TY - CONF AU - Kokas, Márton AU - Kirchlechner-Farkas, Judit Mária AU - Gáspár, Dániel AU - Komlódi, Tímea AU - Ozohanics, Olivér AU - Környei, Zsuzsanna AU - Sváb, Gergely AU - Tretter, László TI - METABOLIKUS POLIHISZTOR VAGY EGYSZERŰ GLUTAMINGYÁR? – CITRÁTKÖR AZ ASZTROCITÁKBAN T2 - Membrán-Transzport konferencia : programfüzet PB - Pécsi Tudományegytem C1 - Sümeg C1 - Pécs PY - 2023 UR - https://m2.mtmt.hu/api/publication/34030843 ID - 34030843 LA - Hungarian DB - MTMT ER - TY - CHAP AU - Tretter, László ED - Mandl, József ED - Csala, Miklós TI - Aminosav-, fehérje-anyagcsere T2 - Orvosi patobiokémia PB - Medicina Könyvkiadó CY - Budapest SN - 9789632267821 PY - 2023 SP - 121 EP - 142 PG - 22 UR - https://m2.mtmt.hu/api/publication/34722580 ID - 34722580 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Weidinger, A. AU - Milivojev, N. AU - Hosmann, A. AU - Duvigneau, J.C. AU - Szabo, C. AU - Törö, G. AU - Rauter, L. AU - Vaglio-Garro, A. AU - Mkrtchyan, G.V. AU - Trofimova, L. AU - Sharipov, R.R. AU - Surin, A.M. AU - Krasilnikova, I.A. AU - Pinelis, V.G. AU - Tretter, László AU - Moldzio, R. AU - Bayır, H. AU - Kagan, V.E. AU - Bunik, V.I. AU - Kozlov, A.V. TI - Oxoglutarate dehydrogenase complex controls glutamate-mediated neuronal death JF - REDOX BIOLOGY J2 - REDOX BIOL VL - 62 PY - 2023 PG - 15 SN - 2213-2317 DO - 10.1016/j.redox.2023.102669 UR - https://m2.mtmt.hu/api/publication/33718236 ID - 33718236 LA - English DB - MTMT ER - TY - JOUR AU - Daradics, Noémi AU - Horváth, Gergő AU - Tretter, László AU - Paál, Ágnes AU - Fülöp, András AU - Budai, András AU - Szijártó, Attila TI - The effect of Cyclophilin D depletion on liver regeneration following associating liver partition and portal vein ligation for staged hepatectomy JF - PLOS ONE J2 - PLOS ONE VL - 17 PY - 2022 IS - 7 PG - 15 SN - 1932-6203 DO - 10.1371/journal.pone.0271606 UR - https://m2.mtmt.hu/api/publication/32989211 ID - 32989211 N1 - These authors contributed equally to this work: Andras Budai, Attila Szijarto AB - Associating Liver Partition and Portal vein ligation for Staged hepatectomy (ALPPS) is a modification of two-stage hepatectomy profitable for patients with inoperable hepatic tumors by standard techniques. Unfortunately, initially poor postoperative outcome was associated with ALPPS, in which mitochondrial dysfunction played an essential role. Inhibition of cyclophilins has been already proposed to be efficient as a mitochondrial therapy in liver diseases. To investigate the effect of Cyclophilin D (CypD) depletion on mitochondrial function, biogenesis and liver regeneration following ALPPS a CypD knockout (KO) mice model was created.Male wild type (WT) (n = 30) and CypD KO (n = 30) mice underwent ALPPS procedure. Animals were terminated pre-operatively and 24, 48, 72 or 168 h after the operation. Mitochondrial functional studies and proteomic analysis were performed. Regeneration rate and mitotic activity were assessed.The CypD KO group displayed improved mitochondrial function, as both ATP production (P < 0.001) and oxygen consumption (P < 0.05) were increased compared to the WT group. The level of mitochondrial biogenesis coordinator peroxisome proliferator-activated receptor γ co-activator 1-α (PGC1-α) was also elevated in the CypD KO group (P < 0.001), which resulted in the induction of the mitochondrial oxidative phosphorylation system. Liver growth increased in the CypD KO group compared to the WT group (P < 0.001).Our study demonstrates the beneficial effect of CypD depletion on the mitochondrial vulnerability following ALPPS. Based on our results we propose that CypD inhibition should be further investigated as a possible mitochondrial therapy following ALPPS. LA - English DB - MTMT ER - TY - JOUR AU - Horváth, Gergő AU - Sváb, Gergely AU - Komlódi, Tímea AU - Ravasz, Dóra AU - Kacsó, Gergely AU - Dóczi, Judit AU - Chinopoulos, Christos AU - Ambrus, Attila AU - Tretter, László TI - Reverse and Forward Electron Flow-Induced H2O2 Formation Is Decreased in α-Ketoglutarate Dehydrogenase (α-KGDH) Subunit (E2 or E3) Heterozygote Knock Out Animals JF - ANTIOXIDANTS J2 - ANTIOXIDANTS-BASEL VL - 11 PY - 2022 IS - 8 PG - 19 SN - 2076-3921 DO - 10.3390/antiox11081487 UR - https://m2.mtmt.hu/api/publication/33070137 ID - 33070137 N1 - Cited By :1 Export Date: 7 October 2022 Correspondence Address: Tretter, L.; Department of Biochemistry, Hungary; email: tretter.laszlo@med.semmelweis-univ.hu Funding details: Semmelweis Egyetem, STIA-OTKA-2021, TKP2021-EGA-25 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, EFOP-3.6.3-VEKOP-16-2017-00009 Funding text 1: This research was funded by the Hungarian Brain Research Program 2 (2017-1.2.1-NKP-2017-00002 to Vera Adam-Vizi, Semmelweis University), STIA-OTKA-2021 grant (from the Semmelweis University, to A.A.), TKP2021-EGA-25 grant to A.A. and C.C., Project no. TKP2021-EGA-25 has been implemented with the support provided by the Ministry of Innovation and Technology of Hungary from the National Research, Development and Innovation Fund, financed under the TKP2021-EGA funding scheme. EFOP-3.6.3-VEKOP-16-2017-00009 support to G.S. AB - α-ketoglutarate dehydrogenase complex (KGDHc), or 2-oxoglutarate dehydrogenase complex (OGDHc) is a rate-limiting enzyme in the tricarboxylic acid cycle, that has been identified in neurodegenerative diseases such as in Alzheimer’s disease. The aim of the present study was to establish the role of the KGDHc and its subunits in the bioenergetics and reactive oxygen species (ROS) homeostasis of brain mitochondria. To study the bioenergetic profile of KGDHc, genetically modified mouse strains were used having a heterozygous knock out (KO) either in the dihydrolipoyl succinyltransferase (DLST+/−) or in the dihydrolipoyl dehydrogenase (DLD+/−) subunit. Mitochondrial oxygen consumption, hydrogen peroxide (H2O2) production, and expression of antioxidant enzymes were measured in isolated mouse brain mitochondria. Here, we demonstrate that the ADP-stimulated respiration of mitochondria was partially arrested in the transgenic animals when utilizing α-ketoglutarate (α-KG or 2-OG) as a fuel substrate. Succinate and α-glycerophosphate (α-GP), however, did not show this effect. The H2O2 production in mitochondria energized with α-KG was decreased after inhibiting the adenine nucleotide translocase and Complex I (CI) in the transgenic strains compared to the controls. Similarly, the reverse electron transfer (RET)-evoked H2O2 formation supported by succinate or α-GP were inhibited in mitochondria isolated from the transgenic animals. The decrease of RET-evoked ROS production by DLST+/− or DLD+/− KO-s puts the emphasis of the KGDHc in the pathomechanism of ischemia-reperfusion evoked oxidative stress. Supporting this notion, expression of the antioxidant enzyme glutathione peroxidase was also decreased in the KGDHc transgenic animals suggesting the attenuation of ROS-producing characteristics of KGDHc. These findings confirm the contribution of the KGDHc to the mitochondrial ROS production and in the pathomechanism of ischemia-reperfusion injury. LA - English DB - MTMT ER - TY - CONF AU - Kokas, Márton AU - Horváth, Gergő AU - Tretter, László TI - AZ α-KETOGLUTARÁT-DEHIDROGENÁZ KOMPLEX DLST+/- ÉS DLD+/- ALEGYSÉGEK KIÜTÉSÉNEK HATÁSA AZ OXIGÉNFOGYASZTÁSRA ÉS REAKTÍV OXIGÉNGYÖKKÉPZŐDÉSRE EGÉR AGYI MITOKONDRIUMOKON T2 - 51. Membrán-Transzport Konferencia PY - 2022 UR - https://m2.mtmt.hu/api/publication/34030854 ID - 34030854 LA - Hungarian DB - MTMT ER - TY - GEN AU - Kokas, Márton AU - Sváb, Gergely AU - Tretter, László TI - A metilénkék hatása a citokróm-c redox állapotára in vivo és in vitro körülmények között PY - 2021 UR - https://m2.mtmt.hu/api/publication/34036737 ID - 34036737 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Sváb, Gergely AU - Kokas, Márton AU - Sipos, Ildikó AU - Ambrus, Attila AU - Tretter, László TI - Methylene Blue Bridges the Inhibition and Produces Unusual Respiratory Changes in Complex III-Inhibited Mitochondria. Studies on Rats, Mice and Guinea Pigs JF - ANTIOXIDANTS J2 - ANTIOXIDANTS-BASEL VL - 10 PY - 2021 IS - 2 PG - 18 SN - 2076-3921 DO - 10.3390/antiox10020305 UR - https://m2.mtmt.hu/api/publication/31887594 ID - 31887594 N1 - Funding details: KTIA_13_NAP-A-III/6 Funding details: 61826 690289, 61830Z0100 Funding details: Hungarian Scientific Research Fund, OTKA, NK 112230 Funding details: Magyar Tudományos Akadémia, MTA, MTA TKI 02001 Funding text 1: Funding: This research was funded by grants from the Hungarian Brain Research Program (KTIA_13_NAP-A-III/6 and 2017-1.2.1-NKP-2017-00002), OTKA (NK 112230), Hungarian Academy of Sciences (MTA TKI 02001) [all to Vera Adam-Vizi], and Hungarian Higher Education Institution Excellence Program (FIKP grants 61826 690289 EATV and 61830Z0100 EATV) [to A.A.]. LA - English DB - MTMT ER - TY - JOUR AU - Veres, Balázs AU - Erős, Krisztián AU - Antus, Csenge Petra AU - Kálmán, Nikoletta AU - Fónai, Fruzsina AU - Jakus, Péter AU - Boros, Éva AU - Hegedűs, Zoltán AU - Nagy, István AU - Tretter, László AU - Gallyas, Ferenc AU - Sümegi, Balázs TI - Cyclophilin D-dependent mitochondrial permeability transition amplifies inflammatory reprogramming in endotoxemia JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 11 PY - 2021 IS - 3 SP - 684 EP - 704 PG - 21 SN - 2211-5463 DO - 10.1002/2211-5463.13091 UR - https://m2.mtmt.hu/api/publication/31822211 ID - 31822211 AB - Microorganisms or LPS (lipopolysaccharide), an outer membrane component of Gram-negative bacteria, can induce a systemic inflammatory response that leads to sepsis, multiple organ dysfunction, and mortality. Here, we investigated the role of cyclophilin D (CypD)-dependent mitochondrial permeability transition (mPT) in the immunosuppressive phase of LPS-induced endotoxic shock. The liver plays an important role in immunity and organ dysfunction; therefore, we used liver RNA sequencing (RNAseq) data, Ingenuity® Pathway Analysis (IPA ® ) to investigate the complex role of mPT formation in inflammatory reprogramming and disease progression. LPS induced significant changes in the expression of 2844 genes, affecting 179 pathways related to mitochondrial dysfunction, defective oxidative phosphorylation, nitric oxide (NO) and reactive oxygen species (ROS) accumulation, nuclear factor, erythroid 2 like 2 (Nrf2), Toll-like receptors (TLRs), and tumor necrosis factor α receptor (TNFR)-mediated processes in wild-type mice. The disruption of CypD reduced LPS-induced alterations in gene expression and pathways involving TNFRs and TLRs, in addition to improving survival and attenuating oxidative liver damage and the related NO- and ROS-producing pathways. CypD deficiency diminished the suppressive effect of LPS on mitochondrial function, nuclear- and mitochondrial-encoded genes, and mitochondrial DNA (mtDNA) quantity, which could be critical in improving survival. Our data propose that CypD-dependent mPT is an amplifier in inflammatory reprogramming and promotes disease progression. The mortality in human sepsis and shock is associated with mitochondrial dysfunction. Prevention of mPT by CypD disruption reduces inflammatory reprogramming, mitochondrial dysfunction, and lethality; therefore, CypD can be a novel drug target in endotoxic shock and related inflammatory diseases. LA - English DB - MTMT ER - TY - JOUR AU - Mikulás, Krisztina Ágnes AU - Komlódi, Tímea AU - Földes, Anna AU - Sváb, Gergely AU - Horváth, Gergő AU - Nagy, Ádám Miklós AU - Ambrus, Attila AU - Gyulai-Gaál, Szabolcs AU - Gera, István AU - Hermann, Péter AU - Varga, Gábor AU - Tretter, László TI - Bioenergetic impairment of triethylene glycol dimethacrylate- (TEGDMA-) treated dental pulp stem cells (DPSCs) and isolated brain mitochondria are amended by redox compound methylene blue JF - MATERIALS J2 - MATERIALS VL - 13 PY - 2020 IS - 16 PG - 19 SN - 1996-1944 DO - 10.3390/ma13163472 UR - https://m2.mtmt.hu/api/publication/31595275 ID - 31595275 N1 - Funding Agency and Grant Number: Hungarian Brain Research Program [KTIA_13_NAP-A-III/6, 2017-1.2.1-NKP-2017-00002]; OTKAOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [NK 112230]; Hungarian Academy of SciencesHungarian Academy of Sciences [MTA TKI 02001]; Hungarian Human Resources Development Operational Program [EFOP-3.6.2-16-2017-00006]; Competition of Faculty of Dentistry, Semmelweis University; Higher Education Institutional Excellence Programme of the Ministry for Innovation and Technology in Hungary of the Semmelweis University [FIKP 61826 690289 EATV] Funding text: This work was supported by grants to the Hungarian Brain Research Program (KTIA_13_NAP-A-III/6 and 2017-1.2.1-NKP-2017-00002), OTKA (NK 112230), and the Hungarian Academy of Sciences (MTA TKI 02001), all to Vera Adam-Vizi, Hungarian Human Resources Development Operational Program (EFOP-3.6.2-16-2017-00006) to Gabor Varga and Anna Foldes, Competition of Faculty of Dentistry, Semmelweis University 2016 to Krisztina Mikulas. "The research was also financed by the Higher Education Institutional Excellence Programme of the Ministry for Innovation and Technology in Hungary, within the framework of the Neurology thematic programme of the Semmelweis University to Attila Ambrus (FIKP 61826 690289 EATV). AB - Background: Triethylene glycol dimethacrylate (TEGDMA) monomers released from resin matrix are toxic to dental pulp cells, induce apoptosis, oxidative stress and decrease viability. Recently, mitochondrial complex I (CI) was identified as a potential target of TEGDMA. In isolated mitochondria supported by CI, substrates oxidation and ATP synthesis were inhibited, reactive oxygen species production was stimulated. Contrary to that, respiratory Complex II was not impaired by TEGDMA. The beneficial effects of electron carrier compound methylene blue (MB) are proven in many disease models where mitochondrial involvement has been detected. In the present study, the bioenergetic effects of MB on TEGDMA-treated isolated mitochondria and on human dental pulp stem cells (DPSC) were analyzed. Methods: Isolated mitochondria and DPSC were acutely exposed to low millimolar concentrations of TEGDMA and 2 μM concentration of MB. Mitochondrial and cellular