Teucher, Nils

[["dc.bibliographiccitation.firstpage","673"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","European Journal of Heart Failure"],["dc.bibliographiccitation.lastpage","680"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Schillinger, Wolfgang"],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Christians, Claus"],["dc.contributor.author","Kohlhaas, Michael"],["dc.contributor.author","Sossalla, Samuel"],["dc.contributor.author","Van Nguyen, Phuc"],["dc.contributor.author","Schmidt, Albrecht G."],["dc.contributor.author","Schunck, Ortwin"],["dc.contributor.author","Nebendahl, Klaus"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","Zeitz, Oliver"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.date.accessioned","2017-09-07T11:52:27Z"],["dc.date.available","2017-09-07T11:52:27Z"],["dc.date.issued","2006"],["dc.description.abstract","We investigated the hypothesis that increased intracellular [Na+](i) in heart failure contributes to preservation of SR Ca2+ load which may become particularly evident at slow heart rates. [Na+]i in SBFI-loaded myocytes from rabbits with pacing-induced heart failure (PHF) was significantly higher at each frequency as compared to Sham-operated animals. Furthermore, PHF rabbits demonstrated reduced SR Ca2+-ATPase protein levels (-37%, p < 0.04) but unchanged Na+/Ca2+ exchanger protein levels. At 0.25 Hz, isometric force was similar in cardiac trabeculae from PHF rabbits as compared to control (PHF, 3.6 +/- 1.3; Sham, 4.4 +/- 0.6 mN/mm(2)). Rapid cooling contractures (RCCs) were unchanged indicating preserved SR Ca2+ load at this frequency. In Sham, isometric twitch force increased with rising frequencies to 29.0 +/- 2.8 mN/mm(2) at 3.0 Hz (p < 0.05) as compared to 0.25 Hz. RCCs showed a parallel increase by 186 +/- 47% (p < 0.01). In PHF, frequency-dependent increase in force (15.8 +/- 4.7 mN/mm(2) at 3.0 Hz) and RCCs (increase by 70 +/- 40%) were significantly blunted. Thus, in PHF in rabbits SR Ca2+ load is preserved at low frequencies despite decreased SR Ca2+-ATPase expression. This may result from [Na+](i)-dependent changes in Na+/Ca2+ exchanger activity. (c) 2006 European Society of Cardiology. Published by Elsevier B.V All rights reserved."],["dc.identifier.doi","10.1016/j.ejheart.2006.01.013"],["dc.identifier.gro","3143598"],["dc.identifier.isi","000242383300002"],["dc.identifier.pmid","16540370"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1130"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1388-9842"],["dc.title","High intracellular Na+ preserves myocardial function at low heart rates in isolated myocardium from failing hearts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","996"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cardiovascular Research"],["dc.bibliographiccitation.lastpage","1003"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Schillinger, Wolfgang"],["dc.contributor.author","Ohler, A."],["dc.contributor.author","Embry, S. L."],["dc.contributor.author","Muller, F"],["dc.contributor.author","Christians, Claus"],["dc.contributor.author","Janssen, P. M. L."],["dc.contributor.author","Kogler, H."],["dc.contributor.author","Teucher, Niels"],["dc.contributor.author","Pieske, Burkert"],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.date.accessioned","2021-06-01T10:50:03Z"],["dc.date.available","2021-06-01T10:50:03Z"],["dc.date.issued","2003"],["dc.description.abstract","Objectives: The functional consequences of Na+/Ca2+ exchanger (NCX) overexpression in heart failure have been controversially discussed. NCX function strongly depends on intracellular sodium which has been shown to be increased in heart failure. Methods and results: We investigated the Na+/K+-ATPase (NKA) inhibitor ouabain (0.5-16 mumol/l) in electrically stimulated, isotonically contracting adult rabbit cardiocytes overexpressing NCX after adenoviral gene transfer (Ad-NCX-GFP, 48 h culture time). Myocytes transfected with adenovirus encoding for green fluorescent protein (Ad-GFP) served as a control. Contractions were analyzed by video-edge detection. In the Ad-NCX-GFP group, the maximum inotropic response was significantly reduced by 50.7% (P < 0.05). This was a result of an enhanced susceptibility to contracture after exposure to the drug (median concentration (25-75%): 4 (4-8) vs. 8 (6-16) mumol/l, P < 0.05). When analyzing relaxation before contracture, the maximum relaxation velocity was reduced (0.15 +/- 0.04 vs. 0.27 +/- 0.04 mum/s, P < 0.05) and the time from peak shortening to 90% of relaxation was increased (298 +/- 39 vs. 185 +/- 15 ms, P < 0.05). No differences in systolic and diastolic parameters were observed with the Na+ channel modulator BDF9198 (1 mumol/l). Conclusions: Inhibition of NKA by ouabain induces a combined diastolic and systolic dysfunction in NCX overexpressing rabbit myocytes. This may be the consequence of cytoplasmic Ca2+ overload due to inhibition of forward mode or induction of reverse mode Na+/Ca2+ exchange. In end-stage failing human myocardium and during digitalis treatment this mechanism may be of major importance. (C) 2003 European Society of Cardiology. Published by Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0008-6363(02)00829-5"],["dc.identifier.gro","3144121"],["dc.identifier.isi","000181975100014"],["dc.identifier.pmid","12650877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86511"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0008-6363"],["dc.title","The functional effect of adenoviral Na+/Ca2+ exchanger overexpression in rabbit myocytes depends on the activity of the Na+/K+-ATPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","263"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","European Journal of Cardio-Thoracic Surgery"],["dc.bibliographiccitation.lastpage","270"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Liakopoulos, Oliver Joannis"],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Muehlfed, Christian"],["dc.contributor.author","Middel, Peter"],["dc.contributor.author","Heusch, Gerd"],["dc.contributor.author","Schoendube, Friedrich Albert"],["dc.contributor.author","Doerge, Hilmar"],["dc.date.accessioned","2018-11-07T09:28:14Z"],["dc.date.available","2018-11-07T09:28:14Z"],["dc.date.issued","2006"],["dc.description.abstract","Objective: Cardiac surgery on cardiopulmonary bypass (CPB) results in progressive myocardial dysfunction, despite unimpaired coronary blood flow, and is associated with increased myocardial tumor necrosis factor-alpha (TNF alpha) expression. We investigated whether anti-inflammatory treatment prevents increased TNF alpha expression and myocardial dysfunction after CPB. Methods and results: Baseline systemic hemodynamics, myocardial contractile function, aortic and coronary blood flow were measured in anesthetized pigs. Then, placebo (PLA; saline; n = 7) or methylprednisolone (MP; 30 mg/kg; n = 6) was infused intravenously and CPB was instituted. Global ischemia was induced for 10 min by aortic cross-clamping, followed by 1 h of cardioplegic cardiac arrest. After declamping and reperfusion, CPB was terminated after a total of 3 h. Measurements were repeated at 15 min, 4 h, and 8 h following termination of CPB. Systemic TNF alpha-plasma concentrations and left ventricular TNF alpha expression were analyzed. With unchanged coronary blood flow in both groups, a progressive toss of myocardial contractile function to 38 +/- 2% of baseline (p < 0.01) and cardiac index to 48 +/- 6% of baseline (p < 0.01) at 8 h after CPB in PLA was attenuated in MP (myocardial function: 72 +/- 3%, p < 0.01 vs PLA; cardiac index: 78 +/- 6%, p < 0.05 vs PLA). Systemic TNFa was increased at 8 h in PLA compared to MP (243 +/- 34 vs 90 +/- 34 pg/ml, p < 0.05). Myocardial TNF alpha was increased at 8 h after CPB compared to baseline and MP (p < 0.05). Myocardial TNF alpha immunostaining was more pronounced in PLA than in MP (p < 0.05), with TNF alpha-mRNA localization predominantly to cardiomyocytes. Conclusions: Methylprednisolone attenuates both systemic and myocardial TNF alpha increases and progressive myocardial dysfunction induced by cardiac surgery, suggesting a key rote for TNF alpha. (c) 2006 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.ejcts.2006.04.019"],["dc.identifier.isi","000240508400014"],["dc.identifier.pmid","16829094"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30725"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1010-7940"],["dc.title","Prevention of TNF alpha-associated myocardial dysfunction resulting from cardiopulmonary bypass