TY - JOUR AU - Venditti, P AU - Zhang, Y AU - Radák, Zsolt AU - Magalhaes, J TI - Exercise in the Prevention and Management of Oxidative Stress-Linked Diseases JF - OXIDATIVE MEDICINE AND CELLULAR LONGEVITY J2 - OXID MED CELL LONGEV PY - 2018 PG - 2 SN - 1942-0900 DO - 10.1155/2018/7643721 UR - https://m2.mtmt.hu/api/publication/3380328 ID - 3380328 LA - English DB - MTMT ER - TY - JOUR AU - Suwa, M AU - Nakano, H AU - Radák, Zsolt AU - Kumagai, S TI - Effects of nitric oxide synthase inhibition on fiber-type composition, mitochondrial biogenesis, and SIRT1 expression in rat skeletal muscle JF - JOURNAL OF SPORTS SCIENCE AND MEDICINE J2 - J SPORT SCI MED VL - 14 PY - 2015 IS - 3 SP - 548 EP - 555 PG - 8 SN - 1303-2968 UR - https://m2.mtmt.hu/api/publication/2990840 ID - 2990840 AB - It was hypothesized that nitric oxide synthases (NOS) regulated SIRT1 expression and lead to a corresponding changes of contractile and metabolic properties in skeletal muscle. The purpose of the present study was to investigate the influence of long-term inhibition of nitric oxide synthases (NOS) on the fiber-type composition, metabolic regulators such as and silent information regulator of transcription 1 (SIRT1) and peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC-1alpha), and components of mitochondrial biogenesis in the soleus and plantaris muscles of rats. Rats were assigned to two groups: control and NOS inhibitor (N (omega)-nitro-L-arginine methyl ester hydrochloride (L-NAME), ingested for 8 weeks in drinking water)-treated groups. The percentage of Type I fibers in the L-NAME group was significantly lower than that in the control group, and the percentage of Type IIA fibers was concomitantly higher in soleus muscle. In plantaris muscle, muscle fiber composition was not altered by L-NAME treatment. L-NAME treatment decreased the cytochrome C protein expression and activity of mitochondrial oxidative enzymes in the plantaris muscle but not in soleus muscle. NOS inhibition reduced the SIRT1 protein expression level in both the soleus and plantaris muscles, whereas it did not affect the PGC-1alpha protein expression. L-NAME treatment also reduced the glucose transporter 4 protein expression in both muscles. These results suggest that NOS plays a role in maintaining SIRT1 protein expression, muscle fiber composition and components of mitochondrial biogenesis in skeletal muscle. Key pointsNOS inhibition by L-NAME treatment decreased the SIRT1 protein expression in skeletal muscle.NOS inhibition induced the Type I to Type IIA fiber type transformation in soleus muscle.NOS inhibition reduced the components of mitochondrial biogenesis and glucose metabolism in skeletal muscle. LA - English DB - MTMT ER - TY - JOUR AU - Suwa, M AU - Nakano, H AU - Radák, Zsolt AU - Kumagai, S TI - A comparison of chronic AICAR treatment-induced metabolic adaptations in red and white muscles of rats JF - JOURNAL OF PHYSIOLOGICAL SCIENCES J2 - J PHYSIOL SCI VL - 65 PY - 2015 IS - 1 SP - 121 EP - 130 PG - 10 SN - 1880-6546 DO - 10.1007/s12576-014-0349-0 UR - https://m2.mtmt.hu/api/publication/2899023 ID - 2899023 AB - The signaling molecule 5'-AMP-activated protein kinase plays a pivotal role in metabolic adaptations. Treatment with 5-aminoimidazole-4-carboxamide-1-beta-D-ribofranoside (AICAR) promotes the expression of metabolic regulators and components involved in glucose uptake, mitochondrial biogenesis, and fatty acid oxidation in skeletal muscle cells. Our aim was to determine whether AICAR-induced changes in metabolic regulators and components were more prominent in white or red muscle. Rats were treated with AICAR (1 mg/g body weight/day) for 14 days, resulting in increased expression levels of nicotinamide phosphoribosyltransferase (NAMPT), peroxisome proliferator-activated receptor-gamma coactivator-1alpha (PGC-1alpha), glucose transporter 4 proteins, and enhanced