respiration and glycolytic flux were measured by high resolution respirometry and by Seahorse XF extracellular analyzer. Mitochondrial membrane potential was measured fluorimetrically. Results: MB partially restored the mitochondrial oxidation, rescued membrane potential in isolated mitochondria and significantly increased the impaired cellular O2 consumption in the presence of TEGDMA. Conclusion: MB is able to protect against TEGDMA-induced CI damage, and might provide protective effects in resin monomer exposed cells. © 2020 by the authors. LA - English DB - MTMT ER - TY - JOUR AU - Saskői, Éva AU - Hujber, Zoltán AU - Nyírő, Gábor AU - Likó, István AU - Mátyási, Barbara AU - Petővári, Gábor AU - Mészáros, Katalin AU - Kovács, Attila Lajos AU - Patthy, László AU - Supekar, Shreyas AU - Fan, Hao AU - Sváb, Gergely AU - Tretter, László AU - Sarkar, Arunabh AU - Nazir, Aamir AU - Sebestyén, Anna AU - Patócs, Attila Balázs AU - Mehta, Anil AU - Vellainé Takács, Krisztina TI - The SDHB Arg230His mutation causing familial paraganglioma alters glycolysis in a new Caenorhabditis elegans model JF - DISEASE MODELS & MECHANISMS J2 - DIS MODEL MECH VL - 13 PY - 2020 IS - 10 PG - 15 SN - 1754-8403 DO - 10.1242/dmm.044925 UR - https://m2.mtmt.hu/api/publication/31523868 ID - 31523868 N1 - These authors contributed equally to this work: Anil Mehta and Krisztina Takács-Vellai LA - English DB - MTMT ER - TY - JOUR AU - Budai, András AU - Horváth, Gergő AU - Tretter, László AU - Radák, Zsolt AU - Koltai, Erika AU - Bori, Zoltán AU - Torma, Ferenc Gergely AU - Lukáts, Ákos AU - Röhlich, Pál AU - Szijártó, Attila AU - Fülöp, András TI - Mitochondrial function after associating liver partition and portal vein ligation for staged hepatectomy in an experimental model JF - BRITISH JOURNAL OF SURGERY J2 - BRIT J SURG VL - 106 PY - 2019 IS - 1 SP - 120 EP - 131 PG - 12 SN - 0007-1323 DO - 10.1002/bjs.10978 UR - https://m2.mtmt.hu/api/publication/3426954 ID - 3426954 LA - English DB - MTMT ER - TY - JOUR AU - Sváb, Gergely AU - Dóczi, Judit AU - Gerencsér, Ákos AU - Ambrus, Attila AU - Gallyas, Ferenc AU - Sümegi, Balázs AU - Tretter, László TI - The Mitochondrial Targets of Neuroprotective Drug Vinpocetine on Primary Neuron Cultures, Brain Capillary Endothelial Cells, Synaptosomes, and Brain Mitochondria JF - NEUROCHEMICAL RESEARCH J2 - NEUROCHEM RES VL - 44 PY - 2019 IS - 10 SP - 2435 EP - 2447 PG - 13 SN - 0364-3190 DO - 10.1007/s11064-019-02871-9 UR - https://m2.mtmt.hu/api/publication/30810275 ID - 30810275 AB - Vinpocetine is considered as neuroprotectant drug and used for treatment of brain ischemia and cognitive deficiencies for decades. A number of enzymes, channels and receptors can bind vinpocetine, however the mechanisms of many effects' are still not clear. The present study investigated the effects of vinpocetine from the mitochondrial bioenergetic aspects. In primary brain capillary endothelial cells the purinergic receptor-stimulated mitochondrial Ca2+ uptake and efflux were studied. Vinpocetine exerted a partial inhibition on the mitochondrial calcium efflux. In rodent brain synaptosomes vinpocetine (30 μM) inhibited respiration in uncoupler stimulated synaptosomes and decreased H2O2 release from the nerve terminals in resting and in complex I inhibited conditions, respectively. In isolated rat brain mitochondria using either complex I or complex II substrates leak respiration was stimulated, but ADP-induced respiration was inhibited by vinpocetine. The stimulation of oxidation was associated with a small extent of membrane depolarization. Mitochondrial H2O2 production was inhibited by vinpocetine under all conditions investigated. The most pronounced effects were detected with the complex II substrate succinate. Vinpocetine also mitigated both Ca2+-induced mitochondrial Ca2+-release and Ca2+-induced mitochondrial swelling. It lowered the rate of mitochondrial ATP synthesis, while increasing ATPase activity. These results indicate more than a single mitochondrial target of this vinca alkaloid. The relevance of the affected mitochondrial mechanisms in the anti ischemic effect of vinpocetine is discussed. LA - English DB - MTMT ER - TY - CHAP AU - Sváb, Gergely AU - Tretter, László AU - Szederkényi, Gábor ED - Vassányi, István TI - Modeling of phenylalanine metabolism and its medical relevance T2 - Proceedings of the Pannonian Conference on Advances in Information Technology (PCIT'2019) PB - University of Pannonia, Faculty of Information Technology CY - Veszprém SN - 9789633961278 PY - 2019 SP - 49 EP - 58 PG - 10 UR - https://m2.mtmt.hu/api/publication/30878884 ID - 30878884 LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Emese AU - Maléth, József AU - Závogyán, Noémi AU - Fanczal, Júlia AU - Grassalkovich, Anna AU - Erdős, Réka AU - Pallagi, Petra AU - Horváth, Gergő AU - Tretter, László AU - Bálint, Emese Réka AU - Rakonczay, Zoltán AU - Venglovecz, Viktória AU - Hegyi, Péter TI - Novel mitochondrial transition pore inhibitor N-methyl-4-isoleucine cyclosporin is a new therapeutic option in acute pancreatitis JF - JOURNAL OF PHYSIOLOGY-LONDON J2 - J PHYSIOL-LONDON VL - 597 PY - 2019 IS - 24 SP - 5879 EP - 5898 PG - 20 SN - 0022-3751 DO - 10.1113/JP278517 UR - https://m2.mtmt.hu/api/publication/30857506 ID - 30857506 N1 - First Department of Medicine, University of Szeged, Szeged, Hungary Momentum Translational Gastroenterology Research Group, Hungarian Academy of Sciences–University of Szeged, Szeged, Hungary Momentum Epithelial Cell Signalling and Secretion Research Group, Hungarian Academy of Sciences–University of Szeged, Szeged, Hungary Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary Department of Pathophysiology, University of Szeged, Szeged, Hungary Department of Pharmacology and Pharmacotherapy, University of Szeged, Szeged, Hungary Institute for Translational Medicine and First Department of Medicine, University of Pécs, Pécs, Hungary Szentágothai Research Centre, University of Pécs, Pécs, Hungary Cited By :18 Export Date: 26 January 2024 CODEN: JPHYA Correspondence Address: Hegyi, P.; Momentum Translational Gastroenterology Research Group, Hungary; email: hegyi2009@gmail.com AB - •Bile acids, ethanol and fatty acids deteriorate pancreatic ductal fluid and bicarbonate secretion via mitochondrial damage, ATP depletion and calcium overload. •It is known that pancreatitis inducing factors open the membrane transition pore (mPTP) channel via cyclophilin D activation in acinar cells causing calcium overload and cell death and genetic or pharmacological inhibition of mPTP improves the outcome of acute pancreatitis in animal models. •In our study we show that genetic and pharmacological inhibition of mPTP protects mitochondrial homeostasis and cell function evoked by pancreatitis-inducing factors in pancreatic ductal cells. •Our results also reveal that the novel Cyclosporin A derivative NIM811 protects mitochondrial function in acinar and ductal cells, moreover it preserves bicarbonate transport mechanisms in pancreatic ductal cells. •We found that NIM811 is highly effective in different experimental pancreatitis models and that NIM811 has no side-effects. NIM811 is a highly suitable compound to be tested in clinical trials .Background and aims Mitochondrial dysfunction plays a crucial role in the development of acute pancreatitis (AP); however, no compound is currently available with clinically acceptable effectiveness and safety. In this study, we investigated the effects of a novel mitochondrial transition pore inhibitor, N-methyl-4-isoleucine cyclosporin (NIM811), in AP. Methods Pancreatic ductal and acinar cells were isolated by enzymatic digestion from Bl/6 mice. In vitro measurements were performed by confocal microscopy and microfluorometry. Preventive effects of pharmacological (cylosporin A (2 µM), NIM811 (2 µM)) or genetic (Ppif-/- /Cyp D KO) inhibition of the mitochondrial transition pore (mPTP) during the administration of either bile acids (BA) or ethanol + fatty acids (EtOH+FA) were examined. Toxicity of mPTP inhibition was investigated by detecting apoptosis and necrosis. In vivo effects of the most promising compound, NIM811 (5 or 10 mg/kg per os), were checked in three different AP models induced by either caerulein (10 × 50 µg/kg), ethanol+ fatty acid (1.75 g/kg ethanol and 750 mg/kg palmitic acid) or 4% taurocholic acid (2 ml/kg). Results Both genetic and pharmacological inhibition of Cyp D significantly prevented the toxic effects of BA and EtOH+FA by restoring mitochondrial membrane potential (Δψ) and preventing the loss of mitochondrial mass. In vivo experiments revealed that per os administration of NIM811 has a protective effect in AP by reducing oedema, necrosis, leukocyte infiltration and serum amylase level in AP models. Administration of NIM811 had no toxic effects. Conclusion The novel mitochondrial transition pore inhibitor NIM811 seems to be an exceptionally good candidate compound for clinical trials in AP. This article is protected by copyright. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Emese AU - Maléth, József AU - R., Erdos AU - N., Závogyán AU - Tretter, László AU - G., Horvath AU - Z.J., Rakonczay AU - Hegyi, Péter TI - Genetic inhibition of cyclophilin d protects against bile acid or ethanol and fatty acid induced pancreatic ductal epithelial cell damage in mice JF - UNITED EUROPEAN GASTROENTEROLOGY JOURNAL J2 - UEG JOURNAL VL - 6 PY - 2018 IS - 8_suppl SP - A102 SN - 2050-6406 UR - https://m2.mtmt.hu/api/publication/30413397 ID - 30413397 LA - English DB - MTMT ER - TY - JOUR AU - Hujber, Zoltán AU - Horváth, Gergő AU - Petővári, Gábor AU - Krencz, Ildikó AU - Dankó, Titanilla AU - Mészáros, Katalin AU - Rajnai, Hajnalka AU - Szoboszlai, Norbert AU - Leenders, William P J AU - Jeney, András AU - Tretter, László AU - Sebestyén, Anna TI - GABA, glutamine, glutamate oxidation and succinic semialdehyde dehydrogenase expression in human gliomas JF - JOURNAL OF EXPERIMENTAL AND CLINICAL CANCER RESEARCH J2 - J EXP CLIN CANC RES VL - 37 PY - 2018 IS - 1 PG - 12 SN - 0392-9078 DO - 10.1186/s13046-018-0946-5 UR - https://m2.mtmt.hu/api/publication/30318236 ID - 30318236 AB - Bioenergetic characterisation of malignant tissues revealed that different tumour cells can catabolise multiple substrates as salvage pathways, in response to metabolic stress. Altered metabolism in gliomas has received a lot of attention, especially in relation to IDH mutations, and the associated oncometabolite D-2-hydroxyglutarate (2-HG) that impact on metabolism, epigenetics and redox status. Astrocytomas and oligodendrogliomas, collectively called diffuse gliomas, are derived from astrocytes and oligodendrocytes that are in metabolic symbiosis with neurons; astrocytes can catabolise neuron-derived glutamate and gamma-aminobutyric acid (GABA) for supporting and regulating neuronal functions.Metabolic characteristics of human glioma cell models - including mitochondrial function, glycolytic pathway and energy substrate oxidation - in relation to IDH mutation status and after 2-HG incubation were studied to understand the Janus-faced role of IDH1 mutations in the progression of gliomas/astrocytomas. The metabolic and bioenergetic features were identified in glioma cells using wild-type and genetically engineered IDH1-mutant glioblastoma cell lines by metabolic analyses with Seahorse, protein expression studies and liquid chromatography-mass spectrometry.U251 glioma cells were characterised by high levels of glutamine, glutamate and GABA oxidation. Succinic semialdehyde dehydrogenase (SSADH) expression was correlated to GABA oxidation. GABA addition to glioma cells increased proliferation rates. Expression of mutated IDH1 and treatment with 2-HG reduced glutamine and GABA oxidation, diminished the pro-proliferative effect of GABA in SSADH expressing cells. SSADH protein overexpression was found in almost all studied human cases with no significant association between SSADH expression and clinicopathological parameters (e.g. IDH mutation).Our findings demonstrate that SSADH expression may participate in the oxidation and/or consumption of GABA in gliomas, furthermore, GABA oxidation capacity may contribute to proliferation and worse prognosis of gliomas. Moreover, IDH mutation and 2-HG production inhibit GABA oxidation in glioma cells. Based on these data, GABA oxidation and SSADH activity could be additional therapeutic targets in gliomas/glioblastomas. LA - English DB - MTMT ER - TY - JOUR AU - Komlódi, Tímea AU - Geibl, FF AU - Sassani, M AU - Ambrus, Attila AU - Tretter, László TI - Membrane potential and delta pH dependency of reverse electron transport-associated hydrogen peroxide production in brain and heart mitochondria JF - JOURNAL OF BIOENERGETICS AND BIOMEMBRANES J2 - J BIOENERG BIOMEMBR VL - 50 PY - 2018 IS - 5 SP - 355 EP - 365 PG - 11 SN - 0145-479X DO - 10.1007/s10863-018-9766-8 UR - https://m2.mtmt.hu/api/publication/3405043 ID - 3405043 N1 - Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, 37-47 Tűzoltó St, Budapest, 1094, Hungary Department of Neurology, Philipps University Marburg, Marburg, 35043, Germany Department of Neuroscience, Sheffield Institute for Translational Neuroscience (SITraN), University of Sheffield, Sheffield, United Kingdom Cited By :6 Export Date: 14 January 2021 CODEN: JBBID Correspondence Address: Tretter, L.; Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, 37-47 Tűzoltó St, Hungary; email: tretter.laszlo@med.semmelweis-univ.hu Chemicals/CAS: glycerophosphate, 12040-65-2, 1555-56-2, 17603-42-8, 27082-31-1, 39951-36-5, 57-03-4, 89923-83-1, 91846-83-2, 1334-74-3, 55073-41-1; hydrogen peroxide, 7722-84-1; nigericin, 28380-24-7; succinic acid, 110-15-6; valinomycin, 2001-95-8; Hydrogen Peroxide Funding details: Magyar Tudományos Akadémia, MTA, MTA TKI 02001 Funding details: Hungarian Scientific Research Fund, OTKA, K 112230 Funding details: 2017–1.2.1-NKP-2017-00002, KTIA_13_NAP-A-III/6 Funding text 1: Funding This work was supported by the Hungarian Brain Research Program (KTIA_13_NAP-A-III/6 and 2017–1.2.1-NKP-2017-00002), OTKA (K 112230), and the Hungarian Academy of Sciences (MTA TKI 02001), all to Vera