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Journal articles on the topic 'Phosphorylation oxidative'

Author: Grafiati

Published: 22 October 2022

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1

Harper, Mary-Ellen, and Martin D. Brand. "Hyperthyroidism stimulates mitochondrial proton leak and ATP turnover in rat hepatocytes but does not change the overall kinetics of substrate oxidation reactions." Canadian Journal of Physiology and Pharmacology 72, no. 8 (August 1, 1994): 899–908. http://dx.doi.org/10.1139/y94-127.

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Thyroid hormones have well-known effects on oxidative phosphorylation, but there is little quantitative information on their important sites of action. We have used top-down elasticity analysis, an extension of metabolic control analysis, to identify the sites of action of thyroid hormones on oxidative phosphorylation in rat hepatocytes. We divided the oxidative phosphorylation system into three blocks of reactions: the substrate oxidation subsystem, the phosphorylating subsystem, and the mitochondrial proton leak subsystem and have identified those blocks of reactions whose kinetics are significantly changed by hyperthyroidism. Our results show significant effects on the kinetics of the proton leak and the phosphorylating subsystems. Quantitative analyses revealed that 43% of the increase in resting respiration rate in hyperthyroid hepatocytes compared with euthyroid hepatocytes was due to differences in the proton leak and 59% was due to differences in the activity of the phosphorylating subsystem. There were no significant effects on the substrate oxidation subsystem. Changes in nonmitochondrial oxygen consumption accounted for −2% of the change in respiration rate. Top-down control analysis revealed that the distribution of control over the rates of mitochondrial oxygen consumption, ATP synthesis and consumption, and proton leak and over mitochondrial membrane potential (Δψm) was similar in hepatocytes from hyperthyroid and littermate-paired euthyroid controls. The results of this study include the first complete top-down elasticity and control analyses of oxidative phosphorylation in hepatocytes from hyperthyroid rats.Key words: thyroid hormones, oxidative phosphorylation, mitochondria, proton leak, thermogenesis.

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2

Nath, Sunil, and John Villadsen. "Oxidative phosphorylation revisited." Biotechnology and Bioengineering 112, no. 3 (January 2, 2015): 429–37. http://dx.doi.org/10.1002/bit.25492.

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3

Hardin, Shane C., Clayton T. Larue, Man-Ho Oh, Vanita Jain, and Steven C. Huber. "Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis." Biochemical Journal 422, no. 2 (August 13, 2009): 305–12. http://dx.doi.org/10.1042/bj20090764.

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The mechanisms involved in sensing oxidative signalling molecules, such as H2O2, in plant and animal cells are not completely understood. In the present study, we tested the postulate that oxidation of Met (methionine) to MetSO (Met sulfoxide) can couple oxidative signals to changes in protein phosphorylation. We demonstrate that when a Met residue functions as a hydrophobic recognition element within a phosphorylation motif, its oxidation can strongly inhibit peptide phosphorylation in vitro. This is shown to occur with recombinant soybean CDPKs (calcium-dependent protein kinases) and human AMPK (AMP-dependent protein kinase). To determine whether this effect may occur in vivo, we monitored the phosphorylation status of Arabidopsis leaf NR (nitrate reductase) on Ser534 using modification-specific antibodies. NR was a candidate protein for this mechanism because Met538, located at the P+4 position, serves as a hydrophobic recognition element for phosphorylation of Ser534 and its oxidation substantially inhibits phosphorylation of Ser534in vitro. Two lines of evidence suggest that Met oxidation may inhibit phosphorylation of NR-Ser534in vivo. First, phosphorylation of NR at the Ser534 site was sensitive to exogenous H2O2 and secondly, phosphorylation in normal darkened leaves was increased by overexpression of the cytosolic MetSO-repair enzyme PMSRA3 (peptide MetSO reductase A3). These results are consistent with the notion that oxidation of surface-exposed Met residues in kinase substrate proteins, such as NR, can inhibit the phosphorylation of nearby sites and thereby couple oxidative signals to changes in protein phosphorylation.

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4

Shoffner, John. "Oxidative Phosphorylation Disease Diagnosis." Seminars in Neurology 19, no. 04 (1999): 341–51. http://dx.doi.org/10.1055/s-2008-1040849.

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5

Terada, H. "Uncouplers of oxidative phosphorylation." Environmental Health Perspectives 87 (July 1990): 213–18. http://dx.doi.org/10.1289/ehp.9087213.

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6

SHOFFNER, JOHN M. "Oxidative Phosphorylation Disease Diagnosis." Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (November 1999): 42. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07817.x.

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7

Lesnefsky, Edward J., and Charles L. Hoppel. "Oxidative phosphorylation and aging." Ageing Research Reviews 5, no. 4 (November 2006): 402–33. http://dx.doi.org/10.1016/j.arr.2006.04.001.

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8

Schatz, Gottfried. "Mitochondria: beyond oxidative phosphorylation." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1271, no. 1 (May 1995): 123–26. http://dx.doi.org/10.1016/0925-4439(95)00018-y.

