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45

Hom, Jennifer R., Rodrigo A. Quintanilla, David L. Hoffman, Karen L. Bentley, Jeffery D. Molkentin, Shey-Shing Sheu, and George A. Porter. "The Embryonic Mitochondrial Permeability Transition Pore Controls Cardiac Myocyte Mitochondrial Maturation and Differentiation." Biophysical Journal 100, no. 3 (February 2011): 46a—47a. http://dx.doi.org/10.1016/j.bpj.2010.12.452.

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46

De Marchi, Elena, Massimo Bonora, Carlotta Giorgi, and Paolo Pinton. "The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux." Cell Calcium 56, no. 1 (July 2014): 1–13. http://dx.doi.org/10.1016/j.ceca.2014.03.004.

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47

Piriou, Vincent, Pascal Chiari, Odile Gateau-Roesch, Laurent Argaud, Danina Muntean, Delphine Salles, Joseph Loufouat, Pierre-Yves Gueugniaud, Jean-Jacques Lehot, and Michel Ovize. "Desflurane-induced Preconditioning Alters Calcium-induced Mitochondrial Permeability Transition." Anesthesiology 100, no. 3 (March 1, 2004): 581–88. http://dx.doi.org/10.1097/00000542-200403000-00018.

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Background Recent investigations have focused on the pivotal role of the mitochondria in the underlying mechanisms volatile anesthetic-induced myocardial preconditioning. This study aimed at examining the effect of anesthetic preconditioning on mitochondrial permeability transition (MPT) pore opening. Methods Anesthetized open chest rabbits were randomized to one of four groups and underwent 10 min of ischemia, except for the sham 1 group (n = 12). Before this, they underwent a treatment period consisting of (1) no intervention (ischemic group; n = 12), (2) 30 min of desflurane inhalation (8.9% end-tidal concentration) followed by a 15-min washout period (desflurane group; n = 12), or (3) ischemic preconditioning (IPC group; n = 12). A second set of experiments was performed to evaluate the effect of a putative mitochondrial adenosine triphosphate-sensitive potassium channel antagonist, 5-hydroxydecanoate (5-HD). The animals underwent the same protocol as previously, plus pretreatment with 5 mg/kg 5-HD. They were randomized to one of five groups: the sham 2 group, receiving no 5-HD (n = 12); the sham 5-HD group (n = 12); the ischemic 5-HD group (n = 12), the desflurane 5-HD group (n = 12), and the IPC 5-HD group (n = 12). At the end of the protocol, the hearts were excised, and mitochondria were isolated. MPT pore opening was assessed by measuring the amount of calcium required to trigger a massive calcium release indicative of MPT pore opening. Results Desflurane and IPC group mitochondria needed a higher calcium load than ischemic group mitochondria (362 +/- 84, 372 +/- 74, and 268 +/- 110 microM calcium, respectively; P < 0.05) to induce MPT pore opening. The sham 1 and sham 2 groups needed a similar amount of calcium to trigger mitochondrial calcium release (472 +/- 70 and 458 +/- 90 microM calcium, respectively). 5-HD preadministration had no effect on sham animals (458 +/- 90 and 440 +/- 128 microM calcium without and with 5-HD, respectively) and ischemic group animals (268 +/- 110 and 292 +/- 102 microM calcium without and with 5-HD, respectively) but abolished the effects of desflurane on calcium-induced MPT pore opening (362 +/- 84 microM calcium without 5-HD vs. 238 +/- 96 microM calcium with 5-HD; P < 0.05) and IPC (372 +/- 74 microM calcium without 5-HD vs. 270 +/- 104 microM calcium with 5-HD; P < 0.05). Conclusion Like ischemic preconditioning, desflurane improved the resistance of the transition pore to calcium-induced opening. This effect was inhibited by 5-HD, suggesting a link between mitochondrial adenosine triphosphate-sensitive potassium and MPT.

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Jia, Kun, and Heng Du. "Mitochondrial Permeability Transition: A Pore Intertwines Brain Aging and Alzheimer’s Disease." Cells 10, no. 3 (March 15, 2021): 649. http://dx.doi.org/10.3390/cells10030649.

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Advanced age is the greatest risk factor for aging-related brain disorders including Alzheimer’s disease (AD). However, the detailed mechanisms that mechanistically link aging and AD remain elusive. In recent years, a mitochondrial hypothesis of brain aging and AD has been accentuated. Mitochondrial permeability transition pore (mPTP) is a mitochondrial response to intramitochondrial and intracellular stresses. mPTP overactivation has been implicated in mitochondrial dysfunction in aging and AD brains. This review summarizes the up-to-date progress in the study of mPTP in aging and AD and attempts to establish a link between brain aging and AD from a perspective of mPTP-mediated mitochondrial dysfunction.

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Belosludtsev, Konstantin N., Natalia V. Belosludtseva, and Mikhail V. Dubinin. "Diabetes Mellitus, Mitochondrial Dysfunction and Ca2+-Dependent Permeability Transition Pore." International Journal of Molecular Sciences 21, no. 18 (September 8, 2020): 6559. http://dx.doi.org/10.3390/ijms21186559.

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Diabetes mellitus is one of the most common metabolic diseases in the developed world, and is associated either with the impaired secretion of insulin or with the resistance of cells to the actions of this hormone (type I and type II diabetes, respectively). In both cases, a common pathological change is an increase in blood glucose—hyperglycemia, which eventually can lead to serious damage to the organs and tissues of the organism. Mitochondria are one of the main targets of diabetes at the intracellular level. This review is dedicated to the analysis of recent data regarding the role of mitochondrial dysfunction in the development of diabetes mellitus. Specific areas of focus include the involvement of mitochondrial calcium transport systems and a pathophysiological phenomenon called the permeability transition pore in the pathogenesis of diabetes mellitus. The important contribution of these systems and their potential relevance as therapeutic targets in the pathology are discussed.

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Lee, Jong Wha, and Yon Hee Shim. "Mitochondrial Permeability Transition Pore and Cardioprotection Against Ischemia-reperfusion Injury." Journal of the Korean Medical Association 52, no. 10 (2009): 1007. http://dx.doi.org/10.5124/jkma.2009.52.10.1007.

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