and cardioplegic arrest by glucocorticoid treatment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cardiovascular Therapeutics"],["dc.bibliographiccitation.lastpage","26"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Unsoeld, Bernhard W."],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Didie, Michael"],["dc.contributor.author","Sossalla, Samuel"],["dc.contributor.author","Jacobshagen, Claudius"],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Schillinger, Wolfgang"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.date.accessioned","2017-09-07T11:44:39Z"],["dc.date.available","2017-09-07T11:44:39Z"],["dc.date.issued","2015"],["dc.description.abstract","BackgroundPantoprazole has been shown to exert a negative inotropic effect in isolated myocardium. The purpose of this study was to evaluate the hemodynamic effects of pantoprazole in vivo in healthy myocardium and in the setting of heart failure. Methods and ResultsHealthy mice and mice with heart failure 4weeks after myocardial infarction induced by permanent LAD ligation were instrumented with a Millar Mikrotip conductance catheter to record pressure-volume loops. Pantoprazole was infused at rates of 3 and 10mg/kg/min intravenously, and hemodynamic parameters were recorded. Infusion of pantoprazole at increasing rates lead to a significant decline of end systolic LV pressure by decreasing heart rate, myocardial contractility and arterial elastance. These effects were quick, beginning immediately with the infusion and usually reaching a plateau after 2 or 3min of infusion. The effects on blood pressure and heart rate were of comparable size in healthy mice and mice with MI. However, in sham-operated mice, there was a compensatory increase in stroke volume that sufficed to maintain cardiac output at a constant level, which was missing in mice with MI. In 4 of 13 mice with MI infusion of 10mg/kg/min pantoprazole lead to pump failure, which was lethal in 2 of these animals. ConclusionAt higher infusion rates, pantoprazole is able to induce negative hemodynamic responses. In particular, in the setting of heart failure, these effects can lead to significant impairment of cardiac function. Therefore, high infusion rates of pantoprazole should be avoided especially in heart failure patients."],["dc.identifier.doi","10.1111/1755-5922.12102"],["dc.identifier.gro","3141966"],["dc.identifier.isi","000348660500004"],["dc.identifier.pmid","25529757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3057"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1755-5922"],["dc.relation.issn","1755-5914"],["dc.title","Negative Hemodynamic Effects of Pantoprazole at High Infusion Rates in Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Circulation: Cardiovascular Genetics"],["dc.bibliographiccitation.lastpage","652"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Buyandelger, Byambajav"],["dc.contributor.author","Mansfield, Catherine"],["dc.contributor.author","Kostin, Sawa"],["dc.contributor.author","Choi, Onjee"],["dc.contributor.author","Roberts, Angharad M."],["dc.contributor.author","Ware, James S."],["dc.contributor.author","Mazzarotto, Francesco"],["dc.contributor.author","Pesce, Francesco"],["dc.contributor.author","Buchan, Rachel"],["dc.contributor.author","Isaacson, Rivka L."],["dc.contributor.author","Vouffo, Josee"],["dc.contributor.author","Gunkel, Sylvia"],["dc.contributor.author","Knoll, Gudrun"],["dc.contributor.author","McSweeney, Sara J."],["dc.contributor.author","Wei, Heming"],["dc.contributor.author","Perrot, Andreas"],["dc.contributor.author","Pfeiffer, Conny"],["dc.contributor.author","Toliat, Mohammad Reza"],["dc.contributor.author","Ilieva, Kristina"],["dc.contributor.author","Krysztofinska, Ewelina"],["dc.contributor.author","Lopez-Olaneta, Marina M."],["dc.contributor.author","Gomez-Salinero, Jesus M."],["dc.contributor.author","Schmidt, Albrecht"],["dc.contributor.author","Ng, Keat-Eng"],["dc.contributor.author","Teucher, Niels"],["dc.contributor.author","Chen, Ju"],["dc.contributor.author","Teichmann, Martin"],["dc.contributor.author","Eilers, Martin"],["dc.contributor.author","Haverkamp, Wilhelm"],["dc.contributor.author","Regitz-Zagrosek, Vera"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Braun, Thomas"],["dc.contributor.author","Pennell, Dudley