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9

Hu, Yuanyu, Xueying Wang, Li Zeng, De-Yu Cai, Kanaga Sabapathy, Stephen P. Goff, Eduardo J. Firpo, and Baojie Li. "ERK Phosphorylates p66shcA on Ser36 and Subsequently Regulates p27kip1 Expression via the Akt-FOXO3a Pathway: Implication of p27kip1 in Cell Response to Oxidative Stress." Molecular Biology of the Cell 16, no. 8 (August 2005): 3705–18. http://dx.doi.org/10.1091/mbc.e05-04-0301.

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Mice deficient for p66shcA represent an animal model to link oxidative stress and aging. p66shcA is implicated in oxidative stress response and mitogenic signaling. Phosphorylation of p66shcA on Ser36 is critical for its function in oxidative stress response. Here we report the identification of ERK as the kinase phosphorylating p66shcA on Ser36. Activation of ERKs was necessary and sufficient for Ser36 phosphorylation. p66shcA interacted with ERK and was demonstrated to be a substrate for ERK, with Ser36 being the major phosphorylation site. Furthermore, in response to H2O2, inhibition of ERK activation repressed p66shcA-dependent phosphorylation of FOXO3a and the down-regulation of its target gene p27kip1. Down-regulation of p27 might promote cell survival, as p27 played a proapoptotic role in oxidative stress response. As a feedback regulation, Ser36 phosphorylated p66shcA attenuated H2O2-induced ERK activation, whereas p52/46shcA facilitated ERK activation, which required tyrosine phosphorylation of CH1 domain. p66shcA formed a complex with p52/46ShcA, which may provide a platform for efficient signal propagation. Taken together, the data suggest there exists an interplay between ERK and ShcA proteins, which modulates the expression of p27 and cell response to oxidative stress.

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10

Umida, Yusupova, Mamatova Zulaykho, Dzhabbarova Gulchehra, Tukhtaeva Feruza, and Almatov Karim. "Influence Of Galangin On Respiration And Oxidative Phosphorylation Of Rat Liver Mitochondria." American Journal of Agriculture and Biomedical Engineering 02, no. 06 (June 23, 2020): 14–23. http://dx.doi.org/10.37547/tajabe/volume02issue06-02.

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11

Traylor, Matthew, Christopher D. Anderson, Robert Hurford, Steve Bevan, and Hugh S. Markus. "Oxidative phosphorylation and lacunar stroke." Neurology 86, no. 2 (December 16, 2015): 141–45. http://dx.doi.org/10.1212/wnl.0000000000002260.

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12

Shoffner, John M. "An Introduction: Oxidative Phosphorylation Diseases." Seminars in Neurology 21, no. 03 (2001): 237–50. http://dx.doi.org/10.1055/s-2001-17941.

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13

Porter, Marty H., and Carolyn D. Berdanier. "Oxidative Phosphorylation: Key to Life." Diabetes Technology & Therapeutics 4, no. 2 (April 2002): 253–54. http://dx.doi.org/10.1089/15209150260007471.

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14

Senior, A. E. "ATP synthesis by oxidative phosphorylation." Physiological Reviews 68, no. 1 (January 1, 1988): 177–231. http://dx.doi.org/10.1152/physrev.1988.68.1.177.

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15

Vahsen, Nicola, Céline Candé, Jean-Jacques Brière, Paule Bénit, Nicholas Joza, Nathanael Larochette, Pier Giorgio Mastroberardino, et al. "AIF deficiency compromises oxidative phosphorylation." EMBO Journal 23, no. 23 (November 4, 2004): 4679–89. http://dx.doi.org/10.1038/sj.emboj.7600461.

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16

Skorobogatova, Y. A., S. V. Nesterov, and L. S. Yaguzhinskiy. "Spin control of oxidative phosphorylation." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1837 (July 2014): e31-e32. http://dx.doi.org/10.1016/j.bbabio.2014.05.308.

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17

Solaini, Giancarlo, Gianluca Sgarbi, and Alessandra Baracca. "Oxidative phosphorylation in cancer cells." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1807, no. 6 (June 2011): 534–42. http://dx.doi.org/10.1016/j.bbabio.2010.09.003.

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18

Kalnenieks, U., A. A. de Graaf, S. Bringer-Meyer, and H. Sahm. "Oxidative phosphorylation in Zymomonas mobilis." Archives of Microbiology 160, no. 1 (July 1993): 74–79. http://dx.doi.org/10.1007/bf00258148.

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19

Acin-Perez⁎, Rebeca, and Giovanni Manfredi. "Regulation of oxidative phosphorylation through phosphorylation of cytochrome oxidase." Mitochondrion 11, no. 4 (July 2011): 655. http://dx.doi.org/10.1016/j.mito.2011.03.061.