mitochondrial biogenesis. These changes were more prominent in white rather than red gastrocnemius muscle or were only observed in the white gastrocnemius. Our results suggest that AICAR induces the expression of metabolic regulators and components, especially in type II (B) fibers. LA - English DB - MTMT ER - TY - JOUR AU - Mosaferi Ziaaldini, Mohammad AU - Koltai, Erika AU - Csende, Zsolt AU - Goto, Sataro AU - Boldogh, Istvan AU - Taylor, Albert W AU - Radák, Zsolt TI - Exercise training increases anabolic and attenuates catabolic and apoptotic processes in aged skeletal muscle of male rats JF - EXPERIMENTAL GERONTOLOGY J2 - EXP GERONTOL VL - 67 PY - 2015 SP - 9 EP - 14 PG - 6 SN - 0531-5565 DO - 10.1016/j.exger.2015.04.008 UR - https://m2.mtmt.hu/api/publication/2883904 ID - 2883904 AB - Abstract Aging results in significant loss of mass and function of the skeletal muscle, which negatively impacts the quality of life. In this study we investigated whether aerobic exercise training has the potential to alter anabolic and catabolic pathways in the skeletal muscle. Five and twenty eight month old rats were used in the study. Aging resulted in decreased levels of follistatin/mTOR/Akt/Erk activation and increased myostatin/Murf1/2, proteasome subunits, and protein ubiquitination levels. In addition, TNF-α, reactive oxygen species (ROS), p53, and Bax levels were increased while Bcl-2 levels were decreased in the skeletal muscle of aged rats. Six weeks of exercise training at 60% of VO2max reversed the age-associated activation of catabolic and apoptotic pathways and increased anabolic signaling. The results suggest that the age-associated loss of muscle mass and cachexia could be due to the orchestrated down-regulation of anabolic and up-regulation of catabolic and pro-apoptotic processes. These metabolic changes can be attenuated by exercise training. LA - English DB - MTMT ER - TY - JOUR AU - Pósa, Anikó AU - Szabó, Renáta AU - Kupai, Krisztina AU - Baráth, Zoltán Lajos AU - Szalai, Zita AU - Csonka, Anett AU - Veszelka, Médea AU - Gyöngyösi, Mariann AU - Radák, Zsolt AU - Ménesi, Rudolf AU - Pávó, Imre AU - Magyariné, Berkó Anikó AU - Varga, Csaba TI - Cardioprotective effects of voluntary exercise in a rat model: role of matrix metalloproteinase-2 JF - OXIDATIVE MEDICINE AND CELLULAR LONGEVITY J2 - OXID MED CELL LONGEV VL - 2015 PY - 2015 IS - Special Issue PG - 9 SN - 1942-0900 DO - 10.1155/2015/876805 UR - https://m2.mtmt.hu/api/publication/2788926 ID - 2788926 N1 - Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Szeged, 6726, Hungary Faculty of Dentistry and Department of Orthodontics and Pediatric Dentistry, University of Szeged, Szeged, 6720, Hungary Department of Cardiology, Medical University of Vienna, Waehringer Guertel 18-20, Vienna, 1090, Austria Institute of Sport Science, Faculty of Physical Education and Sport Science, Semmelweis University, Alkotas Ucta 44, Budapest, 1123, Hungary Cited By :9 Export Date: 28 August 2019 Correspondence Address: Pósa, A.; Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: gelatinase A, 146480-35-5; phentolamine, 50-60-2, 73-05-2; argipressin, 113-79-1; epinephrine, 51-43-4, 55-31-2, 6912-68-1; Arginine Vasopressin; Epinephrine; Matrix Metalloproteinase 2; Phentolamine Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Szeged, 6726, Hungary Faculty of Dentistry and Department of Orthodontics and Pediatric Dentistry, University of Szeged, Szeged, 6720, Hungary Department of Cardiology, Medical University of Vienna, Waehringer Guertel 18-20, Vienna, 1090, Austria Institute of Sport Science, Faculty of Physical Education and Sport Science, Semmelweis University, Alkotas Ucta 44, Budapest, 1123, Hungary Cited By :12 Export Date: 22 November 2020 Correspondence Address: Pósa, A.; Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: gelatinase A, 146480-35-5; phentolamine, 50-60-2, 