Reoxygenation-Induced Mitochondrial Damage is Caused by the Ca2-Dependent Mitochondrial Inner Membrane Permeability Transition

Tanaka, Takaya; Hakoda, Shigeru; Takeyama, Naoshi

doi:10.1016/s0891-5849(98)00017-3

Cited by 11 publications

(6 citation statements)

References 39 publications

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“…Bovine mitochondria were resuspended at 1 mg of protein/ml of 0.3 M mannitol, 10 mM MOPS pH 7.7, 10 mM succinate, 3 M rotenone, 1 mM KH 2 PO 4 , and 10 M EGTA. Changes in the mitochondrial membrane potential were monitored continuously by detection of fluorescence quenching of rhodamine 123 (5 M) (Tamaka et al, 1998) with a spectrofluorometer (RF-5001 PC; Shimadzu, Kyoto, Japan). Fluorescence excited at 503 nm and emitted at 527 nm was measured.…”

Section: Mpt Activity Measured As An Increase In Rhodamine 123mentioning

confidence: 99%

All-trans-Retinoic Acid Binds to and Inhibits Adenine Nucleotide Translocase and induces Mitochondrial Permeability Transition

et al. 2003

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We investigated the effects of retinoic acids on mitochondrial permeability transition (MPT) measured as changes in rhodamine 123 fluorescence from both isolated heart mitochondria and HeLa cells. We report that all-trans-retinoic acid (atRA), 9-cis-retinoic acid, and 13-cis-retinoic acid induce a drop in mitochondrial membrane potential in isolated mitochondria. The atRA effect was done through the induction of MPT because it was dependent on Ca 2ϩ , in a synergic mechanism, and inhibited by cyclosporin A (CsA). Furthermore, atRA also opened MPT in vivo, because treatment of HeLa cells with atRA results in a CsA-sensitive drop of mitochondrial membrane potential. We demonstrated for the first time that retinoic acids inhibit adenine nucleotide translocase (ANT) activity in heart and liver mitochondria. Kinetic studies revealed atRA as an uncompetitive inhibitor of ANT. Photoaffinity labeling of mitochondrial proteins with [3 H]atRA demonstrated the binding of a 31-kDa protein to atRA. This protein was identified as ANT because the presence of carboxyatractyloside, a specific ANT inhibitor, prevented labeling. The specific photolabeling of ANT was also prevented in a concentration-dependent manner by nonlabeled atRA, whereas palmitic acid was ineffective. This study indicates that specific interaction between atRA and ANT takes place regulating MPT opening and adenylate transport. These observations establish a novel mechanism for atRA action, which could control both energetic and apoptotic mitochondrial processes in situations such as retinoic acid treatment.Adenine nucleotide translocase (ANT) is an integral membrane protein of 31 kDa located in mitochondria that catalyzes nucleotide exchange between mitochondria and cytosol. It simultaneously provides ADP for oxidative phosphorylation and ATP to the cytosol for fueling. The existence of two interconvertible conformations of ANT in the mitochondrial membrane has been postulated. The two translocation states of the carrier that correspond to the two conformations are distributed over the cytosol-facing state and matrix-facing state in the presence of ADP or ATP (for reviews, see Klingenberg, 1989;Brandolin et al., 1993).

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Section: Mpt Activity Measured As An Increase In Rhodamine 123mentioning

confidence: 99%

All-trans-Retinoic Acid Binds to and Inhibits Adenine Nucleotide Translocase and induces Mitochondrial Permeability Transition

et al. 2003

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“…The time setting of 24 h after IR also seemed interesting because clinical hepatic functional failure is more apparent a few days after IR. The loss of ⌬ ⌿ is implicated in the pore opening of the mitochondrial inner membrane and development of mitochondrial swelling resulting from massive and abrupt release of accumulated Ca 2+ during hepatic IR injury [37] . In addition, the mitochondrial permeability transition has been shown to play an important role by causing the cessation of respiration and oxidative phosphorylation as well as by facilitating the release of apoptogenic factors [38] .…”