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20

ROUSSEL, Damien, Jean-François DUMAS, Gilles SIMARD, Yves MALTHIÈRY, and Patrick RITZ. "Kinetics and control of oxidative phosphorylation in rat liver mitochondria after dexamethasone treatment." Biochemical Journal 382, no. 2 (August 24, 2004): 491–99. http://dx.doi.org/10.1042/bj20040696.

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The present investigation was undertaken in order to evaluate the contributions of ATP synthesis and proton leak reactions to the rate of active respiration of liver mitochondria, which is altered following dexamethasone treatment (1.5 mg/kg per day for 5 days). We applied top-down metabolic control analysis and its extension, elasticity analysis, to gain insight into the mechanisms of glucocorticoid regulation of mitochondrial bioenergetics. Liver mitochondria were isolated from dexamethasone-treated, pair-fed and control rats when in a fed or overnight fasted state. Injection of dexamethasone for 5 days resulted in an increase in the fraction of the proton cycle of phosphorylating liver mitochondria, which was associated with a decrease in the efficiency of the mitochondrial oxidative phosphorylation process in liver. This increase in proton leak activity occurred with little change in the mitochondrial membrane potential, despite a significant decrease in the rate of oxidative phosphorylation. Regulation analysis indicates that mitochondrial membrane potential homoeostasis is achieved by equal inhibition of the mitochondrial substrate oxidation and phosphorylation reactions in rats given dexamethasone. Our results also suggest that active liver mitochondria from dexamethasone-treated rats are capable of maintaining phosphorylation flux for cellular purposes, despite an increase in the energetic cost of mitochondrial ATP production due to increased basal proton permeability of the inner membrane. They also provide a complete description of the effects of dexamethasone treatment on liver mitochondrial bioenergetics.

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21

Takeuchi, Norio. "Electrochemical Cells Conducting Mitochondorial Oxidative Phosphorylation and NADH Oxidation." Journal of The Electrochemical Society 136, no. 1 (January 1, 1989): 96–101. http://dx.doi.org/10.1149/1.2096622.

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22

Tardo-Dino, Pierre-Emmanuel, Julianne Touron, Stéphane Baugé, Stéphanie Bourdon, Nathalie Koulmann, and Alexandra Malgoyre. "The effect of a physiological increase in temperature on mitochondrial fatty acid oxidation in rat myofibers." Journal of Applied Physiology 127, no. 2 (August 1, 2019): 312–19. http://dx.doi.org/10.1152/japplphysiol.00652.2018.

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We investigated the effect of temperature increase on mitochondrial fatty acid (FA) and carbohydrate oxidation in the slow-oxidative skeletal muscles (soleus) of rats. We measured mitochondrial respiration at 35°C and 40°C with the physiological substrates pyruvate + 4 mM malate (Pyr) and palmitoyl-CoA (PCoA) + 0.5 mM malate + 2 mM carnitine in permeabilized myofibers under nonphosphorylating ([Formula: see text]) or phosphorylating ([Formula: see text]) conditions. Mitochondrial efficiency was calculated by the respiratory control ratio (RCR = [Formula: see text]/[Formula: see text]). We used guanosine triphosphate (GTP), an inhibitor of uncoupling protein (UCP), to study the mechanisms responsible for alterations of mitochondrial efficiency. We measured hydrogen peroxide (H2O2) production under nonphosphorylating and phosphorylating conditions at both temperatures and substrates. We studied citrate synthase (CS) and 3-hydroxyl acyl coenzyme A dehydrogenase (3-HAD) activities at both temperatures. Elevating the temperature from 35°C to 40°C increased PCoA-[Formula: see text] and decreased PCoA-RCR, corresponding to the uncoupling of oxidative phosphorylation (OXPHOS). GTP blocked the heat-induced increase of PCoA-[Formula: see text]. Rising temperature moved toward a Pyr-[Formula: see text] increase, without significance. Heat did not alter H2O2 production, resulting from either PCoA or Pyr oxidation. Heat induced an increase in 3-HAD but not in CS activities. In conclusion, heat induced OXPHOS uncoupling for PCoA oxidation, which was at least partially mediated by UCP and independent of oxidative stress. The classically described heat-induced glucose shift may actually be mostly due to a less efficient FA oxidation. These findings raise questions concerning the consequences of heat-induced alterations in mitochondrial efficiency of FA metabolism on thermoregulation. NEW & NOTEWORTHY Ex vivo exposure of skeletal myofibers to heat uncouples substrate oxidation from ADP phosphorylation, decreasing the efficiency of mitochondria to produce ATP. This heat effect alters fatty acids (FAs) more than carbohydrate oxidation. Alteration of FA oxidation involves uncoupling proteins without inducing oxidative stress. This alteration in lipid metabolism may underlie the preferential use of carbohydrates in the heat and could decrease aerobic endurance.

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23

Peng, Chunwei, Weibiao Kang, and Yunsong Li. "Respiratory chain complex I is related to oxidative phosphorylation in gastric cancer stem cells." STEMedicine 3, no. 2 (April 4, 2022): e123. http://dx.doi.org/10.37175/stemedicine.v3i2.123.