73-05-2; argipressin, 113-79-1; epinephrine, 51-43-4, 55-31-2, 6912-68-1; Arginine Vasopressin; Epinephrine; Matrix Metalloproteinase 2; Phentolamine Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Szeged, 6726, Hungary Faculty of Dentistry and Department of Orthodontics and Pediatric Dentistry, University of Szeged, Szeged, 6720, Hungary Department of Cardiology, Medical University of Vienna, Waehringer Guertel 18-20, Vienna, 1090, Austria Institute of Sport Science, Faculty of Physical Education and Sport Science, Semmelweis University, Alkotas Ucta 44, Budapest, 1123, Hungary Cited By :12 Export Date: 10 January 2021 Correspondence Address: Pósa, A.; Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: gelatinase A, 146480-35-5; phentolamine, 50-60-2, 73-05-2; argipressin, 113-79-1; epinephrine, 51-43-4, 55-31-2, 6912-68-1; Arginine Vasopressin; Epinephrine; Matrix Metalloproteinase 2; Phentolamine Department of Physiology, Anatomy and Neuroscience, University of Szeged, Kozep Fasor 52, Szeged, 6726, Hungary Faculty of Dentistry and Department of Orthodontics and Pediatric Dentistry, University of Szeged, Szeged, 6720, Hungary Department of Cardiology, Medical University of Vienna, Waehringer Guertel 18-20, Vienna, 1090, Austria Institute of Sport Science, Faculty of Physical Education and Sport Science, Semmelweis University, Alkotas Ucta 44, Budapest, 1123, Hungary Cited By :12 Export Date: 12 March 2021 Correspondence Address: Pósa, A.; Department of Physiology, Kozep Fasor 52, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: gelatinase A, 146480-35-5; phentolamine, 50-60-2, 73-05-2; argipressin, 113-79-1; epinephrine, 51-43-4, 55-31-2, 6912-68-1; Arginine Vasopressin; Epinephrine; Matrix Metalloproteinase 2; Phentolamine LA - English DB - MTMT ER - TY - JOUR AU - Marton, Orsolya AU - Koltai, Erika AU - Takeda, M AU - Koch, LG AU - Britton, SL AU - Davies, KJA AU - Boldogh, I AU - Radák, Zsolt TI - Mitochondrial biogenesis-associated factors underlie the magnitude of response to aerobic endurance training in rats JF - PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY J2 - PFLUG ARCH EUR J PHY VL - 467 PY - 2015 IS - 4 SP - 779 EP - 788 PG - 10 SN - 0031-6768 DO - 10.1007/s00424-014-1554-7 UR - https://m2.mtmt.hu/api/publication/2736495 ID - 2736495 N1 - Megjegyzés-24770303 Admin megjegyzés-24765191 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# Admin megjegyzés-24765566 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# Admin megjegyzés-24765620 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# Admin megjegyzés-24768131 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# Admin megjegyzés-24770066 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# Admin megjegyzés-24755875 #JournalID1# Name: PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY ISSN: 0031-6768 #JournalID2# AB - Trainability is important in elite sport and in recreational physical activity, and the wide range for response to training is largely dependent on genotype. In this study, we compare a newly developed rat model system selectively bred for low and high gain in running distance from aerobic training to test whether genetic segregation for trainability associates with differences in factors associated with mitochondrial biogenesis. Low response trainer (LRT) and high response trainer (HRT) rats from generation 11 of artificial selection were trained five times a week, 30 min per day for 3 months at 70 % VO2max to study the mitochondrial molecular background of trainability. As expected, we found significant differential for the gain in running distance between LRT and HRT groups as a result of training. However, the changes in VO2max, COX-4, redox homeostasis associated markers (reactive oxygen species (ROS)), silent mating-type information regulation 2 homolog (SIRT1), NAD+/NADH ratio, proteasome (R2 subunit), and mitochondrial