J."],["dc.contributor.author","Gould, Ian"],["dc.contributor.author","Barton, Paul J. R."],["dc.contributor.author","Lara-Pezzi, Enrique"],["dc.contributor.author","Schaefer, Sebastian"],["dc.contributor.author","Hübner, Norbert"],["dc.contributor.author","Felkin, Leanne E."],["dc.contributor.author","O'Regan, D. P."],["dc.contributor.author","Brand, Thomas"],["dc.contributor.author","Milting, Hendrik"],["dc.contributor.author","Nürnberg, Peter"],["dc.contributor.author","Schneider, Michael D."],["dc.contributor.author","Prasad, Sanjay"],["dc.contributor.author","Petretto, Enrico"],["dc.contributor.author","Knoll, Ralph"],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Background Mutations in sarcomeric and cytoskeletal proteins are a major cause of hereditary cardiomyopathies, but our knowledge remains incomplete as to how the genetic defects execute their effects. Methods and Results We used cysteine and glycine-rich protein 3, a known cardiomyopathy gene, in a yeast 2-hybrid screen and identified zinc-finger and BTB domain-containing protein 17 (ZBTB17) as a novel interacting partner. ZBTB17 is a transcription factor that contains the peak association signal (rs10927875) at the replicated 1p36 cardiomyopathy locus. ZBTB17 expression protected cardiac myocytes from apoptosis in vitro and in a mouse model with cardiac myocyte-specific deletion of Zbtb17, which develops cardiomyopathy and fibrosis after biomechanical stress. ZBTB17 also regulated cardiac myocyte hypertrophy in vitro and in vivo in a calcineurin-dependent manner. Conclusions We revealed new functions for ZBTB17 in the heart, a transcription factor that may play a role as a novel cardiomyopathy gene."],["dc.identifier.doi","10.1161/CIRCGENETICS.113.000690"],["dc.identifier.gro","3141815"],["dc.identifier.isi","000363373800003"],["dc.identifier.pmid","26175529"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1379"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1942-3268"],["dc.relation.issn","1942-325X"],["dc.title","ZBTB17 (MIZ1) Is Important for the Cardiac Stress Response and a Novel Candidate Gene for Cardiomyopathy and Heart Failure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","758"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Circulation Research"],["dc.bibliographiccitation.lastpage","U153"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Knöll, Ralph"],["dc.contributor.author","Linke, Wolfgang A."],["dc.contributor.author","Zou, Peijian"],["dc.contributor.author","Miocic, Snjezana"],["dc.contributor.author","Kostin, Sawa"],["dc.contributor.author","Buyandelger, Byambajav"],["dc.contributor.author","Ku, Ching-Hsin"],["dc.contributor.author","Neef, Stefan"],["dc.contributor.author","Bug, Monika"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Knöll, Gudrun"],["dc.contributor.author","Felkin, Leanne E."],["dc.contributor.author","Wessels, Johannes T."],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Hagn, Franz"],["dc.contributor.author","Kessler, Horst"],["dc.contributor.author","Didie, Michael"],["dc.contributor.author","Quentin, Thomas"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Unsoeld, Bernhard W."],["dc.contributor.author","Schmidt, Albrecht"],["dc.contributor.author","Birks, Emma J."],["dc.contributor.author","Gunkel, Sylvia"],["dc.contributor.author","Lang, Patrick"],["dc.contributor.author","Granzier, Henk"],["dc.contributor.author","Zimmermann, Wolfram-Hubertus"],["dc.contributor.author","Field, Loren J."],["dc.contributor.author","Faulkner, Georgine"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Barton, Paul J. R."],["dc.contributor.author","Sattler, Michael"],["dc.contributor.author","Wilmanns, Matthias"],["dc.contributor.author","Chien, Kenneth R."],["dc.date.accessioned","2017-09-07T11:43:24Z"],["dc.date.available","2017-09-07T11:43:24Z"],["dc.date.issued","2011"],["dc.description.abstract","Rationale: Telethonin (also known as titin-cap or t-cap) is a 19-kDa Z-disk protein with a unique beta-sheet structure, hypothesized to assemble in a palindromic way with the N-terminal portion of titin and to constitute a signalosome participating in the process of cardiomechanosensing. In addition, a variety of telethonin mutations are associated with the development