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Background: Cancer stem cells (CSCs) are the main cause of resistance to anti-cancer drug therapy and distant metastasis of tumors, including gastric cancer. The metabolism of CSCs is an important factor in the maintenance of its stemness. This study is intended to explore the role of oxidative phosphorylation in gastric CSCs. Methods: EpCAM+CD44+ gastric CSCs were sorted from the SGC-7901 cell line. The oxidative phosphorylation and glycolysis were determined by Seahorse experiment, and the oxygen consumption of cells was determined by Clark’s oxygen electrodes. Gene expression and protein levels of mitochondrial proteins belonging to five respiratory chain complexes were checked. Phenformin and siRNA-NDUFB8 were used to inhibit respiratory chain complex I to explore the biological effect of enhanced oxidation phosphorylation in gastric CSCs. Cell migration capacity, proliferation ability, and vascular endothelial growth factor (VEGF) levels were also evaluated. Results: Compared with control cells, the oxidation phosphorylation in mitochondria increased in EpCAM+CD44+ gastric CSCs, although the respiration level remained the same, and no significant changes were observed in glycolysis. Moreover, mRNA and protein expression levels of NDUFB8 in complex I were significantly increased. However, oxidative phosphorylation decreased in EpCAM+CD44+ cells after the treatment of phenformin and siRNA-NDUFB8 compared to the untreated cells. siRNA for NDFUB8 and phenformin inhibition also decreased the ability of cell migration, cell proliferation, as well as the VEGF secretion of gastric CSCs. Conclusion: These results suggest that the increased oxidative phosphorylation was related to respiratory chain complex I and NDUFB8 in gastric CSCs.

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24

Chamberlin, M. E. "Control of oxidative phosphorylation during insect metamorphosis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 287, no. 2 (August 2004): R314—R321. http://dx.doi.org/10.1152/ajpregu.00144.2004.

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The midgut of the tobacco hornworm ( Manduca sexta) is a highly aerobic tissue that is destroyed and replaced by a pupal epithelium at metamorphosis. To determine how oxidative phosphorylation is altered during the programmed death of the larval cells, top-down control analysis was performed on mitochondria isolated from the midguts of larvae before and after the commitment to pupation. Oxygen consumption and protonmotive force (measured as membrane potential in the presence of nigericin) were monitored to determine the kinetic responses of the substrate oxidation system, proton leak, and phosphorylation system to changes in the membrane potential. Mitochondria from precommitment larvae have higher respiration rates than those from postcommitment larvae. State 4 respiration is controlled by the proton leak and the substrate oxidation system. In state 3, the substrate oxidation system exerted 90% of the control over respiration, and this high level of control did not change with development. Elasticity analysis, however, revealed that, after commitment, the activity of the substrate oxidation system falls. This decline may be due, in part, to a loss of cytochrome c from the mitochondria. There are no differences in the kinetics of the phosphorylation system, indicating that neither the F1F0 ATP synthase nor the adenine nucleotide translocase is affected in the early stages of metamorphosis. An increase in proton conductance was observed in mitochondria isolated from postcommitment larvae, indicating that membrane area, lipid composition, or proton-conducting proteins may be altered during the early stages of the programmed cell death of the larval epithelium.

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25

Springett, Roger, Marzena Wylezinska, Ernest B. Cady, Mark Cope, and David T. Delpy. "Oxygen Dependency of Cerebral Oxidative Phosphorylation in Newborn Piglets." Journal of Cerebral Blood Flow & Metabolism 20, no. 2 (February 2000): 280–89. http://dx.doi.org/10.1097/00004647-200002000-00009.

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Changes in hemoglobin oxygenation and oxidation state of the CuA centre of cytochrome oxidase were measured with full spectral near infrared spectroscopy simultaneously with phosphorus metabolites using nuclear magnetic resonance 31P spectroscopy at high time resolution (10 seconds) during transient anoxia (FiO2 = 0.0 for 105 seconds) in the newborn piglet brain. During the onset of anoxia, there was no change in either phosphocreatine (PCr) concentration or the oxidation state of the CuA centre of cytochrome oxidase until there was a substantial fall in cerebral hemoglobin oxygenation, at which point the CuA centre reduced simultaneously with the decline in PCr. At a later time during the anoxia, intracellular pH decreased rapidly, consistent with a fall in cerebral metabolic rate for O2 and reduced flux through the tricarboxylic acid cycle. The simultaneous reduction of CuA and decline in PCr can be explained in terms of the effects of the falling mitochondrial electrochemical potential. From these observations, it is concluded that, at normoxia, oxidative phosphorylation and the oxidation state of the components of the electron transport chain are independent of cerebral oxygenation and that the reduction in the CuA signal occurs when oxygen tension limits the capacity of oxidative phosphorylation to maintain the phosphorylation potential.