network related proteins such as mitochondrial fission protein 1 (Fis1) and mitochondrial fusion protein (Mfn1) suggest that these markers are not strongly involved in the differences in trainability between LRT and HRT. On the other hand, according to our results, we discovered that differences in basal activity of AMP-activated protein kinase alpha (AMPKalpha) and differential changes in aerobic exercise-induced responses of citrate synthase, carbonylated protein, peroxisome proliferator-activated receptor gamma coactivator-1alpha (PGC1-alpha), nuclear respiratory factor 1 (NRF1), mitochondrial transcription factor A (TFAM), and Lon protease limit trainability between these selected lines. From this, we conclude that mitochondrial biogenesis-associated factors adapt differently to aerobic exercise training in training sensitive and training resistant rats. LA - English DB - MTMT ER - TY - CHAP AU - Radák, Zsolt AU - Acs, Zoltan AU - Bori, Zoltán AU - Taylor, Albert W. AU - Yang, Hu ED - Laher, I TI - The Effects of High-Altitude Exposure on Reactive Oxygen and Nitrogen Species T2 - Systems Biology of Free Radicals and Antioxidants PB - Springer Netherlands CY - Berlin CY - Heidelberg SN - 9783642300172 PY - 2014 SP - 407 EP - 416 PG - 10 DO - 10.1007/978-3-642-30018-9_28 UR - https://m2.mtmt.hu/api/publication/31281655 ID - 31281655 LA - English DB - MTMT ER - TY - CHAP AU - Radák, Zsolt ED - LeBourg, E ED - Rattan, SIS TI - Exercise and Hormesis Shaping the Dose-Response Curve T2 - HORMESIS IN HEALTH AND DISEASE SN - 9781482205466 ; 9781482205459 PY - 2014 SP - 37 EP - 44 PG - 8 UR - https://m2.mtmt.hu/api/publication/30784714 ID - 30784714 LA - English DB - MTMT ER - TY - CHAP AU - Radák, Zsolt AU - Hart, N AU - Marton, O AU - Koltai, Erika ED - Laher, I TI - Regular exercise results in systemic adaptation against oxidative stress T2 - Systems Biology of Free Radicals and Antioxidants PB - Springer Netherlands CY - Berlin CY - Heidelberg SN - 9783642300172 PY - 2014 SP - 3855 EP - 3869 PG - 15 DO - 10.1007/978-3-642-30018-9_166 UR - https://m2.mtmt.hu/api/publication/25078167 ID - 25078167 LA - English DB - MTMT ER - TY - JOUR AU - Fehér, J AU - Kovács, Illés AU - Pacella, E AU - Radák, Zsolt TI - A mikroflóra és a bélnyálkahártya kölcsönhatása az irritábilis bél, irritábilis szem és irritábilis elme szindróma kórtanában és kezelésében JF - ORVOSI HETILAP J2 - ORV HETIL VL - 155 PY - 2014 IS - 37 SP - 1454 EP - 1460 PG - 7 SN - 0030-6002 DO - 10.1556/OH.2014.29987 UR - https://m2.mtmt.hu/api/publication/24285489 ID - 24285489 N1 - Cited By :8 Export Date: 8 September 2023 CODEN: ORHEA Chemicals/CAS: retinol, 68-26-8, 82445-97-4; vitamin B group, 12001-76-2; Prebiotics AB - Accumulating clinical evidence supports co-morbidity of irritable bowel, irritable eye and irritable mind symptoms. Furthermore, perturbation of the microbiota-host symbiosis (dysbiosis) is considered a common pathogenic mechanism connecting gastrointestinal, ocular and neuropsychiatric symptoms. Consequently, maintaining or restoring microbiota-host symbiosis represents a new approach to treat these symptoms or to prevent their relapses. Current treatment approach assigned a primary role to live probiotics alone or in combination with prebiotics to enhance colonization of beneficial bacteria and to strengthen the symbiosis. However, several papers showed major benefits of heat-killed probiotics as compared to their live counterparts on both intestinal and systemic symptoms. Recently, in addition to killing probiotics, in a proof of concept study lysates (fragments) of probiotics in combination with vitamins A, B, D and omega 3 fatty acids were successfully tested. These findings suggested a conceptual change in the approach addressed to both the microbiota and host as targets for intervention. Orv. Hetil., 2014, 155(37), 1454-1460. LA - Hungarian DB - MTMT ER -