TY - JOUR AU - Szabó, Renáta AU - Börzsei, Denise AU - Karácsonyi, Zoltán AU - Gesztelyi, Rudolf AU - Nemes, Kolos AU - Magyariné, Berkó Anikó AU - Veszelka, Médea AU - Török, Szilvia AU - Kupai, Krisztina AU - Varga, Csaba AU - Juhász, Béla AU - Pósa, Anikó TI - Postconditioning-like effect of exercis: new paradigm in experimental menopause JF - AMERICAN JOURNAL OF PHYSIOLOGY: HEART AND CIRCULATORY PHYSIOLOGY J2 - AM J PHYSIOL HEART C VL - 316 PY - 2019 IS - 2 SP - H400 EP - H407 PG - 8 SN - 0363-6135 DO - 10.1152/ajpheart.00485.2018 UR - https://m2.mtmt.hu/api/publication/30375043 ID - 30375043 N1 - Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Export Date: 26 August 2019 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4 Funding details: Emberi Eroforrások Minisztériuma, 20391-3/2018/FEKUSTRAT Funding details: European Social Fund, EFOP-3.6.2-16-2017-00009 Funding details: European Commission Funding details: UNKP-17-2, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Export Date: 28 August 2019 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4 Funding details: Emberi Eroforrások Minisztériuma, 20391-3/2018/FEKUSTRAT Funding details: European Social Fund, EFOP-3.6.2-16-2017-00009 Funding details: European Commission Funding details: UNKP-17-2, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Export Date: 29 January 2020 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4; peroxidase, 9003-99-0; Estrogens; Glutathione; Heme Oxygenase (Decyclizing); L-Lactate Dehydrogenase; Peroxidase; Tumor Necrosis Factor-alpha Funding details: Emberi Eroforrások Minisztériuma, 20391-3/2018/FEKUSTRAT Funding details: European Social Fund, EFOP-3.6.2-16-2017-00009 Funding details: European Commission Funding details: UNKP-17-2, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Funding Agency and Grant Number: New National Excellence Program of the Ministry of Human Capacities Grants [UNKP-17-3, UNKP-17-4, UNKP-17-2, GINOP-2.3.2-15-2016-00062]; Ministry of Human Capacities, Hungary [20391-3/2018/FEKUSTRAT]; European UnionEuropean Union (EU); European Social FundEuropean Social Fund (ESF) [EFOP-3.6.2-16-2017-00009] Funding text: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renata), UNKP-17-4 (to P. Aniko), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Export Date: 4 June 2020 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4; peroxidase, 9003-99-0; Estrogens; Glutathione; Heme Oxygenase (Decyclizing); L-Lactate Dehydrogenase; Peroxidase; Tumor Necrosis Factor-alpha Funding details: Emberi Eroforrások Minisztériuma, EMMI, UNKP-17-2, 20391-3/2018/FEKUSTRAT, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding details: European Social Fund, ESF, EFOP-3.6.2-16-2017-00009 Funding details: European Commission, EC Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Export Date: 29 August 2020 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4; peroxidase, 9003-99-0; Estrogens; Glutathione; Heme Oxygenase (Decyclizing); L-Lactate Dehydrogenase; Peroxidase; Tumor Necrosis Factor-alpha Funding details: Emberi Eroforrások Minisztériuma, EMMI, UNKP-17-2, 20391-3/2018/FEKUSTRAT, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding details: European Social Fund, ESF, EFOP-3.6.2-16-2017-00009 Funding details: European Commission, EC Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Cited By :1 Export Date: 10 January 2021 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Univ. of Szeged, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4; peroxidase, 9003-99-0; Estrogens; Glutathione; Heme Oxygenase (Decyclizing); L-Lactate Dehydrogenase; Peroxidase; Tumor Necrosis Factor-alpha Funding details: Emberi Eroforrások Minisztériuma, EMMI, UNKP-17-2, 20391-3/2018/FEKUSTRAT, UNKP-17-3, UNKP-17-4, GINOP-2.3.2-15-2016-00062 Funding details: European Social Fund, ESF, EFOP-3.6.2-16-2017-00009 Funding details: European Commission, EC Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Funding Agency and Grant Number: New National Excellence Program of the Ministry of