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26

Wackerhage, Henning, Uwe Hoffmann, Dieter Essfeld, Dieter Leyk, Klaus Mueller, and Jochen Zange. "Recovery of free ADP, Pi, and free energy of ATP hydrolysis in human skeletal muscle." Journal of Applied Physiology 85, no. 6 (December 1, 1998): 2140–45. http://dx.doi.org/10.1152/jappl.1998.85.6.2140.

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We measured significant undershoots of the concentrations of free ADP ([ADP]) and Pi([Pi]) and the free energy of ATP hydrolysis (Δ G ATP) below initial resting levels during recovery from severe ischemic exercise with 31P-nuclear magnetic resonance spectroscopy in 11 healthy sports students. Undershoots of the rate of oxidative phosphorylation would be predicted if the rate of oxidative phosphorylation would depend solely on free [ADP], [Pi], or Δ G ATP. However, undershoots of the rate of oxidative phosphorylation have not been reported in the literature. Furthermore, undershoots of the rate of oxidative phosphorylation are unlikely because there is evidence that a balance between ATP production and consumption cannot be achieved if an undershoot of the rate of oxidative phosphorylation actually occurs. Therefore, oxidative phosphorylation seems to depend not only on free [ADP], [Pi], or Δ G ATP. An explanation is that acidosis-related or other factors control oxidative phosphorylation additionally, at least under some conditions.

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27

Hirota, Yuko, Dongchon Kang, and Tomotake Kanki. "The Physiological Role of Mitophagy: New Insights into Phosphorylation Events." International Journal of Cell Biology 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/354914.

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Mitochondria play an essential role in oxidative phosphorylation, fatty acid oxidation, and the regulation of apoptosis. However, this organelle also produces reactive oxygen species (ROS) that continually inflict oxidative damage on mitochondrial DNA, proteins, and lipids, which causes further production of ROS. To oppose this oxidative stress, mitochondria possess quality control systems that include antioxidant enzymes and the repair or degradation of damaged mitochondrial DNA and proteins. If the oxidative stress exceeds the capacity of the mitochondrial quality control system, it seems that autophagy degrades the damaged mitochondria to maintain cellular homeostasis. Indeed, recent evidence from yeast to mammals indicates that the autophagy-dependent degradation of mitochondria (mitophagy) contributes to eliminate dysfunctional, aged, or excess mitochondria. In this paper, we describe the molecular processes and regulatory mechanisms of mitophagy in yeast and mammalian cells.

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28

Poppek, Diana, Susi Keck, Gennady Ermak, Tobias Jung, Alexandra Stolzing, Oliver Ullrich, Kelvin J. A. Davies, and Tilman Grune. "Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress." Biochemical Journal 400, no. 3 (November 28, 2006): 511–20. http://dx.doi.org/10.1042/bj20060463.

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Hyperphosphorylated tau proteins accumulate in the paired helical filaments of neurofibrillary tangles seen in such tauopathies as Alzheimer's disease. In the present paper we show that tau turnover is dependent on degradation by the proteasome (inhibited by MG132) in HT22 neuronal cells. Recombinant human tau was rapidly degraded by the 20 S proteasome in vitro, but tau phosphorylation by GSK3β (glycogen synthase kinase 3β) significantly inhibited proteolysis. Tau phosphorylation was increased in HT22 cells by OA [okadaic acid; which inhibits PP (protein phosphatase) 1 and PP2A] or CsA [cyclosporin A; which inhibits PP2B (calcineurin)], and in PC12 cells by induction of a tet-off dependent RCAN1 transgene (which also inhibits PP2B). Inhibition of PP1/PP2A by OA was the most effective of these treatments, and tau hyperphosphorylation induced by OA almost completely blocked tau degradation in HT22 cells (and in cell lysates to which purified proteasome was added) even though proteasome activity actually increased. Many tauopathies involve both tau hyperphosphorylation and the oxidative stress of chronic inflammation. We tested the effects of both cellular oxidative stress, and direct tau oxidative modification in vitro, on tau proteolysis. In HT22 cells, oxidative stress alone caused no increase in tau phosphorylation, but did subtly change the pattern of tau phosphorylation. Tau was actually less susceptible to direct oxidative modification than most cell proteins, and oxidized tau was degraded no better than untreated tau. The combination of oxidative stress plus OA treatment caused extensive tau phosphorylation and significant inhibition of tau degradation. HT22 cells transfected with tau–CFP (cyan fluorescent protein)/tau–GFP (green fluorescent protein) constructs exhibited significant toxicity following tau hyperphosphorylation and oxidative stress, with loss of fibrillar tau structure throughout the cytoplasm. We suggest that the combination of tau phosphorylation and tau oxidation, which also occurs in tauopathies, may be directly responsible for the accumulation of tau aggregates.

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29

Mazur, H. M., V. M. Merlavsky, B. O. Manko, and V. V. Manko. "mPTP opening differently affects electron transport chain and oxidative phosphorylation at succinate and NAD-dependent substrates oxidation in permeabilized rat hepatocytes." Ukrainian Biochemical Journal 92, no. 4 (September 10, 2020): 14–23. http://dx.doi.org/10.15407/ubj92.04.014.

