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• Chlamy 2021 Ile des Embiez FR  + (19th International Conference on the Cell and Molecular Biology of Chlamydomonas, Ile des Embiez, France, 2021)
• FEBS 2023 Luso PT  + (1^st 1st FEBS Workshop “Redox Medicine Workshop, Luso, Portugal, 2023)
• MiPschool Schroecken AT 2007  + (1^st MiP''summer school'' on Mitochondrial Respiratory Physiology, 2007 July 12-18, Schroecken, AT.)
• 1st Myocardial Function Symposium 2020 Graz AT  + (1st Myocardial Function Symposium: “Targets in cardiometabolic disease”, Graz, Austria, 2020)
• SHVM 2021 Virtual  + (1st virtual meeting of the Society for Heart and Vascular Metabolism (SHVM), Virtual, 2021)
• Goncalves 2017 J Cell Commun Signal  + (1α,25-Dihydroxyvitamin D<sub>3</s … 1α,25-Dihydroxyvitamin D₃ (1,25-D₃) is critical for the maintenance of normal male reproduction since reduced fertility is observed in vitamin D-deficient rats. Gamma-glutamyl transpeptidase (GGT) is a membrane-bound enzyme that is localized on Sertoli cells and catalyses the transfer of the gamma-glutamyl residues to an amino acid or peptide acceptor. Sertoli cells are also responsible for providing nutrients, as lactate, to the development of germ cells. The aim of this study was to investigate the effect and the mechanism of action of 1,25-D₃ on GGT on Sertoli cell functions from 30-day-old immature rat testis. Results demonstrated that 1,25-D₃ stimulates GGT activity at Sertoli cells plasma membrane through a PKA-dependent mechanism of action, which was not dependent of active ''de novo'' protein synthesis. The hormone increases glucose uptake, as well as lactate production and release by Sertoli cells without altering the reactive oxygen species (ROS) generation. In addition, 1,25-D₃ did not change reduced glutathione (GSH) amount or oxygen consumption, and diminished Sertoli cell death. These findings demonstrate that 1,25-D₃ stimulatory effect on GGT activity, glucose uptake, LDH activity and lactate production seem to be an important contribution of Sertoli cells for germ cells nutrition and for a full and active ongoing spermatogenesis.mportant contribution of Sertoli cells for germ cells nutrition and for a full and active ongoing spermatogenesis.)
• Royall 1993 Arch Biochem Biophys  + (2',7'-Dichlorofluorescein and dihydrorhoda … 2',7'-Dichlorofluorescein and dihydrorhodamine 123 were evaluated as probes for detecting changes in intracellular H2O2 in cultured endothelial cells. Stable intracellular levels of these probes were established within 15 min of exposure to the probe in culture medium. With continued presence of the probe in the medium, intracellular levels were unchanged for 1 h. However, if medium without the probes was used after intracellular loading had occurred, there was a greater than 90% loss of intracellular dichlorofluorescin, dichlorofluorescein, and dihydrorhodamine 123 while intracellular rhodamine 123 decreased by only 15%. Exposure of endothelial cells to exogenous 100 microM H2O2 for 1 h increased intracellular rhodamine 123 by 83%, but there was a reproducible decrease of 53% in intracellular dichlorofluorescein. Exposure to 0.05 mM BCNU plus 10 mM aminotriazole for 2 h increased intracellular rhodamine 123 by 111%. In vitro studies of dihydrorhodamine 123 oxidation were similar to previous reports of dichlorofluorescin oxidation. Oxidation of dihydrorhodamine 123 does not occur with H2O2 alone, but is mediated by a variety of secondary H2O2-dependent intracellular reactions including H2O2-cytochrome c and H2O2-Fe2+. Our results suggest that detection of increased oxidation of these probes in endothelial cells is most useful as a marker of a change in general cellular oxidant production.ge in general cellular oxidant production.)