Adam-Vizi. AB - Succinate-driven reverse electron transport (RET) is one of the main sources of mitochondrial reactive oxygen species (mtROS) in ischemia-reperfusion injury. RET is dependent on mitochondrial membrane potential (Deltapsim) and transmembrane pH difference (DeltapH), components of the proton motive force (pmf); a decrease in Deltapsim and/or DeltapH inhibits RET. In this study we aimed to determine which component of the pmf displays the more dominant effect on RET-provoked ROS generation in isolated guinea pig brain and heart mitochondria respiring on succinate or alpha-glycerophosphate (alpha-GP). Deltapsim was detected via safranin fluorescence and a TPP(+) electrode, the rate of H2O2 formation was measured by Amplex UltraRed, the intramitochondrial pH (pHin) was assessed via BCECF fluorescence. Ionophores were used to dissect the effects of the two components of pmf. The K(+)/H(+) exchanger, nigericin lowered pHin and DeltapH, followed by a compensatory increase in Deltapsim that led to an augmented H2O2 production. Valinomycin, a K(+) ionophore, at low [K(+)] increased DeltapH and pHin, decreased Deltapsim, which resulted in a decline in H2O2 formation. It was concluded that Deltapsim is dominant over pH in modulating the succinate- and alpha-GP-evoked RET. The elevation of extramitochondrial pH was accompanied by an enhanced H2O2 release and a decreased pH. This phenomenon reveals that from the pH component not pH, but rather absolute value of pH has higher impact on the rate of mtROS formation. Minor decrease of Deltapsim might be applied as a therapeutic strategy to attenuate RET-driven ROS generation in ischemia-reperfusion injury. LA - English DB - MTMT ER - TY - JOUR AU - Mikulás, Krisztina Ágnes AU - Hermann, Péter AU - Gera, István AU - Komlódi, Tímea AU - Horváth, Gergő AU - Ambrus, Attila AU - Tretter, László TI - Triethylene glycol dimethacrylate impairs bioenergetic functions and induces oxidative stress in mitochondria via inhibiting respiratory Complex I JF - DENTAL MATERIALS J2 - DENT MATER VL - 34 PY - 2018 IS - 7 SP - e166 EP - e181 PG - 16 SN - 0109-5641 DO - 10.1016/j.dental.2018.03.012 UR - https://m2.mtmt.hu/api/publication/3362693 ID - 3362693 AB - OBJECTIVES: Earlier studies demonstrated that dental resin monomers lower cellular viability and provoke oxidative stress. Reactive oxygen species (ROS) formation has a key role in triethylene glycol dimethacrylate (TEGDMA) induced adverse reactions. In the present study the effects of TEGDMA on mitochondrial functions were investigated to identify a direct molecular target for cytotoxicity. METHODS: Mitochondria were isolated from guinea pig brain. The most important bioenergetic parameters, oxygen consumption, membrane potential (DeltaPsim), and ATP production were assessed. Mitochondrial H2O2 production and elimination and the NAD(P)H level reported on redox balance. RESULTS: Mitochondria were supported with respiratory substrates to be oxidized by either Complex I (CI) or Complex II (CII). DeltaPsim was depolarized, respiration and ATP production was greatly diminished when applying CI substrates in the presence of TEGDMA. The same parameters remained essentially unaffected when CII substrate plus TEGDMA were applied. H2O2 production by mitochondria was significantly stimulated by TEGDMA in the presence of CI substrates. In the presence of TEGDMA mitochondrial elimination of exogenous H2O2 was impaired. When CII substrate supported the mitochondria in the absence of ADP the H2O2 generation was decreased. NADH autofluorescence results also demonstrated the inhibitory effect of TEGDMA on CI activity. SIGNIFICANCE: TEGDMA inhibits CI in the respiratory chain, which explains effects induced by TEGDMA on redox homeostasis, apoptotic and necrotic cell deaths described in previous studies. Identification of the molecular target of TEGDMA may influence the development of relevant biomaterials and may induce new therapeutic strategies to control the adverse effects of resin monomers. LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Ádám Miklós AU - Fekete, Rebeka AU - Horváth, Gergő AU - Koncsos, Gábor AU - Kriston, Csilla AU - Sebestyén, Anna AU - Giricz, Zoltán AU - Környei, Zsuzsanna AU - Madarász, Emilia AU - Tretter, László TI - Versatility of microglial bioenergetic machinery under starving conditions JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1859 PY - 2018 IS - 3 SP - 201 EP - 214 PG - 14 SN - 0005-2728 DO - 10.1016/j.bbabio.2017.12.002 UR - https://m2.mtmt.hu/api/publication/3308092 ID - 3308092 AB - Microglia are highly dynamic cells in the brain. Their functional diversity and phenotypic versatility brought microglial energy metabolism into the focus of research. Although it is known that microenvironmental cues shape microglial phenotype, their bioenergetic response to local nutrient availability remains unclear. In the present study effects of energy substrates on the oxidative and glycolytic metabolism of primary - and BV-2 microglial cells were investigated. Cellular oxygen consumption, glycolytic activity, the levels of intracellular ATP/ADP, autophagy, mTOR phosphorylation, apoptosis and cell viability were measured in the absence of nutrients or in the presence of physiological energy substrates: glutamine, glucose, lactate, pyruvate or ketone bodies. All of the oxidative energy metabolites increased the rate of basal and maximal respiration. However, the addition of glucose decreased microglial oxidative metabolism and glycolytic activity was enhanced. Increased ATP/ADP ratio and cell viability, activation of the mTOR and reduction of autophagic activity were observed in glutamine-supplemented media. Moreover, moderate and transient oxidation of ketone bodies was highly enhanced by glutamine, suggesting that anaplerosis of the TCA-cycle could stimulate ketone body oxidation. It is concluded that microglia show high metabolic plasticity and utilize a wide range of substrates. Among them glutamine is the most efficient metabolite. To our knowledge these data provide the first account of microglial direct metabolic response to nutrients under short-term starvation and demonstrate that microglia exhibit versatile metabolic machinery. Our finding that microglia have a distinct bioenergetic profile provides a critical foundation for specifying microglial contributions to brain energy metabolism. LA - English DB - MTMT ER - TY - CHAP AU - Sváb, Gergely AU - Szederkényi, Gábor AU - Horváth, G AU - Tretter, László ED - Breitenecke, Felix ED - Kemmetmüller, Wolfgang ED - Körner, Andreas ED - Kugi, Andreas ED - Troch, Inge TI - A Simple Dynamic Model for Mitochondrial Metabolism T2 - MATHMOD 2018 Extended Abstract Volume PB - ARGESIM CY - Bécs SN - 9783901608919 T3 - ARGESIM report ; 55. PY - 2018 SP - 11 EP - 12 PG - 2 UR - https://m2.mtmt.hu/api/publication/3412404 ID - 3412404 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Zimányi, László TI - Bioenergetics: From atomic resolution structures to cancer metabolism JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1859 PY - 2018 IS - 9 SP - 631 EP - 632 PG - 2 SN - 0005-2728 DO - 10.1016/j.bbabio.2018.07.006 UR - https://m2.mtmt.hu/api/publication/3414412 ID - 3414412 LA - English DB - MTMT ER - TY - JOUR AU - Bordt, EA AU - Clerc, P AU - Roelofs, BA AU - Saladino, AJ AU - Tretter, László AU - Ádám, Veronika AU - Cherok, E AU - Khalil, A AU - Yadava, N AU - Ge, SX AU - Francis, TC AU - Kennedy, NW AU - Picton, LK AU - Kumar, T AU - Uppuluri, S AU - Miller, AM AU - Itoh, K AU - Karbowski, M AU - Sesaki, H AU - Hill, RB AU - Polster, BM TI - The Putative Drp1 Inhibitor mdivi-1 Is a Reversible Mitochondrial Complex I Inhibitor that Modulates Reactive Oxygen Species JF - DEVELOPMENTAL CELL J2 - DEV CELL VL - 40 PY - 2017 IS - 6 SP - 583 EP - 594.e6 SN - 1534-5807 DO - 10.1016/j.devcel.2017.02.020 UR - https://m2.mtmt.hu/api/publication/3211755 ID - 3211755 AB - Mitochondrial fission mediated by the GTPase dynamin-related protein 1 (Drp1) is an attractive drug target in numerous maladies that range from heart disease to neurodegenerative disorders. The compound mdivi-1 is widely reported to inhibit Drp1-dependent fission, elongate mitochondria, and mitigate brain injury. Here, we show that mdivi-1 reversibly inhibits mitochondrial complex I-dependent O2 consumption and reverse electron transfer-mediated reactive oxygen species (ROS) production at concentrations (e.g., 50 μM) used to target mitochondrial fission. Respiratory inhibition is rescued by bypassing complex I using yeast NADH dehydrogenase Ndi1. Unexpectedly, respiratory impairment by mdivi-1 occurs without mitochondrial elongation, is not mimicked by Drp1 deletion, and is observed in Drp1-deficient fibroblasts. In addition, mdivi-1 poorly inhibits recombinant Drp1 GTPase activity (Ki > 1.2 mM). Overall, these results suggest that mdivi-1 is not a specific Drp1 inhibitor. The ability of mdivi-1 to reversibly inhibit complex I and modify mitochondrial ROS production may contribute to effects observed in disease models. © 2017 Elsevier Inc. LA - English DB - MTMT ER - TY - JOUR AU - Komlódi, Tímea AU - Tretter, László TI - Methylene blue stimulates substrate-level phosphorylation catalysed by succinyl-CoA ligase in the citric acid cycle JF - NEUROPHARMACOLOGY J2 - NEUROPHARMACOLOGY VL - 123 PY - 2017 SP - 287 EP - 298 PG - 12 SN - 0028-3908 DO - 10.1016/j.neuropharm.2017.05.009 UR - https://m2.mtmt.hu/api/publication/3228818 ID - 3228818 AB - Methylene blue (MB), a potential neuroprotective agent, is efficient in various neurodegenerative disease models. Beneficial effects of MB have been attributed to improvements in mitochondrial functions. Substrate-level phosphorylation (SLP) results in the production of ATP independent from the ATP synthase (ATP-ase). In energetically compromised mitochondria, ATP produced by SLP can prevent the reversal of the adenine nucleotide translocase and thus the hydrolysis of glycolytic ATP. The aim of the present study was to investigate the effect of MB on mitochondrial SLP catalysed by succinyl-CoA ligase. Measurements were carried out on isolated guinea pig cortical mitochondria respiring on α-ketoglutarate, glutamate, malate or succinate. The mitochondrial functions and parameters like ATP synthesis, oxygen consumption, membrane potential, and NAD(P)H level were followed online, in parallel with the redox state of MB. SLP-mediated ATP synthesis was measured in the presence of inhibitors for ATP-ase and adenylate kinase. In the presence of the ATP-ase inhibitor oligomycin MB stimulated respiration with all of the respiratory substrates. However, the rate of ATP synthesis increased only with substrates α-ketoglutarate and glutamate (forming succinyl-CoA). MB efficiently stimulated SLP and restored the membrane potential in mitochondria also with the combined inhibition of Complex I and ATP synthase. ATP formed by SLP alleviated the energetic insufficiency generated by the lack of oxidative phosphorylation. Thus, the MB-mediated stimulation of SLP might be important in maintaining the energetic competence of mitochondria and in preventing the mitochondrial hydrolysis of glycolytic ATP. The mitochondrial effects of MB are explained by the ability to accept electrons from reducing equivalents and transfer them to cytochrome c bypassing the respiratory Complexes I and III. © 2017 Elsevier Ltd. LA - English DB - MTMT ER - TY - JOUR AU - Németh, Beáta AU - Dóczi, Judit AU - Csete, Dániel AU - Kacsó, Gergely AU - Ravasz, Dóra AU - Daniel, Adams AU - Kiss, Gergely AU - Nagy, Ádám Miklós AU - Horváth, Gergő AU - Tretter, László AU - Mócsai, Attila AU - Csépányi-Kömi, Roland AU - Iordanov, Iordan AU - Ádám, Veronika AU - Chinopoulos, Christos TI - Abolition of mitochondrial substrate-level phosphorylation by itaconic acid produced by LPS-induced Irg1 expression in cells of murine macrophage lineage JF - FASEB JOURNAL J2 - FASEB J VL - 30 PY - 2016 IS - 1 SP - 286 EP - 300 PG - 15 SN - 0892-6638 DO - 10.1096/fj.15-279398 UR - https://m2.mtmt.hu/api/publication/2940351 ID - 2940351 LA - English DB - MTMT ER - TY - JOUR AU - Papp, Hajnalka AU - Pongor, Lőrinc AU - Munkácsy, Gyöngyi AU - Horváth, Gergő AU - Nagy, Ádám Miklós AU - Ambrus, Attila AU - Hauser, Péter AU - Szabó, András AU - Tretter, László AU - Győrffy, Balázs TI - TP53 mutation hits energy metabolism and increases glycolysis in breast cancer JF - ONCOTARGET J2 - ONCOTARGET VL - 7 PY - 2016 IS - 41 SP - 67183 EP - 67195 PG - 13 SN - 1949-2553 DO - 10.18632/oncotarget.11594 UR - https://m2.mtmt.hu/api/publication/3111904 ID - 3111904 N1 - Harami-Papp H and Pongor LS have contributed equally to this work. WoS Biosis Citation Index adatbázisban is megtalálható: BCI201700041430 Funding Agency and Grant Number: OTKA Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K108655]; Medinprot program Funding text: The study was supported by the OTKA K108655 grant and the Medinprot program. MTA TTK Lendület Cancer Biomarker Research Group, Magyar tudósok körútja 2., Budapest, H-1117, Hungary Semmelweis University, Department of Medical Biochemistry, Tuzoltó u. 37-47, Budapest, H-1094, Hungary Semmelweis University, 2nd Department of Pediatrics, Tuzoltó u. 7-9., Budapest, H-1094, Hungary MTA TTK Lendület Cancer Biomarker Research Group, Magyar tudósok körútja 2., Budapest, H-1117, Hungary Semmelweis University, Department of Medical Biochemistry, Tuzoltó u. 37-47, Budapest, H-1094, Hungary Semmelweis University, 2nd Department of Pediatrics, Tuzoltó u. 7-9., Budapest, H-1094, Hungary Cited By :23 Export Date: 8 March 2021 Correspondence Address: Gyorffy, B.; MTA TTK Lendület Cancer Biomarker Research Group, Magyar tudósok körútja 2., Hungary; email: gyorffy.balazs@ttk.mta.hu AB - Promising new hallmarks of cancer is alteration of energy metabolism that involves molecular mechanisms shifting cancer cells to aerobe glycolysis. Our goal was to evaluate the correlation between mutation in the commonly mutated tumor suppressor gene TP53 and metabolism. We established a database comprising mutation and RNA-seq expression data of the TCGA repository and performed receiver operating characteristics (ROC) analysis