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30

Willis, Wayne T., Elizabeth A. Willis, Jamie Hudgens, and Lawrence J. Mandarino. "KMADP For Oxidative Phosphorylation Depends On Substrate Oxidative Capacity." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859 (September 2018): e64-e65. http://dx.doi.org/10.1016/j.bbabio.2018.09.192.

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31

Perrini, Sebastio, Federica Tortosa, Annalisa Natalicchio, Consiglia Pacelli, Angelo Cignarelli, Vincenzo O. Palmieri, Cristina Caccioppoli, et al. "The p66Shc protein controls redox signaling and oxidation-dependent DNA damage in human liver cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 309, no. 10 (November 15, 2015): G826—G840. http://dx.doi.org/10.1152/ajpgi.00041.2015.

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The p66Shc protein mediates oxidative stress-related injury in multiple tissues. Steatohepatitis is characterized by enhanced oxidative stress-mediated cell damage. The role of p66Shc in redox signaling was investigated in human liver cells and alcoholic steatohepatitis. HepG2 cells with overexpression of wild-type or mutant p66Shc, with Ser36 replacement by Ala, were obtained through infection with recombinant adenoviruses. Reactive oxygen species and oxidation-dependent DNA damage were assessed by measuring dihydroethidium oxidation and 8-hydroxy-2′-deoxyguanosine accumulation into DNA, respectively. mRNA and protein levels of signaling intermediates were evaluated in HepG2 cells and liver biopsies from control and alcoholic steatohepatitis subjects. Exposure to H2O2 increased reactive oxygen species and phosphorylation of p66Shc on Ser36 in HepG2 cells. Overexpression of p66Shc promoted reactive oxygen species synthesis and oxidation-dependent DNA damage, which were further enhanced by H2O2. p66Shc activation also resulted in increased Erk-1/2, Akt, and FoxO3a phosphorylation. Blocking of Erk-1/2 activation inhibited p66Shc phosphorylation on Ser36. Increased p66Shc expression was associated with reduced mRNA levels of antioxidant molecules, such as NF-E2-related factor 2 and its target genes. In contrast, overexpression of the phosphorylation defective p66Shc Ala36 mutant inhibited p66Shc signaling, enhanced antioxidant genes, and suppressed reactive oxygen species and oxidation-dependent DNA damage. Increased p66Shc protein levels and Akt phosphorylation were observed in liver biopsies from alcoholic steatohepatitis compared with control subjects. In human alcoholic steatohepatitis, increased hepatocyte p66Shc protein levels may enhance susceptibility to DNA damage by oxidative stress by promoting reactive oxygen species synthesis and repressing antioxidant pathways.

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32

DUFOUR, Sylvie, Nicole ROUSSE, Paul CANIONI, and Philippe DIOLEZ. "Top-down control analysis of temperature effect on oxidative phosphorylation." Biochemical Journal 314, no. 3 (March 15, 1996): 743–51. http://dx.doi.org/10.1042/bj3140743.

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The effects of temperature on the control of respiration rate, phosphorylation rate, proton leakage rate, the protonmotive force and the effective ATP/O ratio were determined in isolated rat liver mitochondria over a range of respiratory conditions by applying top-down elasticity and control analyses. Simultaneous measurements of membrane potential, oxidation and phosphorylation rates were performed under various ATP turnover rates, ranging from state 4 to state 3. Although the activities of the three subsystems decreased with temperature (over 30-fold between 37 and 4 °C), the effective ATP/O ratio exhibited a maximum at 25 °C, far below the physiological value. Top-down elasticity analysis revealed that maximal membrane potential was maintained over the range of temperature studied, and that the proton leakage rate was considerably reduced at 4 °C. These results definitely rule out a possible uncoupling of mitochondria at low temperature. At 4 °C, the decrease in ATP/O ratio is explained by the relative decrease in phosphorylation processes revealed by the decrease in depolarization after ADP addition [Diolez and Moreau (1985) Biochim. Biophys. Acta 806, 56–63]. The change in depolarization between 37 and 25 °C was too small to explain the decrease in ATP/O ratio. This result is best explained by the changes in the elasticity of proton leakage to membrane potential between 37 and 25 °C, leading to a higher leak rate at 37 °C for the same value of membrane potential. Top-down control analysis showed that despite the important changes in activities of the three subsystems between 37 and 25 °C, the patterns of the control distribution are very similar. However, a different pattern was obtained at 4 °C under all phosphorylating conditions. Surprisingly, control by the proton leakage subsystem was almost unchanged, although both control patterns by substrate oxidation and phosphorylation subsystems were affected at 4 °C. In comparison with results for 25 and 37 °C, at 4 °C there was evidence for increased control by the phosphorylation subsystem over both fluxes of oxidation and phosphorylation as well as on the ATP/O ratio when the system is close to state 3. However, the pattern of control coefficients as a function of mitochondrial activity also showed enhanced control exerted by the substrate oxidation subsystem under all intermediate conditions. These results suggest that passive membrane permeability to protons is not involved in the effect of temperature on the control of oxidative phosphorylation.