• Lardy 1953 J Biol Chem  + (2,4-Dinitrophenol greatly enhanced the … 2,4-Dinitrophenol greatly enhanced the liberation of inorganic phosphate from ATP by the nuclear and mitochondrial fraction of rat liver. </br>The microsomal and supernatant fractions did not exhibit this effect. </br></br>With mitochondria (Mw) the rate of phosphate liberation was proportional to the DNP concentration up to 6 X 10-5 M In the presence of excess DNP the rate was proportional to the quantity of Mw nd to time. </br></br>With both fresh and preaged Mw, the response to DNP was much greater </br>in mediums containing salt (either NaCl or KCl) than in isotonic sucrose. Magnesium salts in appreciable concentrations depressed the response of fresh Mw to DNP, but enhanced the response in preaged Mw. Calcium salts, which activate ATP hydrolysis by fresh Mw in the absence of DNP, also depressed the effect of DNP on phosphate liberation. Magnesium salts enhanced phosphate liberation by preaged Mw both in the presence and absence of DNP. Calcium was virtually without effect in preaged Mw. </br></br>Oxalacetate enhanced phosphate liberation from ATP by fresh Mw. This dicarboxylic acid as well as succinate and L-malate depressed the </br>effect of DNP on phosphate liberation. Fatty acids also depressed the </br>effect of DNP. Caprylate enhanced phosphate liberation, probably be- </br>cause of its surface activity. </br></br>The thiol inhibitor, p-chloromercuribenzoate, strongly depressed the effect of DNP; iodoacetate and o-iodosobenzoate did not.</br></br>''Continued in Free Text''ate did not. ''Continued in Free Text'')
• Freitas-Correa 2013 Stem Cell Res  + (2,4-Dinitrophenol (DNP) is a neuroprotecti … 2,4-Dinitrophenol (DNP) is a neuroprotective compound previously shown to promote neuronal differentiation in a neuroblastoma cell line and neurite outgrowth in primary neurons. Here, we tested the hypothesis that DNP could induce neurogenesis in embryonic stem cells (ESCs). Murine ESCs, grown as embryoid bodies (EBs), were exposed to 20μM DNP (or vehicle) for 4days. Significant increases in the proportion of nestin- and β-tubulin III-positive cells were detected after EB exposure to DNP, accompanied by enhanced glial fibrillary acidic protein (GFAP), phosphorylated extracellular signal-regulated kinase (p-ERK) and ATP-linked oxygen consumption, thought to mediate DNP-induced neural differentiation. DNP further protected ESCs from cell death, as indicated by reduced caspase-3 positive cells, and increased proliferation. Cell migration from EBs was significantly higher in DNP-treated EBs, and migrating cells were positive for nestin, ß-tubulin III and MAP2, similar to that observed with retinoic acid (RA)-treated EBs. Compared to RA, however, DNP exerted a marked neuritogenic effect on differentiating ESCs, increasing the average length and number of neurites per cell. Results establish that DNP induces neural differentiation of ESCs, accompanied by cell proliferation, migration and neuritogenesis, suggesting that DNP may be a novel tool to induce neurogenesis in embryonic stem cells.duce neurogenesis in embryonic stem cells.)
• Sebollela 2010 Neurotox Res  + (2,4-Dinitrophenol (DNP) is classically kno … 2,4-Dinitrophenol (DNP) is classically known as a mitochondrial uncoupler and, at high concentrations, is toxic to a variety of cells. However, it has recently been shown that, at subtoxic concentrations, DNP protects neurons against a variety of insults and promotes neuronal differentiation and neuritogenesis. The molecular and cellular mechanisms underlying the beneficial neuroactive properties of DNP are still largely unknown. We have now used DNA microarray analysis to investigate changes in gene expression in rat hippocampal neurons in culture treated with low micromolar concentrations of DNP. Under conditions that did not affect neuronal viability, high-energy phosphate levels or mitochondrial oxygen consumption, DNP induced up-regulation of 275 genes and down-regulation of 231 genes. Significantly, several up-regulated genes were linked to intracellular cAMP signaling, known to be involved in neurite outgrowth, synaptic plasticity, and neuronal survival. Differential expression of specific genes was validated by quantitative RT-PCR using independent samples. Results shed light on molecular mechanisms underlying neuroprotection by DNP and point to possible targets for development of novel therapeutics for neurodegenerative disorders.rapeutics for neurodegenerative disorders.)
• 2014 Mitochondrial Disease Clinical Conference  + (2014 Mitochondrial Disease Clinical Conference, Los Angeles, Ca US; [http://www.mitoaction.org/laconference 2014 Mitochondrial Disease Clinical Conference])
• 2015 Spring PaduaMuscleDays  + (2015 Spring PaduaMuscleDays: Translational Myology in Aging and Neuromuscular Disorders, Padova, IT; [http://www.pagepressjournals.org/index.php/bam/announcement/view/176 2015 Spring PaduaMuscleDays].)