to compare expression of each gene between TP53 mutated and wild type samples. All together 762 breast cancer samples were evaluated of which 215 had TP53 mutation. Top up-regulated metabolic genes include glycolytic enzymes (e.g. HK3, GPI, GAPDH, PGK1, ENO1), glycolysis regulator (PDK1) and pentose phosphate pathway enzymes (PGD, TKT, RPIA). Gluconeogenesis enzymes (G6PC3, FBP1) were down-regulated. Oxygen consumption and extracellular acidification rates were measured in TP53 wild type and mutant breast cell lines with a microfluorimetric analyzer. Applying metabolic inhibitors in the presence and absence of D-glucose and L-glutamine in cell culture experiments resulted in higher glycolytic and mitochondrial activity in TP53 mutant breast cancer cell lines. In summary, TP53 mutation influences energy metabolism at multiple levels. Our results provide evidence for the synergistic activation of multiple hallmarks linking to these the mutation status of a key driver gene. LA - English DB - MTMT ER - TY - JOUR AU - Jády, Attila AU - Nagy, Ádám Miklós AU - Kőhidi, Tímea AU - Ferenczi, Szilamér AU - Tretter, László AU - Madarász, Emilia TI - Differentiation-Dependent Energy Production and Metabolite Utilization: A Comparative Study on Neural Stem Cells, Neurons, and Astrocytes. JF - STEM CELLS AND DEVELOPMENT J2 - STEM CELLS DEV VL - 25 PY - 2016 IS - 13 SP - 995 EP - 1005 PG - 11 SN - 1547-3287 DO - 10.1089/scd.2015.0388 UR - https://m2.mtmt.hu/api/publication/3108583 ID - 3108583 N1 - Összes idézések száma a WoS-ban: 0 AB - While it is evident that the metabolic machinery of stem cells should be fairly different from that of differentiated neurons, the basic energy production pathways in neural stem cells (NSCs) or in neurons are far from clear. Using the model of in vitro neuron production by NE-4C NSCs, this study focused on the metabolic changes taking place during the in vitro neuronal differentiation. O2 consumption, H(+) production, and metabolic responses to single metabolites were measured in cultures of NSCs and in their neuronal derivatives, as well as in primary neuronal and astroglial cultures. In metabolite-free solutions, NSCs consumed little O2 and displayed a higher level of mitochondrial proton leak than neurons. In stem cells, glycolysis was the main source of energy for the survival of a 2.5-h period of metabolite deprivation. In contrast, stem cell-derived or primary neurons sustained a high-level oxidative phosphorylation during metabolite deprivation, indicating the consumption of own cellular material for energy production. The stem cells increased O2 consumption and mitochondrial ATP production in response to single metabolites (with the exception of glucose), showing rapid adaptation of the metabolic machinery to the available resources. In contrast, single metabolites did not increase the O2 consumption of neurons or astrocytes. In "starving" neurons, neither lactate nor pyruvate was utilized for mitochondrial ATP production. Gene expression studies also suggested that aerobic glycolysis and rapid metabolic adaptation characterize the NE-4C NSCs, while autophagy and alternative glucose utilization play important roles in the metabolism of stem cell-derived neurons. LA - English DB - MTMT ER - TY - JOUR AU - Koncsos, Gábor AU - Varga, Zoltán AU - Baranyai, Tamás AU - Boengler, K AU - Rohrbach, S AU - Li, L AU - Schluter, KD AU - Schreckenberg, R AU - Radovits, Tamás AU - Oláh, Attila AU - Mátyás, Csaba AU - Lux, Árpád AU - Al-Khrasani, Mahmoud AU - Komlódi, Tímea AU - Bukosza, Éva Nóra AU - Máthé, Domokos AU - Deres, László AU - Bartekova, M AU - Rajtik, T AU - Adameova, A AU - Szigeti, Krisztián AU - Hamar, Péter AU - Helyes, Zsuzsanna AU - Tretter, László AU - Pacher, Pál AU - Merkely, Béla Péter AU - Giricz, Zoltán AU - Schulz, R AU - Ferdinandy, Péter TI - Diastolic dysfunction in prediabetic male rats: role of mitochondrial oxidative stress JF - AMERICAN JOURNAL OF PHYSIOLOGY: HEART AND CIRCULATORY PHYSIOLOGY J2 - AM J PHYSIOL HEART C VL - 311 PY - 2016 IS - 4 SP - H927 EP - H943 PG - 17 SN - 0363-6135 DO - 10.1152/ajpheart.00049.2016 UR - https://m2.mtmt.hu/api/publication/3101389 ID - 3101389 N1 - Funding Agency and Grant Number: European Foundation for the Study of Diabetes (EFSD) New Horizons Collaborative Research Initiative from the European Association for the Study of Diabetes (EASD); Hungarian Scientific Research Fund [OTKA K 109737, PD100245]; Slovak Scientific Grant Agency [VEGA1/0638/12]; Hungarian Academy of Sciences; Rosztoczy Foundation; European Cooperation in Science and Technology [COST-BM1203-STSM 090515-058721]; German Research Foundation [BO-2955/2-1, SCHU 843/9-1] Funding text: This work was supported by the European Foundation for the Study of Diabetes (EFSD) New Horizons Collaborative Research Initiative from the European Association for the Study of Diabetes (EASD) and Hungarian Scientific Research Fund (OTKA K 109737, PD100245 to T. Radovits) and Slovak Scientific Grant Agency (VEGA1/0638/12). Z. Giricz, T. Radovits, and K. Szigeti hold a "Janos Bolyai Research Scholarship" from the Hungarian Academy of Sciences, and Z. Varga was supported by the Rosztoczy Foundation. P. Ferdinandy is a Szentagothai Fellow of the National Program of Excellence (TAMOP 4.2.4. A/2-11-1-2012-0001). T. Baranyai is supported by the European Cooperation in Science and Technology (COST-BM1203-STSM 090515-058721). K. Boengler and R. Schreckenberg are supported by the German Research Foundation (BO-2955/2-1 and SCHU 843/9-1). AB - Although incidence and prevalence of prediabetes are increasing, little is known on its cardiac effects. Therefore, our aim was to investigate the effect of prediabetes on cardiac function and to characterize parameters and pathways associated with deteriorated cardiac performance. Long-Evans rats were fed with either control or high-fat chow for 21 weeks and treated with a single low dose (20 mg/kg) streptozotocin at week 4. High-fat and streptozotocin treatment induced prediabetes as characterized by slightly elevated fasting blood glucose, impaired glucose- and insulin tolerance, increased visceral adipose tissue and plasma leptin levels, as well as sensory neuropathy. In prediabetic animals a mild diastolic dysfunction was observed, the number of myocardial lipid droplets increased, and left ventricular mass and wall thickness were elevated, however, no molecular sign of fibrosis or cardiac hypertrophy was evidenced. In prediabetes, production of reactive oxygen species was elevated in subsarcolemmal mitochondria. Expression of mitofusin-2 was increased while the phosphorylation of phospholamban and expression of Bcl-2/adenovirus E1B 19 kDa protein-interacting protein 3 (BNIP3, a marker of mitophagy) decreased. However, expression of other markers of cardiac auto- and mitophagy, mitochondrial dynamics, inflammation, heat shock proteins, Ca2+/calmodulin-dependent protein kinase II, mTOR or apoptotic pathways were unchanged in prediabetes. This is the first comprehensive analysis of cardiac effects of prediabetes indicating that mild diastolic dysfunction and cardiac hypertrophy are multifactorial phenomena which is associated with early changes in mitophagy, cardiac lipid accumulation and elevated oxidative stress, and that prediabetes-induced oxidative stress originates from the subsarcolemmal mitochondria. LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Patócs, Attila Balázs AU - Chinopoulos, Christos TI - Succinate, an intermediate in metabolism, signal transduction, ROS, hypoxia, and tumorigenesis. JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1857 PY - 2016 IS - 8 SP - 1086 EP - 1101 PG - 16 SN - 0005-2728 DO - 10.1016/j.bbabio.2016.03.012 UR - https://m2.mtmt.hu/api/publication/3037326 ID - 3037326 N1 - Megjegyzés-26138924 N1 Funding Details: 02001, MTA, Hungarian Academy of Sciences N1 Funding Details: 112230, OTKA, Országos Tudományos Kutatási Alapprogramok Megjegyzés-27663752 N1 Funding details: NNF 78905 N1 Funding details: OTKA, OTKA, Országos Tudományos Kutatási Alapprogramok N1 Funding details: 112230, OTKA, Országos Tudományos Kutatási Alapprogramok N1 Funding details: 95003 N1 Funding details: NNF2 85658 N1 Funding details: K 100918 N1 Funding details: 02001, MTA, Magyar Tudományos Akadémia N1 Funding details: KTIA_13_NAP-A-III/6 N1 Funding text: The work described in the text was supported by the Országos Tudományos Kutatási Alapprogramok (OTKA) grant 112230 , the Hungarian Academy of Sciences grant 02001 , the Hungarian Brain Research Program grant KTIA_13_NAP-A-III/6 to Vera Adam-Vizi, grant of MTA-SE “Hereditary” Endocrine Tumours Research Group to A.P., and MTA-SE Lendület Neurobiochemistry Research Division 95003, OTKA NNF 78905, OTKA NNF2 85658 and OTKA K 100918 to C.C. Cited By :72 Export Date: 22 July 2019 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Cited By :72 Export Date: 29 July 2019 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Cited By :92 Export Date: 10 January 2020 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Cited By :92 Export Date: 13 January 2020 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Cited By :114 Export Date: 24 June 2020 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Cited By :147 Export Date: 14 January 2021 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Semmelweis University, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu Chemicals/CAS: itaconic acid, 97-65-4; succinic acid, 110-15-6; succinate dehydrogenase, 9002-02-2, 9028-10-8; HIF1A protein, human; Hypoxia-Inducible Factor 1, alpha Subunit; Protein Subunits; Reactive Oxygen Species; Receptors, G-Protein-Coupled; Succinate Dehydrogenase; Succinic Acid Funding details: Hungarian Scientific Research Fund, OTKA, 112230 Funding details: K 100918, OTKA NNF2 85658, NNF 78905 Funding details: Magyar Tudományos Akadémia, MTA, 02001 Funding details: KTIA_13_NAP-A-III/6 Funding text 1: The work described in the text was supported by the Országos Tudományos Kutatási Alapprogramok (OTKA) grant 112230 , the Hungarian Academy of Sciences grant 02001 , the Hungarian Brain Research Program grant KTIA_13_NAP-A-III/6 to Vera Adam-Vizi, grant of MTA-SE “Hereditary” Endocrine Tumours Research Group to A.P., and MTA-SE Lendület Neurobiochemistry Research Division 95003, OTKA NNF 78905, OTKA NNF2 85658 and OTKA K 100918 to C.C. Cited By :186 Export Date: 31 July 2021 CODEN: BBBEB Correspondence Address: Tretter, L.; Department of Medical Biochemistry, Tuzolto Street 37-47, Hungary; email: laszlo.tretter@eok.sote.hu AB - Succinate is an important metabolite at the cross-road of several metabolic pathways, also involved in the formation and elimination of reactive oxygen species. However, it is becoming increasingly apparent that its realm extends to epigenetics, tumorigenesis, signal transduction, endo- and paracrine modulation and inflammation. Here we review the pathways encompassing succinate as a metabolite or a signal and how these may interact in normal and pathological conditions.1. LA - English DB - MTMT ER - TY - JOUR AU - Yavari, A AU - Stocker, CJ AU - Ghaffari, S AU - Wargent, ET AU - Steeples, V AU - Czibik, G AU - Pinter, K AU - Bellahcene, M AU - Woods, A AU - Martinez, de Morentin PB AU - Cansell, C AU - Lam, BY AU - Chuster, A AU - Petkevicius, K AU - Nguyen-Tu, MS AU - Martinez-Sanchez, A AU - Pullen, TJ AU - Oliver, PL AU - Stockenhuber, A AU - Nguyen, C AU - Lazdam, M AU - O'Dowd, JF AU - Harikumar, P AU - Tóth, Mónika AU - Beall, C AU - Kyriakou, T AU - Parnis, J AU - Sarma, D AU - Katritsis, G AU - Wortmann, DD AU - Harper, AR AU - Brown, LA AU - Willows, R AU - Gandra, S AU - Poncio, V AU - de Oliveira, Figueiredo MJ AU - Qi, NR AU - Peirson, SN AU - McCrimmon, RJ AU - Gereben, Balázs AU - Tretter, László AU - Fekete, Csaba AU - Redwood, C AU - Yeo, GS AU - Heisler, LK AU - Rutter, GA AU - Smith, MA AU - Withers, DJ AU - Carling, D AU - Sternick, EB AU - Arch, JR AU - Cawthorne, MA AU - Watkins, H AU - Ashrafian, H TI - Chronic Activation of gamma2 AMPK Induces Obesity and Reduces beta Cell Function JF - CELL METABOLISM J2 - CELL METAB VL - 23 PY - 2016 IS - 5 SP - 821 EP - 836 PG - 16 SN - 1550-4131 DO - 10.1016/j.cmet.2016.04.003 UR - https://m2.mtmt.hu/api/publication/3082316 ID - 3082316 N1 - PMC PMC4873618 AB - Despite significant advances in our understanding of the biology determining systemic energy homeostasis, the treatment of obesity remains a medical challenge. Activation of AMP-activated protein kinase (AMPK) has been proposed as an attractive strategy for the treatment of obesity and its complications. AMPK is a conserved, ubiquitously expressed, heterotrimeric serine/threonine kinase whose short-term activation has multiple beneficial metabolic effects. Whether these translate into long-term benefits for obesity and its complications is unknown. Here, we observe that mice with chronic AMPK activation, resulting from mutation of the AMPK gamma2 subunit, exhibit ghrelin signaling-dependent hyperphagia, obesity, and impaired pancreatic islet insulin secretion. Humans bearing the homologous mutation manifest a congruent phenotype. Our studies highlight that long-term AMPK activation throughout all tissues can have adverse metabolic consequences, with implications for pharmacological strategies seeking to chronically activate AMPK systemically to treat metabolic disease. LA - English DB - MTMT ER - TY - JOUR AU - Ambrus, Attila AU - Nemeria, NS AU - Törőcsik, Beáta AU - Tretter, László AU - Nilsson, M AU - Jordan, F AU - Ádám, Veronika TI - Formation of reactive oxygen species by human and bacterial pyruvate and 2- oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 89 PY - 2015 SP - 642 EP - 650 PG - 9 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2015.10.001 UR - https://m2.mtmt.hu/api/publication/2953634 ID - 2953634 N1 - 02001, MTA, Magyar Tudományos Akadémia; 112230, OTKA, Magyar Tudományos Akadémia Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, Budapest, 1094, Hungary Department of Chemistry, Rutgers, State University, Newark, NJ 07102, United States Cited By :25 Export Date: 28 May 2020 CODEN: FRBME Correspondence Address: Adam-Vizi, V.; Department of Chemistry, Rutgers, State UniversityUnited States; email: adam.veronika@med.semmelweis-univ.hu Chemicals/CAS: adenosine diphosphate, 20398-34-9, 58-64-0; calcium ion, 14127-61-8; cytochrome c, 9007-43-6, 9064-84-0; oxoglutarate dehydrogenase, 9031-02-1; pyruvic acid, 127-17-3, 19071-34-2, 57-60-3; reduced nicotinamide adenine dinucleotide, 58-68-4; superoxide, 11062-77-4; Ketoglutarate Dehydrogenase Complex; Multienzyme Complexes; Pyruvic Acid; Reactive Oxygen Species; Recombinant Proteins Funding details: Magyar Tudományos Akadémia, MTA Funding details: Hungarian Scientific Research Fund, OTKA Funding details: Hungarian Scientific Research Fund, OTKA, 112230 Funding details: Magyar Tudományos Akadémia, MTA, 02001 Funding details: KTIA_13_NAP-A-III/6 Funding text 1: We are grateful to Drs. Hetalben Patel, Sowmini Kumaran, Junjie Wang, all from Rutgers, and Da Jeong Shim and Edgardo T. Farinas (New Jersey Institute of Technology) for providing purified proteins to this project, and Mulchand S. Patel and his group for providing cells harboring plasmids of the hPDHc components. Financial support is gratefully acknowledged from the Hungarian Academy of Sciences (MTA grant 02001 to A-V.V.), the Hungarian Scientific Research Fund (OTKA, grant 112230 to A-V. V.), the Hungarian Brain Research Program (grant KTIA_13_NAP-A-III/6. to A-V.V.), the Bolyai and the Fulbright Fellowships (to A.A.), and the NIH (NIH-GM-050380 and NIH-GM-116077 to F.J.). Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, Budapest, 1094, Hungary Department of Chemistry, Rutgers, State University, Newark, NJ 07102, United States Cited By :26 Export Date: 5 January 2021 CODEN: FRBME Correspondence Address: Adam-Vizi, V.; Department of Chemistry, Rutgers, State UniversityUnited States; email: adam.veronika@med.semmelweis-univ.hu Chemicals/CAS: adenosine diphosphate, 20398-34-9, 58-64-0; calcium ion, 14127-61-8; cytochrome c, 9007-43-6, 9064-84-0; oxoglutarate dehydrogenase, 9031-02-1; pyruvic acid, 127-17-3, 19071-34-2, 57-60-3; reduced nicotinamide adenine dinucleotide, 58-68-4; superoxide, 11062-77-4; Ketoglutarate Dehydrogenase Complex; Multienzyme Complexes; Pyruvic Acid; Reactive Oxygen Species; Recombinant Proteins Funding details: Magyar Tudományos Akadémia, MTA Funding details: Hungarian Scientific Research Fund, OTKA Funding details: Hungarian Scientific Research Fund, OTKA, 112230 Funding details: Magyar Tudományos Akadémia, MTA, 02001 Funding details: KTIA_13_NAP-A-III/6 Funding text 1: We are grateful to Drs. Hetalben Patel, Sowmini Kumaran, Junjie Wang, all from Rutgers, and Da Jeong Shim and Edgardo T. Farinas (New Jersey Institute of Technology) for providing purified proteins to this project, and Mulchand S. Patel and his group for providing cells harboring plasmids of the hPDHc components. Financial support is gratefully acknowledged from the Hungarian Academy of Sciences (MTA grant 02001 to A-V.V.), the Hungarian Scientific Research Fund (OTKA, grant 112230 to A-V. V.), the Hungarian Brain Research Program (grant KTIA_13_NAP-A-III/6. to A-V.V.), the Bolyai and the Fulbright Fellowships (to A.A.), and the NIH (NIH-GM-050380 and NIH-GM-116077 to F.J.). LA - English DB - MTMT ER - TY - JOUR AU - Fónai, Fruzsina AU - Pribér, János Krisztián AU - Jakus, Péter AU - Kálmán, Nikoletta AU - Antus, Csenge Petra AU - Pollák, Edit AU - Karsai, G AU - Tretter, László AU - Sümegi, Balázs AU - Veres, Balázs TI - Lack of cyclophilin D protects against the development of acute lung injury in endotoxemia. JF - BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE J2 - BBA-MOL BASIS DIS VL - 1852 PY - 2015 IS - 12 SP - 2563 EP - 2573 PG - 11 SN - 0925-4439 DO - 10.1016/j.bbadis.2015.09.004 UR - https://m2.mtmt.hu/api/publication/2943971 ID - 2943971 AB - Sepsis caused by LPS is characterized by an intense systemic inflammatory response affecting the lungs, causing acute lung injury (ALI). Dysfunction of mitochondria and the role of reactive oxygen (ROS) and nitrogen species produced by mitochondria have already been proposed in the pathogenesis of sepsis; however, the exact molecular mechanism is poorly understood. Oxidative stress induces cyclophilin D (CypD)-dependent mitochondrial permeability transition (mPT), leading to organ failure in sepsis. In previous studies mPT was inhibited by cyclosporine A which, beside CypD, inhibits cyclophilin A, B, C and calcineurin, regulating cell death and inflammatory pathways. The immunomodulatory side effects of cyclosporine A make it unfavorable in inflammatory model systems. To avoid these uncertainties in the molecular mechanism, we studied endotoxemia-induced ALI in CypD-/- mice providing unambiguous data for the pathological role of CypD-dependent mPT in ALI. Our key finding is that the loss of this essential protein improves survival rate and it can intensely ameliorate endotoxin-induced lung injury through attenuated proinflammatory cytokine release, down-regulation of redox sensitive cellular pathways such as MAPKs, Akt, and NF-kappaB and reducing the production of ROS. Functional inhibition of NF-kappaB was confirmed by decreased expression of NF-kappaB-mediated proinflammatory genes. We demonstrated that impaired mPT due to the lack of CypD reduces the severity of endotoxemia-induced lung injury suggesting that CypD specific inhibitors might have a great therapeutic potential in sepsis-induced organ failure. Our data highlight a previously unknown regulatory function of mitochondria during inflammatory response. LA - English DB - MTMT ER - TY - JOUR AU - Pribér, János Krisztián AU - Fónai, Fruzsina AU - Jakus, Péter AU - Rácz, Boglárka AU - Chinopoulos, Christos AU - Tretter, László AU - Gallyas, Ferenc AU - Sümegi, Balázs AU - Veres, Balázs TI - Cyclophilin D disruption attenuates lipopolysaccharide-induced inflammatory response in primary mouse macrophages. JF - BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE J2 - BIOCHEM CELL BIOL VL - 93 PY - 2015 IS - 3 SP - 241 EP - 250 PG - 10 SN - 0829-8211 DO - 10.1139/bcb-2014-0120 UR - https://m2.mtmt.hu/api/publication/2853101 ID - 2853101 N1 - Department of Biochemistry and Medical Chemistry, University of Pecs Medical School, 12 Szigeti St., Pecs, H-7624, Hungary Department of Medical Biochemistry, Semmelweis University, Tuzoltó u. 37-47, Budapest, H-1094, Hungary MTA-PTE Nuclear and Mitochondrial Interactions Research Group, Pecs, Hungary Szentagothai Research Centre, Pecs, Hungary Cited By :7 Export Date: 20 February 2020 CODEN: BCBIE Correspondence Address: Veres, B.; Department of Biochemistry and Medical Chemistry, University of Pecs Medical School, 12 Szigeti St., Hungary Funding Agency and Grant Number: National Excellence Program - Elaborating and operating an inland student and researcher personal support system [TAMOP 4.2.4. A/2-11-1-2012-0001]; European UnionEuropean Union (EU); European Social FundEuropean Social Fund (ESF); Hungarian grants [OTKA NN109841, K104220, PTE AOK-KA-2013/31] Funding text: This research was realized in the frames of TAMOP 4.2.4. A/2-11-1-2012-0001 National Excellence Program - Elaborating and operating an inland student and researcher personal support system. The project was subsidised by the European Union and co-financed by the European Social Fund. This work also was supported by Hungarian grants OTKA NN109841, K104220, and PTE AOK-KA-2013/31. Export Date: 19 December 2020 CODEN: BCBIE AB - According to recent results, various mitochondrial processes can actively regulate the immune response. In the present report, we studied whether mitochondrial permeability transition (mPT) has such a role. To this end, we compared bacterial lipopolysaccharide (LPS)-induced inflammatory response in cyclophilin D (CypD) knock-out and wild-type mouse resident peritoneal macrophages. CypD is a regulator of mPT; therefore, mPT is damaged in CypD-/- cells. We chose this genetic modification-based model because the mPT inhibitor cyclosporine A regulates inflammatory processes by several pathways unrelated to the mitochondria. The LPS increased mitochondrial depolarisation, cellular and mitochondrial reactive oxygen species production, nuclear factor-kappaB activation, and nitrite- and tumour necrosis factor alpha accumulation in wild-type cells, but these changes were diminished or absent in the CypD-deficient macrophages. Additionally, LPS enhanced Akt phosphorylation/activation as well as FOXO1 and FOXO3a phosphorylation/inactivation both in wild-type and CypD-/- cells. However, Akt and FOXO phosphorylation was significantly more pronounced in CypD-deficient compared to wild-type macrophages. These results provide the first pieces of experimental evidence for the functional regulatory role of mPT in the LPS-induced early inflammatory response of macrophages. LA - English DB - MTMT ER - TY - JOUR AU - Kovács, István AU - Horvath, M AU - Kovács, Tünde AU - Somogyi, K AU - Tretter, László AU - Geiszt, Miklós AU - Petheő, Gábor L. TI - Comparison of proton channel, phagocyte oxidase, and respiratory burst levels between human eosinophil and neutrophil granulocytes. JF - FREE RADICAL RESEARCH J2 - FREE RADIC RES VL - 48 PY - 2014 IS - 10 SP - 1190 EP - 1199 PG - 10 SN - 1071-5762 DO - 10.3109/10715762.2014.938234 UR - https://m2.mtmt.hu/api/publication/2713247 ID - 2713247 AB - Robust production of reactive oxygen species (ROS) by phagocyte NADPH oxidase (phox) during the respiratory burst (RB) is a characteristic feature of eosinophil and neutrophil granulocytes. In these cells the voltage-gated proton channel (Hv1) is now considered as an ancillary subunit of the phox needed for intense ROS production. Multiple sources reported that the expression of phox subunits and RB is more intensive in eosinophils than in neutrophils. In most of these studies the eosinophils were not isolated from healthy individuals, and a comparative analysis of Hv1 expression had never been carried out. We performed a systematic comparison of the levels of essential phox subunits, Hv1 expression and ROS producing capacity between eosinophils and neutrophils of healthy individuals. The expression of phox components was similar, whereas the amount of Hv1 was approximately 10-fold greater in eosinophils. Furthermore, Hv1 expression correlated with Nox2 expression only in eosinophils. Additionally, in confocal microscopy experiments co-accumulation of Hv1 and Nox2 at the cell periphery was observed in resting eosinophils but not in neutrophils. While phorbol-12-myristate-13-acetate-induced peak extracellular ROS release was approximately 1.7-fold greater in eosinophils, oxygen consumption studies indicated that the maximal intensity of the RB is only approximately 1.4-fold greater in eosinophils. Our data reinforce that eosinophils, unlike neutrophils, generate ROS predominantly extracellularly. In contrast to previous works we have found that the two granulocyte types display very similar phox subunit expression and RB capacity. The large difference in Hv1 expression suggests that its support to intense ROS production is more important at the cell surface. LA - English DB - MTMT ER - TY - JOUR AU - Nemeria, NS AU - Ambrus, Attila AU - Patel, H AU - Gerfen, G AU - Ádám, Veronika AU - Tretter, László AU - Zhou, J AU - Wang, J AU - Jordan, F TI - Human 2-Oxoglutarate Dehydrogenase Complex E1 Component Forms a Thiamin-derived Radical by Aerobic Oxidation of the Enamine Intermediate. JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 289 PY - 2014 IS - 43 SP - 29859 EP - 29873 PG - 15 SN - 0021-9258 DO - 10.1074/jbc.M114.591073 UR - https://m2.mtmt.hu/api/publication/2769374 ID - 2769374 N1 - Department of Chemistry, Rutgers University, Newark, NJ 07102, United States Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, Budapest, 1094, Hungary Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, United States Cited By :25 Export Date: 28 May 2020 CODEN: JBCHA Correspondence Address: Jordan, F.; Department of Chemistry, Rutgers UniversityUnited States Chemicals/CAS: citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; hydrogen peroxide, 7722-84-1; oxoglutarate dehydrogenase, 9031-02-1; reduced nicotinamide adenine dinucleotide, 58-68-4; superoxide, 11062-77-4; thiamine, 59-43-8, 67-03-8; 2 oxoglutaric acid, 328-50-7; cocarboxylase, 154-87-0; alpha-ketoglutaric acid; Amines; Free Radicals; Ketoglutarate Dehydrogenase Complex; Ketoglutaric Acids; Organophosphonates; Phosphinic Acids; Reactive Oxygen Species; Thiamine; Thiamine Pyrophosphate Funding details: National Science Foundation, NSF, CHE 1213550 Funding details: National Institutes of Health, NIH, GM-050380 Funding details: National Institutes of Health, NIH, GM097499 Department of Chemistry, Rutgers University, Newark, NJ 07102, United States Department of Medical Biochemistry, MTA-SE Laboratory for Neurobiochemistry, Semmelweis University, Budapest, 1094, Hungary Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461, United States Cited By :26 Export Date: 5 January 2021 CODEN: JBCHA Correspondence Address: Jordan, F.; Department of Chemistry, Rutgers UniversityUnited States Chemicals/CAS: citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; hydrogen peroxide, 7722-84-1; oxoglutarate dehydrogenase, 9031-02-1; reduced nicotinamide adenine dinucleotide, 58-68-4; superoxide, 11062-77-4; thiamine, 59-43-8, 67-03-8; 2 oxoglutaric acid, 328-50-7; cocarboxylase, 154-87-0; alpha-ketoglutaric acid; Amines; Free Radicals; Ketoglutarate Dehydrogenase Complex; Ketoglutaric Acids; Organophosphonates; Phosphinic Acids; Reactive Oxygen Species; Thiamine; Thiamine Pyrophosphate Funding details: National Science Foundation, NSF, CHE 1213550 Funding details: National Institutes of Health, NIH, GM-050380 Funding details: National Institutes of Health, NIH, GM097499 AB - Herein are reported unique properties of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc), a rate-limiting enzyme in the Krebs (citric acid) cycle. (a) Functionally competent 2-oxoglutarate dehydrogenase (E1o-h) and dihydrolipoyl succinyltransferase components have been expressed according to kinetic and spectroscopic evidence. (b) A stable free radical, consistent