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33

Ogura, Masato, Junko Yamaki, Miwako K. Homma, and Yoshimi Homma. "Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components." Biochemical Journal 447, no. 2 (September 26, 2012): 281–89. http://dx.doi.org/10.1042/bj20120509.

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Mitochondrial protein tyrosine phosphorylation is an important mechanism for the modulation of mitochondrial functions. In the present study, we have identified novel substrates of c-Src in mitochondria and investigated their function in the regulation of oxidative phosphorylation. The Src family kinase inhibitor PP2 {amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4d] pyrimidine} exhibits significant reduction of respiration. Similar results were obtained from cells expressing kinase-dead c-Src, which harbours a mitochondrial-targeting sequence. Phosphorylation-site analysis selects c-Src targets, including NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr193 of respiratory complex I and SDHA (succinate dehydrogenase A) at Tyr215 of complex II. The phosphorylation of these sites by c-Src is supported by an in vivo assay using cells expressing their phosphorylation-defective mutants. Comparison of cells expressing wild-type proteins and their mutants reveals that NDUFV2 phosphorylation is required for NADH dehydrogenase activity, affecting respiration activity and cellular ATP content. SDHA phosphorylation shows no effect on enzyme activity, but perturbed electron transfer, which induces reactive oxygen species. Loss of viability is observed in T98G cells and the primary neurons expressing these mutants. These results suggest that mitochondrial c-Src regulates the oxidative phosphorylation system by phosphorylating respiratory components and that c-Src activity is essential for cell viability.

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34

Shoubridge, E. A. "Nuclear genetic defects of oxidative phosphorylation." Human Molecular Genetics 10, no. 20 (October 1, 2001): 2277–84. http://dx.doi.org/10.1093/hmg/10.20.2277.

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35

Xu, Zhongnan, Yueheng Li, Guangquan Mo, Yucheng Zheng, Shaogao Zeng, Ping-Hua Sun, and Zhixiong Ruan. "Electrochemical Oxidative Phosphorylation of Aldehyde Hydrazones." Organic Letters 22, no. 10 (April 28, 2020): 4016–20. http://dx.doi.org/10.1021/acs.orglett.0c01343.

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36

Benard, G., B. Faustin, E. Passerieux, A. Galinier, C. Rocher, N. Bellance, J. P. Delage, L. Casteilla, T. Letellier, and R. Rossignol. "Physiological diversity of mitochondrial oxidative phosphorylation." American Journal of Physiology-Cell Physiology 291, no. 6 (December 2006): C1172—C1182. http://dx.doi.org/10.1152/ajpcell.00195.2006.

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To investigate the physiological diversity in the regulation and control of mitochondrial oxidative phosphorylation, we determined the composition and functional features of the respiratory chain in muscle, heart, liver, kidney, and brain. First, we observed important variations in mitochondrial content and infrastructure via electron micrographs of the different tissue sections. Analyses of respiratory chain enzyme content by Western blot also showed large differences between tissues, in good correlation with the expression level of mitochondrial transcription factor A and the activity of citrate synthase. On the isolated mitochondria, we observed a conserved molar ratio between the respiratory chain complexes and a variable stoichiometry for coenzyme Q and cytochrome c, with typical values of [1–1.5]:[30–135]:[3]:[9–35]:[6.5–7.5] for complex II:coenzyme Q:complex III:cytochrome c:complex IV in the different tissues. The functional analysis revealed important differences in maximal velocities of respiratory chain complexes, with higher values in heart. However, calculation of the catalytic constants showed that brain contained the more active enzyme complexes. Hence, our study demonstrates that, in tissues, oxidative phosphorylation capacity is highly variable and diverse, as determined by different combinations of 1) the mitochondrial content, 2) the amount of respiratory chain complexes, and 3) their intrinsic activity. In all tissues, there was a large excess of enzyme capacity and intermediate substrate concentration, compared with what is required for state 3 respiration. To conclude, we submitted our data to a principal component analysis that revealed three groups of tissues: muscle and heart, brain, and liver and kidney.

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37

Wilson, David F., David K. Harrison, and Sergei A. Vinogradov. "Oxygen, pH, and mitochondrial oxidative phosphorylation." Journal of Applied Physiology 113, no. 12 (December 15, 2012): 1838–45. http://dx.doi.org/10.1152/japplphysiol.01160.2012.