Human Capacities Grants [UNKP-17-3, UNKP-17-4, UNKP-17-2, GINOP-2.3.2-15-2016-00062]; Ministry of Human Capacities, Hungary [20391-3/2018/FEKUSTRAT]; European UnionEuropean Commission; European Social FundEuropean Social Fund (ESF) [EFOP-3.6.2-16-2017-00009] Funding text: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renata), UNKP-17-4 (to P. Aniko), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Orthopaedics, University of Debrecen, Debrecen, Hungary Department of Pharmacology and Pharmacotherapy, University of Debrecen, Debrecen, Hungary Department of Physiology, Anatomy, and Neuroscience, Interdisciplinary Excellence Centre, University of Szeged, Szeged, Hungary Cited By :2 Export Date: 12 March 2021 CODEN: AJPPD Correspondence Address: Pósa, A.; Pósa, Közép Fasor 52, Hungary; email: paniko@bio.uszeged.hu Chemicals/CAS: alanine aminotransferase, 9000-86-6, 9014-30-6; alkaline phosphatase, 9001-78-9; aspartate aminotransferase, 9000-97-9; glutathione, 70-18-8; glutathione disulfide, 27025-41-8; heme oxygenase, 9059-22-7; lactate dehydrogenase, 9001-60-9; myeloperoxidase; triptorelin, 57773-63-4; peroxidase, 9003-99-0; Estrogens; Glutathione; Heme Oxygenase (Decyclizing); L-Lactate Dehydrogenase; Peroxidase; Tumor Necrosis Factor-alpha Funding details: European Commission, EC Funding details: European Social Fund, ESF, EFOP-3.6.2-16-2017-00009 Funding details: Emberi Eroforrások Minisztériuma, 20391-3/2018/FEKUSTRAT, GINOP-2.3.2-15-2016-00062, UNKP-17-2, UNKP-17-3, UNKP-17-4 Funding text 1: This work was supported by the New National Excellence Program of the Ministry of Human Capacities Grants UNKP-17-3 (to S. Renáta), UNKP-17-4 ( to P. Anikó), and UNKP-17-2 (B. Denise), GINOP-2.3.2-15-2016-00062, and Ministry of Human Capacities, Hungary Grant 20391-3/2018/FEKUSTRAT. Furthermore, this work was supported by the European Union, cofinanced by the European Social Fund (EFOP-3.6.2-16-2017-00009). AB - The progression of coronary artery diseases in premenopausal women is lower than in age-matched men; however, its probability increases rapidly after menopause. The aim of our study was to investigate the postconditioning-like effects of voluntary physical exercise on postmenopausal cardiovascular outcomes after myocardial infarction. We used fertile Wistar females [control (CTRL)] and pharmacologically induced estrogen-deficient (POVX; 750 mu g/kg triptorelin im. every 4th week) rats. CTRL and POVX animals were randomly assigned to receive an injection of 0.1 mg isoproterenol (ISO)/kg. At the 20th hour after ISO injection, serum markers of myocardial injury, such as lactate dehydrogenase (LDH) and myoglobin, were measured. After a 3-wk resting period, ISO-treated and untreated animals were further divided into subgroups on the basis of 6 wk of physical exercise. At the end of the experiment, cardiac activity and content of the antioxidative heme oxygenase (HO) enzyme, levels of GSM and GSH + GSSG, activity of myeloperoxidase, as well as the concentration of TNF-alpha were determined. At the end of the experimental period, we observed a significant decrease in the activity and content of HO enzymes in POVX and POVX/ISO rats, whereas physical exercise significantly improved 110 and GSH values in both CTRL and POVX rats. Furthermore, our training protocol significantly reduced the pathological levels of myeloperoxidase and TNF-alpha. Our findings clearly demonstrate that modulation of the HO system by voluntary physical exercise is a key process to decrease inflammatory parameters and ameliorate the antioxidative status in estrogen-deficient conditions postmyocardial injury. LA - English DB - MTMT ER - TY - JOUR AU - Pósa, Anikó AU - Szabó, Renáta AU - Kupai, Krisztina AU - Magyariné, Berkó Anikó AU - Veszelka, Médea AU - Szűcs, Gergő AU - Börzsei, Denise AU - Gyongyosi, M AU - Pavo, I AU - Deim, Zoltán AU - Szilvássy, Zoltán AU - Juhász, Béla AU - Varga, Csaba TI - Cardioprotective Effect of Selective Estrogen Receptor Modulator Raloxifene Are Mediated by Heme Oxygenase in Estrogen-Deficient