with the C2-(C2alpha-hydroxy)-gamma-carboxypropylidene thiamin diphosphate (ThDP) cation radical was detected by electron spin resonance upon reaction of the E1o-h with 2-oxoglutarate (OG) by itself or when assembled from individual components into OGDHc. (c) An unusual stability of the E1o-h-bound C2-(2alpha-hydroxy)-gamma-carboxypropylidene thiamin diphosphate (the "ThDP-enamine"/C2alpha-carbanion, the first postdecarboxylation intermediate) was observed, probably stabilized by the 5-carboxyl group of OG, not reported before. (d) The reaction of OG with the E1o-h gave rise to superoxide anion and hydrogen peroxide (reactive oxygen species (ROS)). (e) The relatively stable enzyme-bound enamine is the likely substrate for oxidation by O2, leading to the superoxide anion radical (in d) and the radical (in b). (f) The specific activity assessed for ROS formation compared with the NADH (overall complex) activity, as well as the fraction of radical intermediate occupying active centers of E1o-h are consistent with each other and indicate that radical/ROS formation is an "off-pathway" side reaction comprising less than 1% of the "on-pathway" reactivity. However, the nearly ubiquitous presence of OGDHc in human tissues, including the brain, makes these findings of considerable importance in human metabolism and perhaps disease. LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ambrus, Attila TI - Measurement of ROS homeostasis in isolated mitochondria JF - METHODS IN ENZYMOLOGY J2 - METHOD ENZYMOL VL - 547 PY - 2014 SP - 199 EP - 223 PG - 25 SN - 0076-6879 DO - 10.1016/B978-0-12-801415-8.00012-6 UR - https://m2.mtmt.hu/api/publication/2770712 ID - 2770712 N1 - Funding details: Magyar Tudományos Akadémia, MTA, MTA TKI 02001 Funding details: Hungarian Scientific Research Fund, OTKA, NK 81983 Funding details: KTIA_13_NAP-A-III/6 Funding text 1: This work was supported by OTKA (NK 81983), Hungarian Academy of Sciences MTA TKI 02001, and Hungarian Brain Research Program—Grant No. KTIA_13_NAP-A-III/6. AB - In this chapter, we describe the currently most advanced methods applied for the quantitative assessment of ROS homeostasis inside the mitochondrion. These techniques are of particular interest in the field of oxidative stress. After discussing the importance of quantifying mitochondrial ROS homeostasis, three major aspects of this phenomenon and the pertinent methodologies for detection are delineated in detail. First the most important methods, based on fluorimetric or spectrophotometric approaches, for the detection of mitochondrial ROS are described. Elimination of ROS generated inside the mitochondrion is another crucial mechanism that also needs to be quantified accurately to estimate the antioxidant capacity of mitochondria under specific conditions. Since ROS generation and elimination manifest in concert, there needs to exist independent methods for the estimation of the net effect. Such a sensitive biochemical marker in the mitochondrion is aconitase, a citric acid cycle enzyme which is greatly sensitive to ROS. We describe two procedures for the precise determination of aconitase activity. A few auxiliary techniques and good practices having relevance in the successful accomplishment of the more delicate approaches are also mentioned. All other relevant technical considerations including advantages/disadvantages of the various methods and the most common artifacts are also discussed. © 2014 Elsevier Inc. LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Horváth, Gergő AU - Hölgyesi, Áron AU - Essek, F AU - Ádám, Veronika TI - Enhanced hydrogen peroxide generation accompanies the beneficial bioenergetic effects of methylene blue in isolated brain mitochondria JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 77 PY - 2014 SP - 317 EP - 330 PG - 14 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2014.09.024 UR - https://m2.mtmt.hu/api/publication/2749008 ID - 2749008 N1 - Correspondence Address: Adam-Vizi, V.; MTA-SE Laboratory for Neurobiochemistry, Department of Medical Biochemistry, Semmelweis UniversityHungary Chemicals/CAS: adenosine diphosphate, 20398-34-9, 58-64-0; adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; calcium, 7440-70-2, 14092-94-5; cytochrome c, 9007-43-6, 9064-84-0; glycerophosphate, 12040-65-2, 1555-56-2, 17603-42-8, 27082-31-1, 39951-36-5, 57-03-4, 89923-83-1, 91846-83-2, 1334-74-3, 55073-41-1; hydrogen peroxide, 7722-84-1; methylene blue, 61-73-4; oxygen, 7782-44-7; reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone), 9028-04-0; succinic acid, 110-15-6; ubiquinol cytochrome c reductase, 9027-03-6; Adenosine Triphosphate; Calcium; Hydrogen Peroxide; Methylene Blue; Neuroprotective Agents Funding details: Magyar Tudományos Akadémia, MTA, MTA TKI 02001 Funding details: Hungarian Scientific Research Fund, OTKA, NK 81983 Funding details: KTIA_13_NAP-A-III/6 Funding text 1: This work was supported by OTKA ( NK 81983 ), Hungarian Academy of Sciences MTA TKI 02001 , and Hungarian Brain Research Program Grant No. KTIA_13_NAP-A-III/6 . LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Veronika AU - Tretter, László TI - The role of mitochondrial dehydrogenases in the generation of oxidative stress JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 62 PY - 2013 IS - 5 SP - 757 EP - 763 PG - 7 SN - 0197-0186 DO - 10.1016/j.neuint.2013.01.012 UR - https://m2.mtmt.hu/api/publication/2227476 ID - 2227476 AB - In addition to complexes in the respiratory chain, few dehydrogenases playing key roles in the physiological metabolism in neurons, are able to generate reactive oxygen species (ROS) in mitochondria. One of them is the Krebs cycle enzyme, α-ketoglutarate dehydrogenase (α-KGDH), which is capable of producing superoxide and hydrogen peroxide by the E3 subunit of the enzyme regulated by changes in the NADH/NAD+ ratio. Mutations in the E3 subunit known to be related to diseases in humans were shown to have increased ROS-forming ability. α-Glycerophosphate dehydrogenase (α-GPDH) located on the outer surface of the inner membrane can also generate ROS, which is stimulated by Ca2+. ROS production by α-GPDH is unique as it does not require Ca2+ uptake and it is observed in respiring as well as damaged, bioenergetically incompetent mitochondria. The possible role of ROS generation by these dehydrogenases in brain pathology is discussed in this review. © 2013 Elsevier Ltd. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Yu-Fan, Hsieh AU - Guang-Yaw, Liu AU - Yi-Ju, Lee AU - Jiann-Jou, Yang AU - Dánielné Sándor, Katalin AU - Sarang, Zsolt AU - Angela, Bononi AU - Paolo, Pinton AU - Tretter, László AU - Szondy, Zsuzsanna AU - Gregory, J Tsay TI - Transglutaminase 2 Contributes to Apoptosis Induction in Jurkat T Cells by Modulating Ca(2+) Homeostasis via Cross-Linking RAP1GDS1 JF - PLOS ONE J2 - PLOS ONE VL - 8 PY - 2013 IS - 12 PG - 30 SN - 1932-6203 DO - 10.1371/journal.pone.0081516 UR - https://m2.mtmt.hu/api/publication/2505661 ID - 2505661 AB - BACKGROUND: Transglutaminase 2 (TG2) is a protein cross-linking enzyme known to be associated with the in vivo apoptosis program of T cells. However, its role in the T cell apoptosis program was not investigated yet. RESULTS: Here we report that timed overexpression of both the wild type (wt) and the cross-linking mutant of TG2 induced apoptosis in Jurkat T cells, the wt being more effective. Part of TG2 colocalised with mitochondria. WtTG2-induced apoptosis was characterized by enhanced mitochondrial Ca(2+) uptake. Ca(2+)-activated wtTG2 cross-linked RAP1, GTP-GDP dissociation stimulator 1, an unusual guanine exchange factor acting on various small GTPases, to induce a yet uncharacterized signaling pathway that was able to promote the Ca(2+) release from the endoplasmic reticulum via both Ins3P and ryanodine sensitive receptors leading to a consequently enhanced mitochondrial Ca(2+)uptake. CONCLUSIONS: Our data indicate that TG2 might act as a Ca(2+) sensor to amplify endoplasmic reticulum-derived Ca(2+) signals to enhance mitochondria Ca(2+) uptake. Since enhanced mitochondrial Ca(2+) levels were previously shown to sensitize mitochondria for various apoptotic signals, our data demonstrate a novel mechanism through which TG2 can contribute to the induction of apoptosis in certain cell types. Since, as compared to knock out cells, physiological levels of TG2 affected Ca(2+) signals in mouse embryonic fibroblasts similar to Jurkat cells, our data might indicate a more general role of TG2 in the regulation of mitochondrial Ca(2+) homeostasis. LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Horváth, Gergő AU - Ádám, Veronika TI - Mitochondrial effects of a possible neuroprotectant, methylene blue. Studies on isolated brain mitochondria and on BV-2 microglial cell line JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1817 PY - 2012 IS - S SP - S152 EP - S152 SN - 0005-2728 UR - https://m2.mtmt.hu/api/publication/2529233 ID - 2529233 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - High Ca 2+ load promotes Hydrogen peroxide generation via activation of α-glycerophosphate dehydrogenase in brain mitochondria JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 53 PY - 2012 IS - 11 SP - 2119 EP - 2130 PG - 12 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2012.09.029 UR - https://m2.mtmt.hu/api/publication/2124569 ID - 2124569 AB - H 2O 2 generation associated with α-glycerophosphate (α-GP) oxidation was addressed in guinea pig brain mitochondria challenged with high Ca 2+ load (10μM). Exposure to 10μM Ca 2+ induced an abrupt 2.5-fold increase in H 2O 2 release compared to that measured in the presence of a physiological cytosolic Ca 2+ concentration (100nM) from mitochondria respiring on 5mM α-GP in the presence of ADP (2mM). The Ca 2+-induced stimulation of H 2O 2 generation was reversible and unaltered by the uniporter blocker Ru 360, indicating that it did not require Ca 2+ uptake into mitochondria. Enhanced H 2O 2 generation by Ca 2+ was also observed in the absence of ADP when mitochondria exhibited permeability transition pore opening with a decrease in the NAD(P)H level, dissipation of membrane potential, and mitochondrial swelling. Furthermore, mitochondria treated with the pore-forming peptide alamethicin also responded with an elevated H 2O 2 generation to a challenge with 10μM Ca 2+. Ca 2+-induced promotion of H 2O 2 formation was further enhanced by the complex III inhibitor myxothiazol. With 20mM α-GP concentration, stimulation of H 2O 2 formation by Ca 2+ was detected only in the presence, not in the absence, of ADP. It is concluded that α-glycerophosphate dehydrogenase, which is accessible to and could be activated by a rise in the level of cytosolic Ca 2+, makes a major contribution to Ca 2+-stimulated H 2O 2 generation. This work highlights a unique high-Ca 2+-stimulated reactive oxygen species-forming mechanism in association with oxidation of α-GP, which is largely independent of the bioenergetic state and can proceed even in damaged, functionally incompetent mitochondria. © 2012 Elsevier Inc. LA - English DB - MTMT ER - TY - JOUR AU - Ambrus, Attila AU - Törőcsik, Beáta AU - Tretter, László AU - Ozohanics, Olivér AU - Ádám, Veronika TI - Stimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenase JF - HUMAN MOLECULAR GENETICS J2 - HUM MOL GENET VL - 20 PY - 2011 IS - 15 SP - 2984 EP - 2995 PG - 12 SN - 0964-6906 DO - 10.1093/hmg/ddr202 UR - https://m2.mtmt.hu/api/publication/1666747 ID - 1666747 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Angeli, BE AU - Ardestani, MR AU - Goracci, G AU - Ádám, Veronika TI - Reversible inhibition of hydrogen peroxide elimination by calcium in brain mitochondria. JF - JOURNAL OF NEUROSCIENCE RESEARCH J2 - J NEUROSCI RES VL - 89 PY - 2011 IS - 12 SP - 1965 EP - 1972 PG - 8 SN - 0360-4012 DO - 10.1002/jnr.22658 UR - https://m2.mtmt.hu/api/publication/1616633 ID - 1616633 LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Veronika AU - Komáry, Zsófia AU - Tretter, László TI - Substrate-dependence of mitochondrial reactive oxygen species generation JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1797 PY - 2010 IS - Suppl. SP - 55 EP - 55 PG - 1 SN - 0005-2728 DO - 10.1016/j.bbabio.2010.04.179 UR - https://m2.mtmt.hu/api/publication/1430452 ID - 1430452 LA - English DB - MTMT ER - TY - JOUR AU - Ambrus, Attila AU - Tretter, László AU - Ádám, Veronika TI - Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1797 PY - 2010 IS - Suppl. SP - 57 EP - 57 PG - 1 SN - 0005-2728 DO - 10.1016/j.bbabio.2010.04.187 UR - https://m2.mtmt.hu/api/publication/1430453 ID - 1430453 LA - English DB - MTMT ER - TY - JOUR AU - Komáry, Zsófia AU - Tretter, László AU - Ádám, Veronika TI - Membrane potential-related effect of calcium on reactive oxygen species generation in isolated brain mitochondria. JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1797 PY - 2010 IS - 6-7 SP - 922 EP - 928 PG - 7 SN - 0005-2728 DO - 10.1016/j.bbabio.2010.03.010 UR - https://m2.mtmt.hu/api/publication/1327784 ID - 1327784 LA - English DB - MTMT ER - TY - CONF AU - Ádám, Veronika AU - Ambrus, Attila AU - Tretter, László TI - Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid T2 - Frontiers in Systems Neuroscience PY - 2009 SP - online DO - 10.3389/conf.neuro.01.2009.04.136 UR - https://m2.mtmt.hu/api/publication/3037386 ID - 3037386 LA - English DB - MTMT ER - TY - JOUR AU - Ambrus, Attila AU - Tretter, László AU - Ádám, Veronika TI - Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 109 PY - 2009 IS - Suppl. 