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The oxygen dependence of mitochondrial oxidative phosphorylation was measured in suspensions of isolated rat liver mitochondria using recently developed methods for measuring oxygen and cytochrome c reduction. Cytochrome- c oxidase (energy conservation site 3) activity of the mitochondrial respiratory chain was measured using an artificial electron donor ( N, N, N′, N′-tetramethyl- p-phenylenediamine) and ascorbate to directly reduce the cytochrome c, bypassing sites 1 and 2. For mitochondrial suspensions with added ATP, metabolic conditions approximating those in intact cells and decreasing oxygen pressure both increased reduction of cytochrome c and decreased respiratory rate. The kinetic parameters [ KM and maximal rate ( VM)] for oxygen were determined from the respiratory rates calculated for 100% reduction of cytochrome c. At 22°C, the KM for oxygen is near 3 Torr (5 μM), 12 Torr (22 μM), and 18 Torr (32 μM) at pH 6.9, 7.4, and 7.9, respectively, and VM corresponds to a turnover number for cytochrome c at 100% reduction of near 80/s and is independent of pH. Uncoupling oxidative phosphorylation increased the respiratory rate at saturating oxygen pressures by twofold and decreased the KM for oxygen to <2 Torr at all tested pH values. Mitochondrial oxidative phosphorylation is an important oxygen sensor for regulation of metabolism, nutrient delivery to tissues, and cardiopulmonary function. The decrease in KM for oxygen with acidification of the cellular environment impacts many tissue functions and may give transformed cells a significant survival advantage over normal cells at low-pH, oxygen-limited environment in growing tumors.

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Bose, Salil, Stephanie French, Frank J. Evans, Fredric Joubert, and Robert S. Balaban. "Metabolic Network Control of Oxidative Phosphorylation." Journal of Biological Chemistry 278, no. 40 (July 18, 2003): 39155–65. http://dx.doi.org/10.1074/jbc.m306409200.

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39

Hinkle, Peter C., M. Arun Kumar, Andrea Resetar, and David L. Harris. "Mechanistic stoichiometry of mitochondrial oxidative phosphorylation." Biochemistry 30, no. 14 (April 1991): 3576–82. http://dx.doi.org/10.1021/bi00228a031.

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40

MATSUN-YAGI, Akemi. "A brief view of oxidative phosphorylation." Seibutsu Butsuri 30, no. 3 (1990): 141–45. http://dx.doi.org/10.2142/biophys.30.141.

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41

Radda, G. K., G. J. Kemp, P. Styles, and D. J. Taylor. "Control of oxidative phosphorylation in muscle." Biochemical Society Transactions 21, no. 3 (August 1, 1993): 762–64. http://dx.doi.org/10.1042/bst0210762.

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42

Taylor, R. W., M. A. Birch-Machin, S. Lowerson, H. S. A. Sherratt, I. C. West, K. Bartlett, and D. M. Turnbull. "Defects of oxidative phosphorylation in man." Biochemical Society Transactions 21, no. 3 (August 1, 1993): 804–7. http://dx.doi.org/10.1042/bst0210804.

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43

Matsuno-Yagi, Akemi, and Youssef Hatefi. "Role of energy in oxidative phosphorylation." Journal of Bioenergetics and Biomembranes 20, no. 4 (August 1988): 481–502. http://dx.doi.org/10.1007/bf00762205.

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44

Clerc, Pascaline, Michel Rigoulet, Xavier Leverve, and Eric Fontaine. "Nitric oxide increases oxidative phosphorylation efficiency." Journal of Bioenergetics and Biomembranes 39, no. 2 (April 20, 2007): 158–66. http://dx.doi.org/10.1007/s10863-007-9074-1.

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45

Glick, Gary D. "Inhibiting oxidative phosphorylation restrains autoimmune disease." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857 (August 2016): e14. http://dx.doi.org/10.1016/j.bbabio.2016.04.380.

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46

Korzeniewski, Bernard. "Simulation of oxidative phosphorylation in hepatocytes." Biophysical Chemistry 58, no. 3 (February 1996): 215–24. http://dx.doi.org/10.1016/0301-4622(95)00077-1.

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Salhi, Amel, Alexander C. Jordan, Irineu I. Bochaca, Allison Izsak, Farbod Darvishian, Yariv Houvras, Keith M. Giles, and Iman Osman. "Oxidative Phosphorylation Promotes Primary Melanoma Invasion." American Journal of Pathology 190, no. 5 (May 2020): 1108–17. http://dx.doi.org/10.1016/j.ajpath.2020.01.012.

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Rottenberg, Hagai. "Decoupling of oxidative phosphorylation and photophosphorylation." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1018, no. 1 (July 1990): 1–17. http://dx.doi.org/10.1016/0005-2728(90)90103-b.

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49

Shoffner, John M. "Oxidative phosphorylation defects and Alzheimer's disease." neurogenetics 1, no. 1 (May 1, 1997): 13–19. http://dx.doi.org/10.1007/s100480050002.

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Morava, Eva, Richard Rodenburg, Heidi Zweers van Essen, Maaike De Vries, and Jan Smeitink. "Dietary intervention and oxidative phosphorylation capacity." Journal of Inherited Metabolic Disease 29, no. 4 (June 19, 2006): 589. http://dx.doi.org/10.1007/s10545-006-0227-x.

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