Rat JF - OXIDATIVE MEDICINE AND CELLULAR LONGEVITY J2 - OXID MED CELL LONGEV VL - 2017 PY - 2017 PG - 9 SN - 1942-0900 DO - 10.1155/2017/2176749 UR - https://m2.mtmt.hu/api/publication/3258158 ID - 3258158 N1 - Department of Physiology, Anatomy and Neuroscience, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary Department of Cardiology, Medical University of Vienna, Vienna, Austria Department of Pharmacology and Pharmacotherapy, Faculty of Medicine, University of Debrecen, Debrecen, Hungary Cited By :14 Export Date: 20 October 2023 Correspondence Address: Posa, A.; Department of Physiology, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: argipressin, 113-79-1; epinephrine, 51-43-4, 55-31-2, 6912-68-1; estradiol, 50-28-2; heme oxygenase 2, 391963-41-0; myeloperoxidase; phentolamine, 50-60-2, 73-05-2; protoporphyrin tin, 14325-05-4; raloxifene, 82640-04-8, 84449-90-1; heme oxygenase, 9059-22-7; Cardiotonic Agents; Estrogens; Heme Oxygenase (Decyclizing); heme oxygenase-2; Hmox1 protein, rat; Raloxifene Hydrochloride; Receptors, Estrogen Manufacturers: Novo Nordisk, Denmark; Lilly, United States AB - Estrogens and raloxifene (RAL) have beneficial effects on certain cardiovascular indices in postmenopausal women characterized by estrogen deficiency. Heme oxygenase (HO) activity is increased by 17 beta-estradiol (E-2) and RAL in estrogen-deficient rat resulting in vasorelaxation mediated by carbon monoxide. We determined the expressions of HO in cardiac and aortic tissues after ovariectomy (OVX) and subsequent RAL or E-2 treatment. We investigated the effects of pharmacological inhibition of HO enzyme on the arginine vasopressin-(AVP-) induced blood pressure in vivo, the epinephrine- and phentolamine-induced electrocardiogram ST segment changes in vivo, and the myeloperoxidase (MPO) enzyme activity. When compared with intact females, OVX decreased the HO-1 and HO-2 expression, aggravated the electrocardiogram signs of heart ischemia and the blood pressure response to AVP, and increased the cardiac MPO. E-2 and RAL are largely protected against these negative impacts induced by OVX. The pharmacological inhibition of HO in E-2- or RAL-treated OVX animals, however, restored the cardiovascular status close to that observed in nontreated OVX animals. The decreased expression of HO enzymes and the changes in blood pressure ischemia susceptibility and inflammatory state in OVX rat can be reverted by the administration of E-2 or RAL partly through its antioxidant and anti-inflammatory roles. LA - English DB - MTMT ER - TY - JOUR AU - Cabrera-Fuentes, HA AU - Aragones, J AU - Bernhagen, J AU - Boening, A AU - Boisvert, WA AU - Botker, HE AU - Bulluck, H AU - Cook, S AU - Di Lisa, F AU - Engel, FB AU - Engelmann, B AU - Ferrazzi, F AU - Ferdinandy, Péter AU - Fong, A AU - Fleming, I AU - Gnaiger, E AU - Hernandez-Resendiz, S AU - Kalkhoran, SB AU - Kim, MH AU - Lecour, S AU - Liehn, EA AU - Marber, MS AU - Mayr, M AU - Miura, T AU - Ong, SB AU - Peter, K AU - Sedding, D AU - Singh, MK AU - Suleiman, MS AU - Schnittler, HJ AU - Schulz, R AU - Shim, W AU - Tello, D AU - Vogel, CW AU - Walker, M AU - Li, QO AU - Yellon, DM AU - Hausenloy, DJ AU - Preissner, KT TI - From basic mechanisms to clinical applications in heart protection, new players in cardiovascular diseases and cardiac theranostics: meeting report from the third international symposium on "New frontiers in cardiovascular research" JF - BASIC RESEARCH IN CARDIOLOGY J2 - BASIC RES CARDIOL VL - 111 PY - 2016 IS - 6 PG - 13 SN - 0300-8428 DO - 10.1007/s00395-016-0586-x UR - https://m2.mtmt.hu/api/publication/3126895 ID - 3126895 N1 - Megjegyzés-27190691 In press-ként idézi a fenti közleményt! Institute of Biochemistry, Medical School, Justus-Liebig University, Giessen, Germany Cardiovascular and Metabolic Disorders Program, Duke-National University of Singapore, 8 College Road, Singapore, 169857, Singapore National Heart Research Institute Singapore, National Heart Centre Singapore, Singapore, Singapore Department of Microbiology, Kazan