1 SP - 222 EP - 229 PG - 8 SN - 0022-3042 DO - 10.1111/j.1471-4159.2009.05942.x UR - https://m2.mtmt.hu/api/publication/1234615 ID - 1234615 AB - Dihydrolipoamide dehydrogenase (LADH) is a flavo-enzyme that serves as a subunit of alpha-ketoglutarate dehydrogenase complex (alpha-KGDHC). Reactive oxygen species (ROS) generation by alpha-KGDHC has been assigned to LADH (E3 subunit) and explained by the diaphorase activity of E3. Dysfunctions of alpha-KGDHC and concurrent ROS production have been implicated in neurodegeneration, ischemia-reperfusion, and other pathological conditions. In this work we investigated the in-depth details of ROS generation by isolated LADH and alpha-KGDHC. We found a parallel generation of superoxide and hydrogen peroxide by the E3 subunit of alpha-KGDHC which could be blocked by lipoic acid (LA) acting on a site upstream of the E3 subunit. The pathologically relevant ROS generation (at high NADH/NAD+ ratio and low pH) in the reverse mode of alpha-KGDHC could also be inhibited by LA. Our results contradict the previously proposed mechanism for pH-dependent ROS generation by LADH, showing no disassembling of the E3 functional homodimer at acidic pH using a physiologically relevant method for the examination. It is also suggested that LA could be beneficial in reducing the cell damage related to excessive ROS generation under pathological conditions. LA - English DB - MTMT ER - TY - JOUR AU - Komáry, Zsófia AU - Tretter, László AU - Ádám, Veronika TI - H(2)O(2) generation is decreased by calcium in isolated brain mitochondria. JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS J2 - BBA-BIOENERGETICS VL - 1777 PY - 2008 IS - 7-8 SP - 800 EP - 807 PG - 8 SN - 0005-2728 DO - 10.1016/j.bbabio.2008.05.004 UR - https://m2.mtmt.hu/api/publication/1127363 ID - 1127363 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Uncoupling is without an effect on the production of reactive oxygen species by in situ synaptic mitochondria JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 103 PY - 2007 IS - 5 SP - 1864 EP - 1871 PG - 8 SN - 0022-3042 DO - 10.1111/j.1471-4159.2007.04891.x UR - https://m2.mtmt.hu/api/publication/1127361 ID - 1127361 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Takacs, K AU - Kover, K AU - Ádám, Veronika TI - Stimulation of H(2)O(2) generation by calcium in brain mitochondria respiring on alpha-glycerophosphate. JF - JOURNAL OF NEUROSCIENCE RESEARCH J2 - J NEUROSCI RES VL - 85 PY - 2007 IS - 15 SP - 3471 EP - 3479 PG - 9 SN - 0360-4012 DO - 10.1002/jnr.21405 UR - https://m2.mtmt.hu/api/publication/1127360 ID - 1127360 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Moderate dependence of ROS formation on ΔΨm in isolated brain mitochondria supported by NADH-linked substrates JF - NEUROCHEMICAL RESEARCH J2 - NEUROCHEM RES VL - 32 PY - 2007 IS - 4-5 SP - 569 EP - 575 PG - 7 SN - 0364-3190 DO - 10.1007/s11064-006-9130-y UR - https://m2.mtmt.hu/api/publication/1127359 ID - 1127359 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Takacs, K AU - Hegedűs, V AU - Ádám, Veronika TI - Characteristics of alpha-glycerophosphate evoked H2 O2 generation in brain mitochondria. JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 100 PY - 2007 IS - 3 SP - 650 EP - 663 PG - 14 SN - 0022-3042 DO - 10.1111/j.1471-4159.2006.04223.x UR - https://m2.mtmt.hu/api/publication/1127358 ID - 1127358 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Mayer-Takacs, D AU - Ádám, Veronika TI - The effect of bovine serum albumin on the membrane potential and reactive oxygen species generation in succinate-supported isolated brain mitochondria JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 50 PY - 2007 IS - 1 SP - 139 EP - 147 PG - 9 SN - 0197-0186 DO - 10.1016/j.neuint.2006.07.010 UR - https://m2.mtmt.hu/api/publication/1067039 ID - 1067039 LA - English DB - MTMT ER - TY - CHAP AU - Tretter, László ED - Góth, L TI - Mitochondrial production of reactive oxygen species T2 - Reactive Oxygen Species and Diseases PB - Research Signpost CY - Budapest SN - 8130801817 PY - 2007 SP - 1 EP - 31 PG - 31 UR - https://m2.mtmt.hu/api/publication/2463303 ID - 2463303 LA - English DB - MTMT ER - TY - JOUR AU - Sipos, Ildikó AU - Törőcsik, Beáta AU - Tretter, László AU - Ádám, Veronika TI - Impaired regulation of pH homeostasis by oxidative stress in rat brain capillary endothelial cells JF - CELLULAR AND MOLECULAR NEUROBIOLOGY J2 - CELL MOL NEUROBIOL VL - 25 PY - 2005 IS - 1 SP - 141 EP - 151 PG - 11 SN - 0272-4340 DO - 10.1007/s10571-004-1379-6 UR - https://m2.mtmt.hu/api/publication/1030894 ID - 1030894 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Reactive oxygen species production by complex I in brain mitochondria. The role of reverse electron transport JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 94 PY - 2005 IS - Suppl. 2 SP - 247 EP - 247 PG - 1 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030892 ID - 1030892 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Liktor, Bálint (ifj.) AU - Ádám, Veronika TI - Dual effect of pyruvate in isolated nerve terminals: Generation of reactive oxygen species and protection of aconitase JF - NEUROCHEMICAL RESEARCH J2 - NEUROCHEM RES VL - 30 PY - 2005 IS - 10 SP - 1331 EP - 1338 PG - 8 SN - 0364-3190 DO - 10.1007/s11064-005-8805-0 UR - https://m2.mtmt.hu/api/publication/1030889 ID - 1030889 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress JF - PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B - BIOLOGICAL SCIENCES J2 - PHILOS T ROY SOC B VL - 360 PY - 2005 IS - 1464 SP - 2335 EP - 2345 PG - 11 SN - 0962-8436 DO - 10.1098/rstb.2005.1764 UR - https://m2.mtmt.hu/api/publication/1030888 ID - 1030888 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Sipos, Ildikó AU - Ádám, Veronika TI - Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease JF - NEUROCHEMICAL RESEARCH J2 - NEUROCHEM RES VL - 29 PY - 2004 IS - 3 SP - 569 EP - 577 PG - 9 SN - 0364-3190 DO - 10.1023/B:NERE.0000014827.94562.4b UR - https://m2.mtmt.hu/api/publication/1030899 ID - 1030899 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase JF - JOURNAL OF NEUROSCIENCE J2 - J NEUROSCI VL - 24 PY - 2004 IS - 36 SP - 7771 EP - 7778 PG - 8 SN - 0270-6474 DO - 10.1523/JNEUROSCI.1842-04.2004 UR - https://m2.mtmt.hu/api/publication/1030897 ID - 1030897 LA - English DB - MTMT ER - TY - JOUR AU - Milusheva, Elisaveta AU - Sperlágh, Beáta AU - Shikova, L AU - Baranyi, Mária AU - Tretter, László AU - Ádám, Veronika AU - Vizi, E. Szilveszter TI - Non-synaptic release of H³noradrenaline in response to oxidative stress combined with mitochondrial dysfunction in rat hippocampal slices JF - NEUROSCIENCE J2 - NEUROSCIENCE VL - 120 PY - 2003 SP - 771 EP - 781 PG - 11 SN - 0306-4522 DO - 10.1016/S0306-4522(03)00340-3 UR - https://m2.mtmt.hu/api/publication/109265 ID - 109265 N1 - Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :29 Export Date: 31 July 2019 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: AUTO21 Network of Centres of Excellence Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT27/2000 Funding details: TS040736, T037457, Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 11 August 2019 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: AUTO21 Network of Centres of Excellence Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT27/2000 Funding details: TS040736, T037457, Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 14 August 2019 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: AUTO21 Network of Centres of Excellence Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT27/2000 Funding details: TS040736, T037457, Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 18 April 2020 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Hungarian Scientific Research Fund, OTKA, TS040736, T037457 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 19 April 2020 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Hungarian Scientific Research Fund, OTKA, TS040736, T037457 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 21 April 2020 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Hungarian Scientific Research Fund, OTKA, TS040736, T037457 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 3 August 2020 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: Volkswagen Foundation Funding details: ICA1-CT-2000-70004 Funding details: Hungarian Scientific Research Fund, OTKA, TS040736, T037457 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 26 April 2021 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding details: Volkswagen Foundation Funding details: Hungarian Scientific Research Fund, OTKA, T037457, TS040736 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 7 September 2021 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding details: Volkswagen Foundation Funding details: Hungarian Scientific Research Fund, OTKA, T037457, TS040736 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Institute of Physiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 23, 1113, Sofia, Bulgaria Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :30 Export Date: 8 September 2021 CODEN: NRSCD Correspondence Address: Sperlágh, B.; Department of Pharmacology, P.O. Box 67, H-1450 Budapest, Hungary; email: sperlagh@koki.hu Chemicals/CAS: 2 amino 5 phosphonovaleric acid, 76726-92-6; 6 cyano 7 nitro 2,3 quinoxalinedione, 115066-14-3; 7 nitroindazole, 2942-42-9; hydrogen peroxide, 7722-84-1; oligomycin, 1404-19-9; rotenone, 83-79-4; sodium, 7440-23-5; tetrabenazine, 58-46-8; tritium, 10028-17-8 Funding details: ICA1-CT-2000-70004 Funding details: Egészségügyi Tudományos Tanács, ETT, ETT27/2000 Funding details: Volkswagen Foundation Funding details: Hungarian Scientific Research Fund, OTKA, T037457, TS040736 Funding text 1: This study was supported by the grants of the Hungarian Research Foundation (OTKA T037457, TS040736), the Hungarian Medical Research Council (ETT27/2000), and the Hungarian National Found for Research and Development (NKFP), the Volkswagen Foundation and by the Centre of Excellence grant of EU Framework Program five (ICA1-CT-2000-70004). LA - English DB - MTMT ER - TY - JOUR AU - Sipos, Ildikó AU - Tretter, László AU - Ádám, Veronika TI - Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 84 PY - 2003 IS - 1 SP - 112 EP - 118 PG - 7 SN - 0022-3042 DO - 10.1046/j.1471-4159.2003.01513.x UR - https://m2.mtmt.hu/api/publication/1030907 ID - 1030907 LA - English DB - MTMT ER - TY - JOUR AU - Sipos, Ildikó AU - Tretter, László AU - Ádám, Veronika TI - Reactive oxygen species production in synaptosomes is independent of Delta Psi(m) JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 85 PY - 2003 IS - Suppl. 2 SP - 28 EP - 28 PG - 1 SN - 0022-3042 DO - 10.1046/j.1471-4159.85.s2.19_2.x UR - https://m2.mtmt.hu/api/publication/1030903 ID - 1030903 N1 - Poster session LA - English DB - MTMT ER - TY - JOUR AU - Sipos, Ildikó AU - Tretter, László AU - Ádám, Veronika TI - The production of reactive oxygen species in intact isolated nerve terminals is independent of the mitochondrial membrane potential JF - NEUROCHEMICAL RESEARCH J2 - NEUROCHEM RES VL - 28 PY - 2003 IS - 10 SP - 1575 EP - 1581 PG - 7 SN - 0364-3190 DO - 10.1023/A:1025634728227 UR - https://m2.mtmt.hu/api/publication/1030901 ID - 1030901 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Repassy, R AU - Ádám, Veronika TI - Endogenous glutamate contributes to the maintenance of glutathione level under oxidative stress in isolated nerve terminals JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 42 PY - 2003 IS - 5 SP - 393 EP - 400 PG - 8 SN - 0197-0186 DO - 10.1016/S0197-0186(02)00140-7 UR - https://m2.mtmt.hu/api/publication/1030906 ID - 1030906 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Glutamate release by an Na+ load and oxidative stress in nerve terminals: relevance to ischemia/reperfusion JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 83 PY - 2002 IS - 4 SP - 855 EP - 862 PG - 8 SN - 0022-3042 DO - 10.1046/j.1471-4159.2002.01191.x UR - https://m2.mtmt.hu/api/publication/1030908 ID - 1030908 LA - English DB - MTMT ER - TY - JOUR AU - Gerevich, Zoltán AU - Tretter, László AU - Ádám, Veronika AU - Baranyi, Mária AU - Kiss, János AU - Zelles, Tibor AU - Vizi, E. Szilveszter TI - Analysis of high intracellular [Na⁺]-induced release of ³noradrenaline in rat hippocampal slices JF - NEUROSCIENCE J2 - NEUROSCIENCE VL - 104 PY - 2001 IS - 3 SP - 761 EP - 768 PG - 8 SN - 0306-4522 DO - 10.1016/S0306-4522(01)00102-6 UR - https://m2.mtmt.hu/api/publication/244300 ID - 244300 N1 - Department of Pharmacology, Institute of Experimental Medicine, Hungarian Academy of Sciences, P.O. Box 67, H-1450 Budapest, Hungary Department of Medical Biochemistry, Neurochemical Group, Semmelweis University, P.O. Box 262, H-1444 Budapest, Hungary Cited By :29 Export Date: 22 June 2023 CODEN: NRSCD Correspondence Address: Vizi, E.S.; Department of Pharmacology, P.O. Box 67, H-1450 Budapest, Hungary; email: esvizi@koki.hu Chemicals/CAS: Adrenergic Uptake Inhibitors; Calcium, 7440-70-2; Chelating Agents; Norepinephrine, 51-41-2; Sodium Channels; Sodium, 7440-23-5; Tritium, 10028-17-8; Veratridine, 71-62-5 Funding details: Egészségügyi Tudományos Tanács, ETT, 283/2000, ETT 568/2000 Funding details: Hungarian Scientific Research Fund, OTKA, T-029859, T-032789 Funding text 1: This work was supported by the Hungarian Medical Research Council (ETT 568/2000 and 283/2000) and the Hungarian Research Fund (T-029859 and T-032789). J.P.K. is a János Bólyai Research Fellow. AB - Our aim was to investigate the mechanisms involved in the high intracellular sodium-induced transmitter release in the CNS through the characterisation of the veratridine-evoked (40 μM) noradrenaline release from rat hippocampal slices. The response to veratridine was completely inhibited by tetrodotoxin (1 μM), indicating that the effect is due to the activation of sodium channels. Omission of Ca2+ from the superfusion fluid inhibited the veratridine-evoked release by 72%, showing that the majority of release results from external Ca2+-dependent exocytosis. The residual Ca2+-independent release was not blocked by the intracellular Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N,N-tetraacetic acid acetoxymethyl ester (100 μM) suggesting that intracellular Ca2+ stores are not involved in this component of veratridine effect. The noradrenaline uptake blockers, desipramine (10 μM) and nisoxetine (10 μM), inhibited the external Ca2+-independent release by 50 and 46%, respectively, indicating that the release partly originates from the reversal of transporters (carrier-mediated release). In contrast to uptake blockers, lowering the temperature, another possibility to inhibit transporter function, completely inhibited the effect of veratridine in the absence of Ca2+. Further experiments revealed that low temperature (20 and 12°C) reduces the veratridine-induced increase of intracellular sodium concentration ([Na+]i) in rat cortical synaptosomes (68 and 78% inhibition, respectively). The clinical relevance of our data is that during ischemia a massive release of transmitters occurs mainly due to the elevation of [Na+]i, which contributes to the development of ischemic brain injury. Our results show that low temperature may be a better therapeutic approach to the treatment of ischemia because it has a dual action on this process. Firstly, it inhibits the function of uptake transporters and hence reduces the carrier-mediated outflow of transmitters. Secondly, it inhibits the sodium influx and therefore prevents the unwanted elevation of [Na+]i. Our data also suggest that veratridine stimulation can be a suitable model for ischemic conditions. © 2001 IBRO. LA - English DB - MTMT ER - TY - JOUR AU - Sipos, Ildikó AU - Tretter, László AU - Ádám, Veronika TI - The effects of oxidative stress on calcium and pH homeostasis in rat brain capillary endothelial cells JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 77 PY - 2001 IS - Suppl. 