• 2016 Spring PaduaMuscleDays Padua IT  + (2016 Spring PaduaMuscleDays: Muscle Decline in Aging and Neuromuscular Disorders - Mechanisms and Countermeasures, Padua, IT)
• JSBBA 2017 Kyoto JP  + (2017 Annual Meeting of the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA), Kyoto, Japan)
• Movement and Cognition 2018 MA US  + (2018 world conference on Movement and Cognition, Boston, Massachusetts, USA, 2018)
• Movement and Cognition 2019 Tel-Aviv IL  + (2019 World conference on Movement and Cognition, Tel-Aviv, Israel, 2019)
• 2020 PaduaMuscleDays Padua IT  + (2020 PaduaMuscleDays - 30 years of translational research, Vitual Event, 2020)
• Movement and Cognition 2020 Paris FR  + (2020 World conference on Movement and Cognition, Paris, France, 2020)
• EBEC2018 Budapest HU  + (20^th European Bioenergetics Conference 2018, Budapest, Hungary, 2018)
• SHVM 2023 Graz AT  + (20th Annual Meeting of the Society for Heart and Vascular Metabolism (SHVM), Graz, Austria, 2023)
• SFRR 2021 Virtual  + (20th Biennial Meeting of SFRR International, Virtual, 2021)
• International Botanical Congress 2024 Madrid ES  + (20th International Botanical Congress (IBC), Madrid, ES, 2024)
• EBEC2022 Aix-en-Provence FR  + (21^st European Bioenergetics Conference 2022, Aix-en-Provence, France, 2022.)
• EBEC2024 Innsbruck AT  + (22^st European Bioenergetics Conference 2024, Innsbruck, Austria, 2024)
• GFB 2023 Bedoin FR  + (22nd GFB conference, Bedoin, France, 2023)

• 24th Kalorimetrietage 2021 Braunschweig DE  + (24th Kalorimetrietage, Braunschweig, Germany, 2021.)

• 25th Krakow Conference on Endothelium 2017 PL  + (25^th Krakow Conference on Endothelium, Krakow, Poland.)
• SFRR 2018 Auckland NZ  + (26th Meeting for the Society for Free Radical Research Australasia SFRR(A), Auckland, New Zeland, 2018)
• ECSS 2023 Paris FR  + (28^th ECSS Congress, Paris, France, 2023)
• 28th Congress of the Polish Physiological Society 2021 Virtual  + (28th Congress of the Polish Physiological Society, Virtual, 2021)
• FEBS 2022 Mutters AT  + (2^nd FEBS Workshop on Ageing and Regeneration, Mutters, Austria, 2022)
• Cardiovascular Metabolic Disease 2015  + (2nd Annual Conference of the Prevention and Control of Cardiovascular Metabolic Disease, Wuhan, CN; post-conference workshop '''[[MiPNet20.11_IOC102_Wuhan | 102nd Oroboros O2k-Workshop]]'''.)
• Mitochondria-Targeted Drug Development 2022 Boston US  + (2nd Annual Mitochondria-Targeted Drug Development, Boston MA, US, 2022.)
• 2nd International Munich ROS Meeting 2018 Munich DE  + (2nd International Munich ROS Meeting, Munich, Germany, 2018)
• 2nd Mitochondria Conference 2023 Lisbon PT  + (2nd Mitochondria Conference, Lisbon, Portugal, 2023.)
• Pereira 2009 Biochem J  + (3-BrPA (3-bromopyruvate) is an alkylating … 3-BrPA (3-bromopyruvate) is an alkylating agent with antitumoral activity on hepatocellular carcinoma. This compound inhibits cellular ATP production owing to its action on glycolysis and oxidative phosphorylation; however, the specific metabolic steps and mechanisms of 3-BrPA action in human hepatocellular</br>carcinomas, particularly its effects on mitochondrial energetics, are poorly understood. In the present study it was found that incubation of HepG2 cells with a low concentration of 3-BrPA for a short period (150 μMfor 30 min) significantly affected both glycolysis and mitochondrial respiratory functions. The activity of mitochondrial hexokinase was not inhibited by 150 μM 3-BrPA, but this concentration caused more than 70% inhibition of GAPDH (glyceraldehyde-3-phosphate dehydrogenase) and 3-phosphoglycerate kinase activities. Additionally, 3-BrPA treatment significantly impaired lactate production by HepG2 cells, even when glucose was withdrawn from the incubation medium.</br>Oxygen consumption of HepG2 cells supported by either pyruvate/malate or succinate was inhibited when cells were preincubated with 3-BrPA in glucose-free medium. On the other hand, when cells were pre-incubated in glucose-supplemented medium, oxygen consumption was affected only when succinate</br>was used as the oxidizable substrate. An increase in oligomycinindependent</br>respiration was observed in HepG2 cells treated with 3-BrPA only when incubated in glucose-supplemented medium, indicating that 3-BrPA induces mitochondrial proton leakage as well as blocking the electron transport system. The activity</br>of succinate dehydrogenase was inhibited by 70% by 3-BrPA treatment. These results suggest that the combined action of 3- BrPA on succinate dehydrogenase and on glycolysis, inhibiting steps downstream of the phosphorylation of glucose, play an important role in HepG2 cell death.lay an important role in HepG2 cell death.)