Section: Discussionmentioning

confidence: 99%

Modification of the Hepatic Mitochondrial Proteome in Response to Ischemic Preconditioning following Ischemia-Reperfusion Injury of the Rat Liver

et al. 2007

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Background/Aim: Ischemic preconditioning (IPC) may reduce hepatic ischemia-reperfusion (IR) injury, but efficacy of IPC on mitochondrial proteome is not demonstrated. We investigated how IPC modifies the mitochondrial proteome after IR injury. Methods: Rats were subjected to 25 min of portal triad crossclamping (IR group, n = 8). In the IPC group (n = 8), 10 min of temporal portal triad clamping was performed before 25 min of portal clamping. Samples were obtained after 24 h. The mitochondrial inner-membrane potential was measured by the uptake of a lipophilic cationic carbocyanine probe and mitochondrial proteome was also investigated using 2-dimensional differential in-gel electrophoresis and liquid chromatography-tandem mass spectrometry. Results: Mitochondrial inner-membrane potential and glutathione were lower and serum transaminase was higher in the IPC group than in the IR group. The mitochondrial precursor of aldehyde dehydrogenase 2 and α-methylacyl-CoA-racemase were upregulated in the IPC group in comparison to the IR group. In contrast, protein disulfide-isomerase A3 precursor, 60S acid ribosomal protein P0, carbonic anhydrase 3 and superoxide dismutase were significantly more downregulated in the IPC group than in the IR group. Conclusions: A hepatoprotective effect by IPC was not shown; however, IPC caused significant up- or downregulation of several mitochondrial proteins.

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“…Depending on the isolation procedure the latter was shown to change in both directions. 6,7,13,14 Dephosphorylation of cytochrome oxidase through Ca 2+ -activated phosphatases is supposed to increase membrane potential, [15][16][17] while aging was reported to drastically decrease membrane potential. [18][19][20] Nevertheless, in both cases ROS formation was observed.…”

Section: The Effect Of Oxygen Tension Appliedmentioning

confidence: 99%

Are mitochondria a spontaneous and permanent source of reactive oxygen species?

Nohl¹,

Gille²,

Kozlov³

et al. 2003

Redox Report

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The bioenergetic properties of mitochondria in combination with the high turnover rate of dioxygen qualify these organelles for the formation of reactive oxygen species (ROS). The assumption that mitochondria are the major intracellular source of ROS was essentially based on in vitro experiments with isolated mitochondria. The transfer of these data to the living cell may, however, be incorrect. Artefacts due to the preparation procedure or inadequate detection methods of ROS may lead to false positive results. Inhomogeneous results were found to be due to an interaction of the detection system with components of the respiratory chain which could be avoided by a recently developed non-invasive method. One of the most critical electron transfer steps in the respiratory chain is the electron bifurcation from ubiquinol to the cytochrome bc(1) complex. This electron bifurcation requires the free mobility of the head domain of the Rieske iron-sulfur protein. Inhibition of electron bifurcation by antimycin A causes leakage of single electrons to oxygen which results in the release of ROS. Hindrance of electron bifurcation was also observed following alterations of the physical state of membrane phospholipids in which the cytochrome bc(1) complex is inserted. Irrespective of whether the fluidity of the membrane was elevated or decreased, electron flow rates to the Rieske iron-sulfur protein were drastically reduced. Concomitantly superoxide radicals were released from these mitochondria, strongly suggesting the involvement of the ubiquinol/cytochrome bc(1) redox couple in this process.

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Reoxygenation-Induced Mitochondrial Damage is Caused by the Ca2-Dependent Mitochondrial Inner Membrane Permeability Transition

Cited by 11 publications

References 39 publications

All-trans-Retinoic Acid Binds to and Inhibits Adenine Nucleotide Translocase and induces Mitochondrial Permeability Transition

All-trans-Retinoic Acid Binds to and Inhibits Adenine Nucleotide Translocase and induces Mitochondrial Permeability Transition

Modification of the Hepatic Mitochondrial Proteome in Response to Ischemic Preconditioning following Ischemia-Reperfusion Injury of the Rat Liver

Are mitochondria a spontaneous and permanent source of reactive oxygen species?

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