1 SP - 38 EP - 39 PG - 2 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/244296 ID - 244296 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Rozsa, A AU - Ádám, Veronika TI - Oxidative stress and sodium load influence glutamate homeostasis and glutamate release in isolated nerve terminals JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 78 PY - 2001 IS - Suppl. 1 SP - 72 EP - 72 PG - 1 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030912 ID - 1030912 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Repassy, R AU - Ádám, Veronika TI - The role of endogenous glutamate in the maintenance of glutathione-dependent antioxidant capacity of isolated nerve terminals. JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 77 PY - 2001 IS - Suppl. 1 SP - 32 EP - 32 PG - 1 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/244283 ID - 244283 LA - English DB - MTMT ER - TY - JOUR AU - Chinopoulos, Christos AU - Tretter, László AU - Rózsa, Adrienn AU - Ádám, Veronika TI - Exacerbated responses to oxidative stress by an Na+ load in isolated nerve terminals: the role of ATP depletion and rise of [Ca2+](i) JF - JOURNAL OF NEUROSCIENCE J2 - J NEUROSCI VL - 20 PY - 2000 IS - 6 SP - 2094 EP - 2103 PG - 10 SN - 0270-6474 UR - https://m2.mtmt.hu/api/publication/1030923 ID - 1030923 LA - English DB - MTMT ER - TY - JOUR AU - Chinopoulos, Christos AU - Tretter, László AU - Ádám, Veronika TI - Reversible depolarization of in situ mitochondria by oxidative stress parallels a decrease in NAD(P)H level in nerve terminals JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 36 PY - 2000 IS - 6 SP - 483 EP - 488 PG - 6 SN - 0197-0186 DO - 10.1016/S0197-0186(99)00161-8 UR - https://m2.mtmt.hu/api/publication/1030922 ID - 1030922 LA - English DB - MTMT ER - TY - JOUR AU - Perovic, S AU - Tretter, László AU - Brummer, F AU - Wetzler, C Brenner J AU - Donner, G AU - Schroder, HC AU - Muller, WE TI - Dinoflagellates from marine algal blooms produce neurotoxic compounds: effects on free calcium levels in neuronal cells and synaptosomes JF - ENVIRONMENTAL TOXICOLOGY AND PHARMACOLOGY J2 - ENVIRON TOXICOL PHAR VL - 8 PY - 2000 IS - 2 SP - 83 EP - 94 PG - 12 SN - 1382-6689 DO - 10.1016/S1382-6689(99)00035-6 UR - https://m2.mtmt.hu/api/publication/1507629 ID - 1507629 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of alpha-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress JF - JOURNAL OF NEUROSCIENCE J2 - J NEUROSCI VL - 20 PY - 2000 IS - 24 SP - 8972 EP - 8979 PG - 8 SN - 0270-6474 UR - https://m2.mtmt.hu/api/publication/1030917 ID - 1030917 LA - English DB - MTMT ER - TY - JOUR AU - Chinopoulos, Christos AU - Tretter, László AU - Ádám, Veronika TI - Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 73 PY - 1999 IS - 1 SP - 220 EP - 228 PG - 9 SN - 0022-3042 DO - 10.1046/j.1471-4159.1999.0730220.x UR - https://m2.mtmt.hu/api/publication/1030931 ID - 1030931 LA - English DB - MTMT ER - TY - JOUR AU - Perovic, S AU - Wetzler, C AU - Brummer, F AU - Elbrachter, M AU - Tretter, László AU - Wichels, A AU - Muller, WEG AU - Schröder, HC TI - Changes of ICE protease activities caused by toxic supernatants of dinoflagellates (Prorocentrum species) from marine algal blooms JF - EUROPEAN JOURNAL OF PROTISTOLOGY J2 - EUR J PROTISTOL VL - 35 PY - 1999 IS - 3 SP - 267 EP - 274 PG - 8 SN - 0932-4739 UR - https://m2.mtmt.hu/api/publication/1507670 ID - 1507670 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Inhibition of alpha-ketoglutarate dehydrogenase due to H2O2-induced oxidative stress in nerve terminals. Oxidative/Energy Metabolism in Neurodegenerative Disorders TS - Oxidative/Energy Metabolism in Neurodegenerative Disorders JF - ANNALS OF THE NEW YORK ACADEMY OF SCIENCES J2 - ANN NY ACAD SCI VL - 893 PY - 1999 IS - 1 SP - 412 EP - 416 PG - 5 SN - 0077-8923 DO - 10.1111/j.1749-6632.1999.tb07867.x UR - https://m2.mtmt.hu/api/publication/1059589 ID - 1059589 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Rózsa, Adrienn AU - Chinopoulos, Christos AU - Ádám, Veronika TI - Oxidative stress-induced changes in the redox state and citric acid cycle function in isolated nerve endings JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 73 PY - 1999 IS - Suppl SP - S200 EP - S200 PG - 1 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030929 ID - 1030929 LA - English DB - MTMT ER - TY - JOUR AU - Chinopoulos, Christos AU - Tretter, László AU - Ádám, Veronika TI - Mitochondrial membrane potential in isolated nerve terminals under peroxidative stress. JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 71 PY - 1998 IS - Suppl. 1. SP - S16 EP - S16 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030933 ID - 1030933 LA - English DB - MTMT ER - TY - JOUR AU - Környei, Zsuzsanna AU - Tóth, B AU - Tretter, László AU - Madarász, Emilia TI - Effects of retinoic acid on rat forebrain cells derived from embryonic and perinatal rats JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 33 PY - 1998 IS - 6 SP - 541 EP - 549 PG - 9 SN - 0197-0186 DO - 10.1016/S0197-0186(98)00063-1 UR - https://m2.mtmt.hu/api/publication/108534 ID - 108534 N1 - Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Biochemistry II, Semmelweis Medical School, Budapest, Hungary Cited By :12 Export Date: 24 July 2019 CODEN: NEUID Correspondence Address: Madarasz, E.; Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary; email: madarasz@koki.hu Chemicals/CAS: Glutamic Acid, 56-86-0; N-Methylaspartate, 6384-92-5; Receptors, N-Methyl-D-Aspartate; Tretinoin, 302-79-4 Funding details: Hungarian Scientific Research Fund, T020344, T000623 Funding text 1: This work was supported by OTKA (T000623 and T020344) to E. Madarász and by PhD training programs Behavioural Neurobiology (Eötvös Loránd University, Budapest) to Zs. Környei and Neurosciences (Semmelweis Medical School, Budapest, Eötvös Loránd University and Institute of Experimental Medicine of Hungarian Academy of Sciences) to B. Tóth. The authors thank Prof. Robert Balázs for critical reading of the manuscript. The assistence of Ildikó Józsa, Gabriella Szôke and Katalin Takács is gratefully acknowledged. Authors also thank Dr Géza Szabó (EGIS Pharmaceuticals) for his contribution to the assays on TCP-binding by washed membrane preparations. Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary Department of Biochemistry II, Semmelweis Medical School, Budapest, Hungary Cited By :12 Export Date: 11 August 2019 CODEN: NEUID Correspondence Address: Madarasz, E.; Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary; email: madarasz@koki.hu Chemicals/CAS: Glutamic Acid, 56-86-0; N-Methylaspartate, 6384-92-5; Receptors, N-Methyl-D-Aspartate; Tretinoin, 302-79-4 Funding details: Hungarian Scientific Research Fund, T020344, T000623 Funding text 1: This work was supported by OTKA (T000623 and T020344) to E. Madarász and by PhD training programs Behavioural Neurobiology (Eötvös Loránd University, Budapest) to Zs. Környei and Neurosciences (Semmelweis Medical School, Budapest, Eötvös Loránd University and Institute of Experimental Medicine of Hungarian Academy of Sciences) to B. Tóth. The authors thank Prof. Robert Balázs for critical reading of the manuscript. The assistence of Ildikó Józsa, Gabriella Szôke and Katalin Takács is gratefully acknowledged. Authors also thank Dr Géza Szabó (EGIS Pharmaceuticals) for his contribution to the assays on TCP-binding by washed membrane preparations. LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Chinopoulos, Christos AU - Ádám, Veronika TI - Plasma membrane depolarization and disturbed Na+ homeostasis induced by the protonophore carbonyl cyanide-p-trifluoromethoxyphenyl-hydrazon in isolated nerve terminals JF - MOLECULAR PHARMACOLOGY J2 - MOL PHARMACOL VL - 53 PY - 1998 IS - 4 SP - 734 EP - 741 PG - 8 SN - 0026-895X DO - 10.1124/mol.53.4.734 UR - https://m2.mtmt.hu/api/publication/1030935 ID - 1030935 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - The neuroprotective drug vinpocetine prevents veratridine-induced [Na+](i) and [Ca2(+)](i) rise in synaptosomes JF - NEUROREPORT J2 - NEUROREPORT VL - 9 PY - 1998 IS - 8 SP - 1849 EP - 1853 PG - 5 SN - 0959-4965 DO - 10.1097/00001756-199806010-00034 UR - https://m2.mtmt.hu/api/publication/1030934 ID - 1030934 LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Veronika AU - Tretter, László AU - Chinopoulos, Christos TI - Enhanced stimulation-evoked Ca2+-signal and impaired ATP production by hydrogen peroxide in synaptosomes. Comparison with the effect of protonophores JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 69 PY - 1997 IS - Suppl. SP - S214 EP - S214 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030859 ID - 1030859 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Chinopoulos, Christos AU - Ádám, Veronika TI - Enhanced depolarization-evoked calcium signal and reduced [ATP]/[ADP] ratio are unrelated events induced by oxidative stress in synaptosomes JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 69 PY - 1997 IS - 6 SP - 2529 EP - 2537 PG - 9 SN - 0022-3042 DO - 10.1046/j.1471-4159.1997.69062529.x UR - https://m2.mtmt.hu/api/publication/1030858 ID - 1030858 LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Veronika AU - Tretter, László TI - Early events in isolated nerve terminals due to free radicals JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 66 PY - 1996 IS - Suppl. 2. SP - S31 EP - S31 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030860 ID - 1030860 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Early events in free radical-mediated damage of isolated nerve terminals: Effects of peroxides on membrane potential and intracellular Na+ and Ca+ concentrations JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 66 PY - 1996 IS - 5 SP - 2057 EP - 2066 PG - 10 SN - 0022-3042 DO - 10.1046/j.1471-4159.1996.66052057.x UR - https://m2.mtmt.hu/api/publication/1030862 ID - 1030862 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Ádám, Veronika TI - Free radicals enhance Ca2+-signal and inhibit glutamate release in response to K+-depolarization in synaptosomes JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 66 PY - 1996 IS - Suppl. 2. SP - S59 EP - S59 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030861 ID - 1030861 LA - English DB - MTMT ER - TY - JOUR AU - Carvalho, C M AU - Ferreira, I L AU - Duarte, C B AU - Malva, J O AU - Tretter, László AU - Ádám, Veronika AU - Carvalho, A P TI - RELATION OF [CA2+](I) TO DOPAMINE RELEASE IN STRIATAL SYNAPTOSOMES - ROLE OF CA2+ CHANNELS JF - BRAIN RESEARCH J2 - BRAIN RES VL - 669 PY - 1995 IS - 2 SP - 234 EP - 244 PG - 11 SN - 0006-8993 DO - 10.1016/0006-8993(94)01252-D UR - https://m2.mtmt.hu/api/publication/1030864 ID - 1030864 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Bors, P AU - Ádám, Veronika TI - THE EFFECT OF FREE-RADICALS ON SYNAPTOSOMAL IONIC HOMEOSTASIS JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 63 PY - 1994 IS - Suppl. 1 SP - S92 EP - S92 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030866 ID - 1030866 LA - English DB - MTMT ER - TY - JOUR AU - Ádám, Veronika AU - Deri, Z AU - Bors, P AU - Tretter, László TI - LACK OF INVOLVEMENT OF [CA2+]I IN THE EXTERNAL CA2+-INDEPENDENT RELEASE OF ACETYLCHOLINE EVOKED BY VERATRIDINE, OUABAIN AND ALPHA-LATROTOXIN - POSSIBLE ROLE OF [NA+]I JF - JOURNAL OF PHYSIOLOGY (PARIS 1992-) J2 - J PHYSIOL (PARIS 1992-) VL - 87 PY - 1993 IS - 1 SP - 43 EP - 50 PG - 8 SN - 0928-4257 DO - 10.1016/0928-4257(93)90023-M UR - https://m2.mtmt.hu/api/publication/1030871 ID - 1030871 LA - English DB - MTMT ER - TY - JOUR AU - Bors, P AU - Tretter, László AU - Ádám, Veronika TI - RELATIONSHIP BETWEEN SYNAPTOSOMAL ION DISTRIBUTION AND NEUROTRANSMITTER RELEASE - EFFECT OF HYDROPEROXIDES JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 61 PY - 1993 IS - Suppl. SP - S144 EP - S144 SN - 0022-3042 UR - https://m2.mtmt.hu/api/publication/1030868 ID - 1030868 LA - English DB - MTMT ER - TY - JOUR AU - INSTITORIS, E AU - Tretter, László AU - GAAL, D TI - SEVERE DEPLETION OF CELLULAR THIOLS AND GLUTATHIONE-RELATED ENZYMES OF A CARMUSTINE-RESISTANT L1210 STRAIN ASSOCIATES WITH COLLATERAL SENSITIVITY TO CYCLOPHOSPHAMIDE JF - CANCER CHEMOTHERAPY AND PHARMACOLOGY J2 - CANCER CHEMOTH PHARM VL - 33 PY - 1993 IS - 1 SP - 85 EP - 88 PG - 4 SN - 0344-5704 DO - 10.1007/BF00686029 UR - https://m2.mtmt.hu/api/publication/1507442 ID - 1507442 LA - English DB - MTMT ER - TY - JOUR AU - Tretter, László AU - Bors, P AU - Ádám, Veronika TI - EFFECT OF HYDROPEROXIDES ON THE INTRACELLULAR [CA2+] AND MEMBRANE-POTENTIAL OF SYNAPTOSOMES JF - JOURNAL OF NEUROCHEMISTRY J2 - J NEUROCHEM VL - 61 PY - 1993 IS - Suppl. 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COMPARATIVE-STUDIES ON FERROUS ION AND ADP.FE/NADPH-INDUCED PEROXIDATION JF - JOURNAL OF BIOENERGETICS AND BIOMEMBRANES J2 - J BIOENERG BIOMEMBR VL - 19 PY - 1987 IS - 1 SP - 21 EP - 30 PG - 10 SN - 0145-479X UR - https://m2.mtmt.hu/api/publication/1506662 ID - 1506662 LA - English DB - MTMT ER -