Federal University, Kazan, Russian Federation Centro de Biotecnología-FEMSA, Tecnológico de Monterrey, Monterrey, NL, Mexico Research Unit, Hospital of Santa Cristina, Research Institute Princesa, Autonomous University of Madrid, Madrid, Spain Department of Vascular Biology, Institute for Stroke and Dementia Research, Klinikum der Ludwig-Maximilians-Universität, Munich, Germany Munich Cluster for Systems Neurology (SyNergy), Munich, Germany Department of Cardiovascular Surgery, Medical School, Justus-Liebig-University, Giessen, Germany Center for Cardiovascular Research, John A. Burns School of Medicine, University of Hawaii, Honolulu, United States Department of Cardiology, Aarhus University Hospital, Skejby, Aarhus N, Denmark Department of Biomedical Sciences, University of Padova, Padua, Italy Experimental Renal and Cardiovascular Research, Department of Nephropathology, Institute of Pathology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nuremberg, Germany Institut für Laboratoriumsmedizin, Ludwig-Maximilians-Universität, Munich, Germany Institute of Human Genetics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nuremberg, Germany Department of Pharmacology and Pharmacotherapy, Semmelweis University, Budapest, Hungary Pharmahungary Group, Szeged, Hungary Department of Cardiology, Sarawak Heart Centre, Sarawak, Malaysia Institute for Vascular Signalling, Centre for Molecular Medicine, Goethe-University, Frankfurt, Germany D. Swarovski Research Lab, Department of Visceral, Transplant Thoracic Surgery, Medical Univ Innsbruck, Innsbruck, Austria Department of Cardiology, Dong-A University Hospital, Busan, South Korea Hatter Institute and MRC Inter-University Cape Heart Unit, Faculty of Health Sciences, University of Cape Town, Cape Town, South Africa Institute for Molecular Cardiovascular Research, RWTH University Hospital, Aachen, Germany Department of Cardiology, The Rayne Institute, St Thomas’ Campus, King’s College London, London, United Kingdom The James Black Centre, King’s College, University of London, London, United Kingdom Department of Cardiovascular, Renal and Metabolic Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan Baker IDI Heart and Diabetes Institute, Melbourne, Australia Department of Cardiology and Angiology, Hannover Medical School, Hannover, Germany Bristol Heart Institute, University of Bristol, Bristol Royal Infirmary, Bristol, United Kingdom Institute of Anatomy and Vascular Biology, Westfalian-Wilhelms-University, Münster, Germany Institute of Physiology, Justus-Liebig University, Giessen, Germany Department of Pathology, John A. Burns School of Medicine, University of Hawaii, Honolulu, United States The Hatter Cardiovascular Institute, University College London, London, United Kingdom The National Institute of Health Research University College London Hospitals Biomedical Research Centre, London, United Kingdom Department of Cardiovascular Medicine, National Institute of Cardiology, Ignacio Chavez, Mexico, D.F., Mexico Cited By :25 Export Date: 14 July 2019 CODEN: BRCAB Correspondence Address: Hausenloy, D.J.; Cardiovascular and Metabolic Disorders Program, Duke-National University of Singapore, 8 College Road, Singapore; email: derek.hausenloy@duke-nus.edu.sg AB - In this meeting report, particularly addressing the topic of protection of the cardiovascular system from ischemia/reperfusion injury, highlights are presented that relate to conditioning strategies of the heart with respect to molecular mechanisms and outcome in patients' cohorts, the influence of co-morbidities and medications, as well as the contribution of innate immune reactions in cardioprotection. Moreover, developmental or systems biology approaches bear great potential in systematically uncovering unexpected components involved in ischemia-reperfusion injury or heart regeneration. Based on the characterization of particular platelet integrins, mitochondrial redox-linked proteins, or lipid-diol compounds in cardiovascular diseases, their targeting by newly developed theranostics