• Jardim-Messeder 2012 Int J Biochem Cell Biol  + (3-Bromopyruvate (3BrPA) is an antitumor ag … 3-Bromopyruvate (3BrPA) is an antitumor agent that alkylates the thiol groups of enzymes and has been proposed as a treatment for neoplasias because of its specific reactivity with metabolic energy transducing enzymes in tumor cells. In this study, we show that the sarco/endoplasmic reticulum calcium (Ca²⁺) ATPase (SERCA) type 1 is one of the target enzymes of 3BrPA activity. Sarco/endoplasmic reticulum vesicles (SRV) were incubated in the presence of 1mM 3BrPA, which was unable to inhibit the ATPase activity of SERCA. However, Ca²⁺-uptake activity was significantly inhibited by 80% with 150μM 3BrPA. These results indicate that 3BrPA has the ability to uncouple the ATP hydrolysis from the calcium transport activities. In addition, we observed that the inclusion of 2mM reduced glutathione (GSH) in the reaction medium with different 3BrPA concentrations promoted an increase in 40% in ATPase activity and protects the inhibition promoted by 3BrPA in calcium uptake activity. This derivatization is accompanied by a decrease of reduced cysteine (Cys), suggesting that GSH and 3BrPA increases SERCA activity and transport by pyruvylation and/or S-glutathiolation mediated by GSH at a critical Cys residues of the SERCA.hiolation mediated by GSH at a critical Cys residues of the SERCA.)
• Jardim-Messeder 2016 Anticancer Res  + (3-bromopyruvate (3BrPA) is an antitumor ag … 3-bromopyruvate (3BrPA) is an antitumor agent able to inhibit aerobic glycolysis and oxidative phosphorylation, therefore inducing cell death. However, cancer cells are also highly dependent of glutaminolysis and tricarboxylic acid cycle (TCA) regarding survival and 3BrPA action in these metabolic routes is poorly understood.</br></br>The effect of 3BrPA was characterized in mice liver and kidney mitochondria, as well as in human HepG2 cells.</br></br>Low concentration of 3-BrPA significantly affected both glutaminolysis and TCA cycle functions, through inhibition of isocitrate dehydrogenase, α-ketoglutarate dehydrogenase and succinate dehydrogenase. Additionally, 3-BrPA treatment significantly decreased the reduced status of thiol groups in HepG2 cells without proportional increase of oxidizing groups, suggesting that these chemical groups are the target of alkylation reactions induced by 3-BrPA.</br></br>This work demonstrates, for the first time, the effect of 3-BrPA in glutaminolysis and TCA cycle. Our results suggest that the combined action of 3-BrPA in glutaminolysis, TCA and glycolysis, inhibiting steps downstream of the glucose and glutamine metabolism, has an antitumor effect.</br></br>Copyright© 2016 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved.John G. Delinassios), All rights reserved.)
• Vevera 2016 Physiol Res  + (3-hydroxy-3-methylglutaryl-coenzyme A (HMG … 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors (statins) are widely used drugs for lowering blood lipid levels and preventing cardiovascular diseases. However, statins can have serious adverse effects, which may be related to development of mitochondrial dysfunctions. The aim of study was to demonstrate the ''in vivo'' effect of high and therapeutic doses of statins on mitochondrial respiration in blood platelets. Model approach was used model in the study. Simvastatin was administered to rats at a high dose for 4 weeks. Humans were treated with therapeutic doses of rosuvastatin or atorvastatin for 6 weeks. Platelet mitochondrial respiration was measured using high-resolution respirometry. In rats, a significantly lower physiological respiratory rate was found in intact platelets of simvastatin-treated rats compared to controls. In humans, no significant changes in mitochondrial respiration were detected in intact platelets; however, decreased complex I-linked respiration was observed after statin treatment in permeabilized platelets. We propose that the small ''in vivo'' effect of statins on platelet energy metabolism can be attributed to drug effects on complex I of the electron transport system. Both intact and permeabilized platelets can be used as a readily available biological model to study changes in cellular energy metabolism in patients treated with statins.tabolism in patients treated with statins.)
• JACBS Taipei TW  + (32^th Joint Annual Conference of Biomedical Science, Taipei, Taiwan.)