of several different diseases; however, little is known about the underlying molecular mechanisms and telethonin's in vivo function. Objective: Here we aim to investigate the role of telethonin in vivo and to identify molecular mechanisms underlying disease as a result of its mutation. Methods and Results: By using a variety of different genetically altered animal models and biophysical experiments we show that contrary to previous views, telethonin is not an indispensable component of the titin-anchoring system, nor is deletion of the gene or cardiac specific overexpression associated with a spontaneous cardiac phenotype. Rather, additional titin-anchorage sites, such as actin-titin cross-links via alpha-actinin, are sufficient to maintain Z-disk stability despite the loss of telethonin. We demonstrate that a main novel function of telethonin is to modulate the turnover of the proapoptotic tumor suppressor p53 after biomechanical stress in the nuclear compartment, thus linking telethonin, a protein well known to be present at the Z-disk, directly to apoptosis (\"mechanoptosis\"). In addition, loss of telethonin mRNA and nuclear accumulation of this protein is associated with human heart failure, an effect that may contribute to enhanced rates of apoptosis found in these hearts. Conclusions: Telethonin knockout mice do not reveal defective heart development or heart function under basal conditions, but develop heart failure following biomechanical stress, owing at least in part to apoptosis of cardiomyocytes, an effect that may also play a role in human heart failure. (Circ Res. 2011; 109: 758-769.)"],["dc.identifier.doi","10.1161/CIRCRESAHA.111.245787"],["dc.identifier.gro","3142667"],["dc.identifier.isi","000294950000008"],["dc.identifier.pmid","21799151"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0009-7330"],["dc.title","Telethonin Deficiency Is Associated With Maladaptation to Biomechanical Stress in the Mammalian Heart"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Heart Journal"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Miller, SLW"],["dc.contributor.author","Loughrey, C."],["dc.contributor.author","Kania, A."],["dc.contributor.author","Burow, A."],["dc.contributor.author","Teucher, N."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Smith, Godfrey L."],["dc.date.accessioned","2018-11-07T10:37:13Z"],["dc.date.available","2018-11-07T10:37:13Z"],["dc.date.issued","2003"],["dc.format.extent","667"],["dc.identifier.doi","10.1016/S0195-668X(03)96074-X"],["dc.identifier.isi","000185638802427"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45512"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","W B Saunders Co Ltd"],["dc.publisher.place","London"],["dc.relation.conference","Congress of the European-Society-of-Cardiology"],["dc.relation.eventlocation","VIENNA, AUSTRIA"],["dc.relation.issn","0195-668X"],["dc.title","Sorcin over-expression reduces contractility by affecting intracellular and trans-sarcolemmal Ca2+ cycling in cardiomyocytes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Heart Journal"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Gupta, S. N."],["dc.contributor.author","Rokita, Adam G."],["dc.contributor.author","Schmidt, K."],["dc.contributor.author","Unsoeld, Bernhard W."],["dc.contributor.author","Teucher, N."],["dc.contributor.author","Sowa, T."],["dc.contributor.author","Sag, Can Martin"],["dc.contributor.author","Neef, S."],["dc.contributor.author","Maier, Lars. S."],["dc.date.accessioned","2018-11-07T11:11:17Z"],["dc.date.available","2018-11-07T11:11:17Z"],["dc.date.issued","2008"],["dc.format.extent","19"],["dc.identifier.isi","000208702500066"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53396"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.issn","0195-668X"],["dc.title","CaMKII prolongs action potential duration in pressure overload induced hypertrophy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Rokita, Adam G."],["dc.contributor.author","Unsoeld, Bernhard W."],["dc.contributor.author","Sossalla, Samuel T."],["dc.contributor.author","Becker, Alexander"],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Grebe, Cornelia"],["dc.contributor.author","Preuss, Lena"],["dc.contributor.author","Gupta, Shamindra