and technologies opens new avenues for diagnosis and therapy of myocardial infarction to improve the patients' outcome. LA - English DB - MTMT ER - TY - JOUR AU - Pósa, Anikó AU - Pavo, I AU - Varga, Csaba TI - Heme oxygenase contributes to estradiol and raloxifene-induced vasorelaxation in estrogen deficiency JF - INTERNATIONAL JOURNAL OF CARDIOLOGY J2 - INT J CARDIOL VL - 189 PY - 2015 IS - 1 SP - 252 EP - 254 PG - 3 SN - 0167-5273 DO - 10.1016/j.ijcard.2015.04.112 UR - https://m2.mtmt.hu/api/publication/2885084 ID - 2885084 N1 - Cited By :7 Export Date: 17 February 2023 CODEN: IJCDD Correspondence Address: Pósa, A.; Department of Physiology, Kozep fasor 52, Hungary; email: paniko@bio.u-szeged.hu Chemicals/CAS: argipressin, 113-79-1; carbon monoxide, 630-08-0; endothelial nitric oxide synthase, 503473-02-7; estradiol, 50-28-2; heme oxygenase, 9059-22-7; phenylephrine, 532-38-7, 59-42-7, 61-76-7; protoporphyrin, 553-12-8; raloxifene, 82640-04-8, 84449-90-1; Estradiol; Estrogens; Heme Oxygenase (Decyclizing); Raloxifene Hydrochloride LA - English DB - MTMT ER - TY - JOUR AU - Pósa, Anikó AU - Kupai, Krisztina AU - Ménesi, Rudolf AU - Szalai, Zita AU - Szabó, Renáta AU - Pintér, Zoltán AU - Pálfi, György AU - Gyöngyösi, M AU - Magyariné, Berkó Anikó AU - Pávó, I AU - Varga, Csaba TI - Sexual dimorphism of cardiovascular ischemia susceptibility is mediated by heme oxygenase JF - OXIDATIVE MEDICINE AND CELLULAR LONGEVITY J2 - OXID MED CELL LONGEV VL - 2013 PY - 2013 IS - Special Issue PG - 11 SN - 1942-0900 DO - 10.1155/2013/521563 UR - https://m2.mtmt.hu/api/publication/2473505 ID - 2473505 AB - We investigated the gender differences in heme-oxygenase (HO) enzyme, which produces endogenous vascular protective carbon monoxide (CO). We studied (1) the activity and expression of HO enzymes in the left ventricle (LV) and aorta, (2) basal increase in basal blood pressure provoked by arginine vasopressine (AVP) in vivo, (3) the heart perfusion induced by AVP, (4) the ST segment depression provoked by adrenaline and 30 seconds later phentolamine, and (5) the aorta ring contraction induced by AVP in female and male Wistar rats. We found that HO activity and the expression of HO-1 and HO-2 were increased in female rat aorta and LV. We demonstrated that the basal blood pressure and administration of AVP provoked blood pressure response are increased in the males; the female myocardium was less sensitive towards angina. Both differences could be aggravated by the inhibition of HO. The aorta rings were more susceptible towards vasoconstriction by AVP in males; isolated heart perfusion decrease was higher in males. The HO inhibition aggravated the heart perfusion in both sexes. In conclusion, the increased HO activity and expression in females might play a role in the sexual dimorphism of cardiovascular ischemia susceptibility during the reproductive age. © 2013 Anikó Pósa et al. LA - English DB - MTMT ER - TY - JOUR AU - Juhász, Béla AU - Thirunavukkarasu, M AU - Pant, R AU - Zhan, L AU - Penumathsa, SV AU - Secor, ER AU - Srivastava, S AU - Raychaudhuri, U AU - Menon, VP AU - Otani, H AU - Thrall, RS AU - Maulik, N TI - Bromelain induces cardioprotection against ischemia-reperfusion injury through Akt/FOXO pathway in rat myocardium JF - AMERICAN JOURNAL OF PHYSIOLOGY: HEART AND CIRCULATORY PHYSIOLOGY J2 - AM J PHYSIOL HEART C VL - 294 PY - 2008 IS - 3 SP - H1365 EP - H1370 SN - 0363-6135 DO - 10.1152/ajpheart.01005.2007 UR - https://m2.mtmt.hu/api/publication/1195223 ID - 1195223 LA - English DB - MTMT ER - TY - JOUR AU - Pacher, Pál AU - Mukhopadhyay, P AU - Mohanraj, R AU - Godlewski, G AU - Batkai, S AU - Kunos, G TI - Modulation of the endocannabinoid system in cardiovascular disease: therapeutic potential and limitations JF - HYPERTENSION J2 - HYPERTENSION VL - 52 PY - 2008 IS - 4 SP - 601 EP - 607 PG - 7 SN - 0194-911X DO - 10.1161/HYPERTENSIONAHA.105.063651 UR - https://m2.mtmt.hu/api/publication/2204594 ID - 2204594 N1 - Megjegyzés-23491427 : Pal/0000-0001-7036-8108 LA - English DB - MTMT ER -