• APS2020 Chicago US  + (32nd APS Annual Convention, Chicago, USA, 2020)
• 36th Congress Czech Nutrition Society 2020 Hradec Kralove CZ  + (36th annual international congress of Czech Nutrition Society, Hradec Kralove, Czech Republic, 2020)
• 37th Annual Meeting of the ISHR-ES 2023 Porto PT  + (37th Annual Meeting of the ISHR-ES, Porto, Portugal, 2023)
• MiPschool Baton Rouge LA US 2009  + (3^rd MiP''summer school'' on Mitochondrial Respiratory Physiology, 2009 June 17-23, Baton Rouge, Louisiana US.)
• Eugeny I. Schwartz Conference 2015  + (3^rd Russian Congress with International Participation “Molecular Basis of Clinical Medicine: State-of-the-Art and Perspectives” dedicated to the memory of Eugeny I. Schwartz, St. Petersburg , Russia;)
• Ophthalmology Conference 2018 Rome IT  + (3rd Edition of International Conference on Eye and Vision, Rome, Italy; 2018)
• METABO & Cancer 2019 Marseille FR  + (3rd edition - Metabolism and Cancer Meeting, Marseille, France, 2019)
• MacDonald 2014 Abstract MiP2014  + (4-hydroxy-2-oxoglutarate aldolase (HOGA) i … 4-hydroxy-2-oxoglutarate aldolase (HOGA) is a bi-functional mitochondrial enzyme, expressed predominantly in liver and kidney. HOGA is involved in the hydroxyproline degradation pathway (HOGglyoxylate+pyruvate), and mutations in HOGA result in primary Hyperoxaluria Type III, characterized by excessive oxalate production and kidney stone deposition [1]. We hypothesized that HOGA may also be involved in the TCA cycle as an oxaloacetate decarboxylase (oxaloacetatepyruvate; Fig. 1), which may allow the TCA cycle to turnover in the absence of pyruvate and/or excess oxaloacetate. </br>The kinetics of HOGA with substrates HOG and oxaloacetate were investigated by measuring the ''K''’_m and ''k''_cat of recombinant human HOGA, using an LDH-coupled microplate assay. The role of HOGA in the TCA cycle was investigated using mitochondria, isolated from rat liver and kidney, where HOGA is highly expressed, and brain and heart, where expression is lower. ADP-stimulated malate respiration was measured relative to ADP-malate + pyruvate (M:PM), using oxygraphy (Oroboros Oxygraph-2k, note malate was used as oxaloacetate cannot cross the inner mitochondrial membrane).</br> </br>While HOGA was 75% less efficient at cleaving oxaloacetate than its other substrate, HOG (''K''’_m/''k''_cat), the ''K''’_m for oxaloacetate was within range of that estimated for TCA intermediates (''K''’_m,ox=129±8 µM, ''k''_cat,ox=0.52±0.01 s^-1; ''K''’_m,HOG=55±5 µM, ''k''_cat,HOG=1.01±0.03 s^-1). Overall, HOGA appears to use the same catalytic mechanism to cleave both HOG and oxaloacetate substrates. Interestingly, the TCA cycle intermediate a-ketoglutarate was found to be a competitive inhibitor of HOGA oxaloacetate decarboxylase activity (''K''_i=2.8 mM). Mitochondria from rat liver had the highest M:PM respiration relative to all other organs (0.46±0.05, ''P''<0.05). Though kidney had a higher M:PM respiration than heart (0.27±0.02 vs 0.15±0.02, ''P''<0.05 in kidney and heart, respectively), brain respired as well as kidney (0.33±0.04).</br></br> </br>In summary, HOGA cleaves oxaloacetate and HOG using the same catalytic mechanism but was less efficient with oxaloacetate. Liver and kidney have high HOGA expression, and mitochondria from both respire significantly better on malate relative to PM than heart mitochondria. The brain respires just as well with malate compared to kidney, and this may be due to high expression of malic enzyme, which can convert malate directly to pyruvate (Fig. 1). Malate supported respiration in HOGA overexpressing cells will confirm the direct role of HOGA in the TCA cycle.ession of malic enzyme, which can convert malate directly to pyruvate (Fig. 1). Malate supported respiration in HOGA overexpressing cells will confirm the direct role of HOGA in the TCA cycle.)
• MBSJ 2018 Yokohama JP  + (41st Annual Meeting of the Molecular Biology Society of Japan, Yokohama, Japan, 2018.)
• The 42nd Annual Meeting of The Molecular Biology Society of Japan  + (42nd Annual Meeting of The Molecular Biology Society of Japan, Kurume, 2018)
• ISOTT 2015  + (43^rd Annual Meeting of the International Society on Oxygen Transport to Tissue (ISOTT))