N."],["dc.contributor.author","Schmidt, Kathie"],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Schäfer, Katrin"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Zhu, W."],["dc.contributor.author","Reuter, Sean P."],["dc.contributor.author","Field, Loren J."],["dc.contributor.author","Kararigas, Georgios"],["dc.contributor.author","Regitz-Zagrosek, Vera"],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Krueger, Martina"],["dc.contributor.author","Linke, Wolfgang A."],["dc.contributor.author","Backs, Johannes"],["dc.date.accessioned","2018-11-07T08:56:56Z"],["dc.date.available","2018-11-07T08:56:56Z"],["dc.date.issued","2011"],["dc.format.extent","E421"],["dc.identifier.doi","10.1161/CIRCULATIONAHA.110.017566"],["dc.identifier.isi","000289833500003"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23266"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","0009-7322"],["dc.title","Response to Letter Regarding Article, \"Differential Cardiac Remodeling in Preload Versus Afterload\""],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2724"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","2732"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Koegler, Harald"],["dc.contributor.author","Schott, Peter"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Milting, Hendrik"],["dc.contributor.author","Van, Phuc Nguyen"],["dc.contributor.author","Kohlhaas, Michael"],["dc.contributor.author","Grebe, Cornelia"],["dc.contributor.author","Kassner, Astrid"],["dc.contributor.author","Domeier, Erik"],["dc.contributor.author","Teucher, Nils"],["dc.contributor.author","Seidler, Tim"],["dc.contributor.author","Knoell, Ralph"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","El-Banayosy, Aly"],["dc.contributor.author","Koerfer, Reiner"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.date.accessioned","2017-09-07T11:52:41Z"],["dc.date.available","2017-09-07T11:52:41Z"],["dc.date.issued","2006"],["dc.description.abstract","Background - In heart failure ( HF), ventricular myocardium expresses brain natriuretic peptide ( BNP). Despite the association of elevated serum levels with poor prognosis, BNP release is considered beneficial because of its antihypertrophic, vasodilating, and diuretic properties. However, there is evidence that BNP-mediated signaling may adversely influence cardiac remodeling, with further impairment of calcium homeostasis. Methods and Results - We studied the effects of BNP on preload-dependent myocardial sarcoplasmic reticulum Ca2+ ATPase ( SERCA2a) expression. In rabbit isolated muscle strips stretched to high preload and shortening isotonically over 6 hours, the SERCA/glyceraldehyde phosphate dehydrogenase mRNA ratio was enhanced by 168% ( n = 8) compared with unloaded preparations ( n = 8; P < 0.001). Recombinant human BNP at a concentration typically found in end-stage HF patients ( 350 pg/mL) abolished SERCA upregulation by stretch ( n = 9; P < 0.0001 versus BNP free). Inhibition of cyclic guanosine 3', 5' monophosphate ( cGMP)-phosphodiesterase-5 mimicked this effect, whereas inhibition of cGMP-dependent protein kinase restored preload-dependent SERCA upregulation in the presence of recombinant human BNP. Furthermore, in myocardium from human end-stage HF patients undergoing cardiac transplantation ( n = 15), BNP expression was inversely correlated with SERCA levels. Moreover, among 23 patients treated with left ventricular assist devices, significant SERCA2a recovery occurred in those downregulating BNP. Conclusions - Our data indicate that preload stimulates SERCA expression. BNP antagonizes this mechanism via guanylyl cyclase-A, cGMP, and cGMP-dependent protein kinase. This novel action of BNP to uncouple preload-dependent SERCA expression may adversely affect contractility in patients with HF."],["dc.identifier.doi","10.1161/CIRCULATIONAHA.105.608828"],["dc.identifier.gro","3143676"],["dc.identifier.isi","000238223400010"],["dc.identifier.pmid","16754798"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1216"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1524-4539"],["dc.relation.issn","0009-7322"],["dc.title","Relevance of brain natriuretic peptide in preload-dependent regulation of cardiac sarcoplasmic reticulum Ca2+ ATPase expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]