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3. Glial cell line derived neurotrophic factor (GDNF) induces mucosal healing via intestinal stem cell niche activation.

Author

Hörner, Marius, Burkard, Natalie, Kelm, Matthias, Leist, Antonia, Selig, Thekla, Kollmann, Catherine, Meir, Michael, Otto, Christoph, Germer, Christoph‐Thomas, Kretzschmar, Kai, Flemming, Sven, and Schlegel, Nicolas

Subjects
*STEM cell niches, *WOUND healing, *SODIUM sulfate, *INTESTINAL mucosa, *NEUROGLIA
Abstract

Mucosal healing is critical to maintain and restore intestinal homeostasis in inflammation. Previous data provide evidence that glial cell line‐derived neurotrophic factor (GDNF) restores epithelial integrity by largely undefined mechanisms. Here, we assessed the role of GDNF for mucosal healing. In dextran sodium sulphate (DSS)‐induced colitis in mice application of GDNF enhanced recovery as revealed by reduced disease activity index and histological inflammation scores. In biopsy‐based wounding experiments GDNF application in mice improved healing of the intestinal mucosa. GDNF‐induced epithelial recovery was also evident in wound assays from intestinal organoids and Caco2 cells. These observations were accompanied by an increased number of Ki67‐positive cells in vivo after GDNF treatment, which were present along elongated proliferative areas within the crypts. In addition, the intestinal stem cell marker and R‐spondin receptor LGR5 was significantly upregulated following GDNF treatment in all experimental models. The effects of GDNF on cell proliferation, LGR5 and Ki67 upregulation were blocked using the RET‐specific inhibitor BLU‐667. Downstream of RET‐phosphorylation, activation of Src kinase was involved to mediate GDNF effects. GDNF promotes intestinal wound healing by promoting cell proliferation. This is mediated by RET‐dependent activation of Src kinase with consecutive LGR5 upregulation, indicating activation of the stem cell niche. [ABSTRACT FROM AUTHOR]

Published
2024
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4. Neurotrophic factor GDNF regulates intestinal barrier function in inflammatory bowel disease

Author

Meir, Michael, Burkard, Natalie, Ungewi[beta], Hanna, Diefenbacher, Markus, Flemming, Sven, Kannapin, Felix, Germer, Christoph-Thomas, Schweinlin, Matthias, Metzger, Marco, Waschke, Jens, and Schlegel, Nicolas

Subjects
Dextrans, Keratin, Gastrointestinal diseases, Inflammation, House mouse, Colitis, Sulfates, Polysaccharides
Abstract

Introduction Inflammatory bowel disease (IBD), encompassing Crohn's disease (CD) and ulcerative colitis (UC), is caused by a complex interplay between environmental factors, the composition of gut microbiota, and an inappropriate [...], Impaired intestinal epithelial barrier (IEB) function with loss of desmosomal junctional protein desmoglein 2 (DSG2) is a hallmark in the pathogenesis of inflammatory bowel disease (IBD). While previous studies have reported that glial cell line-derived neurotrophic factor (GDNF) promotes IEB function, the mechanisms are poorly understood. We hypothesized that GDNF is involved in the loss of DSG2, resulting in impaired IEB function as seen in IBD. In the inflamed intestine of patients with IBD, there was a decrease in GDNF concentrations accompanied by a loss of DSG2, changes of the intermediate filament system, and increased phosphorylation of p38 MAPK and cytokeratins. DSG2-deficient and RET-deficient Caco2 cells revealed that GDNF specifically recruits DSG2 to the cell borders, resulting in increased DSG2-mediated intercellular adhesion via the RET receptor. Challenge of Caco2 cells and enteroids with proinflammatory cytokines as well as dextran sulfate sodium-induced (DSS-induced) colitis in C57Bl/6 mice led to impaired IEB function with reduced DSG2 mediated by p38 MAPK-dependent phosphorylation of cytokeratins. GDNF blocked all inflammation-induced changes in the IEB. GDNF attenuates inflammation-induced impairment of IEB function caused by the loss of DSG2 through p38 MAPK-dependent phosphorylation of cytokeratin. The reduced GDNF in patients with IBD indicates a disease-relevant contribution to the development of IEB dysfunction.

Published
2019
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6. Class Project: Effects of security priming on working memory

Author

Tesher Zafrin, Ma, Choi, Hernandez, Karen, Abraham, Heidi Cielo, Emmanouil, Tatiana Aloi, Kasindorf, Jack, Burkard, Natalie, Hendricks, Derek, Yip, Justin, Ruchshona Ilkhomova, Marielis Nunez, Wong, Christopher, Hamacher, Katja, and Zambrano, Angelina

Subjects
security priming, Social and Behavioral Sciences, working memory
Abstract

Though there is strong evidence to suggest that security priming has been shown to improve the perception of tonal thresholds, the effect has been less thoroughly investigated with regards to memory. Therefore, we will measure working memory via an OSPAN test to determine if the effect exists in working memory.

Published
2023
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8. Plakophilin 2 regulates intestinal barrier function by modulating protein kinase C activity in vitro.

Author

Nagler, Simon, Ghoreishi, Yalda, Kollmann, Catherine, Kelm, Matthias, Gerull, Brenda, Waschke, Jens, Burkard, Natalie, and Schlegel, Nicolas

Subjects
PROTEIN kinase C, INTESTINES, CELL adhesion, TIGHT junctions, DESMOSOMES
Abstract

Previous data provided evidence for a critical role of desmosomes to stabilize intestinal epithelial barrier (IEB) function. These studies suggest that desmosomes not only contribute to intercellular adhesion but also play a role as signaling hubs. The contribution of desmosomal plaque proteins plakophilins (PKP) in the intestinal epithelium remains unexplored. The intestinal expression of PKP2 and PKP3 was verified in human gut specimens, human intestinal organoids as well as in Caco2 cells whereas PKP1 was not detected. Knock-down of PKP2 using siRNA in Caco2 cells resulted in loss of intercellular adhesion and attenuated epithelial barrier. This was paralleled by changes of the whole desmosomal complex, including loss of desmoglein2, desmocollin2, plakoglobin and desmoplakin. In addition, tight junction proteins claudin1 and claudin4 were reduced following the loss of PKP2. Interestingly, siRNA-induced loss of PKP3 did not change intercellular adhesion and barrier function in Caco2 cells, while siRNA-induced loss of both PKP2 and PKP3 augmented the changes observed for reduced PKP2 alone. Moreover, loss of PKP2 and PKP2/3, but not PKP3, resulted in reduced activity levels of protein kinase C (PKC). Restoration of PKC activity using Phorbol 12-myristate 13-acetate (PMA) rescued loss of intestinal barrier function and attenuated the reduced expression patterns of claudin1 and claudin4. Immunostaining, proximity ligation assays and co-immunoprecipitation revealed a direct interaction between PKP2 and PKC. In summary, our in vitro data suggest that PKP2 plays a critical role for intestinal barrier function by providing a signaling hub for PKC-mediated expression of tight junction proteins claudin1 and claudin4. [ABSTRACT FROM AUTHOR]

Published
2023
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17. Desmoglein2 Regulates Claudin2 Expression by Sequestering PI-3-Kinase in Intestinal Epithelial Cells

Author

Burkard, Natalie, Meir, Michael, Kannapin, Felix, Otto, Christoph, Petzke, Maximilian, Germer, Christoph-Thomas, Waschke, Jens, and Schlegel, Nicolas

Subjects
Male, Cell Membrane Permeability, tight junction, Immunology, Tight Junctions, Dsg2, Mice, Phosphatidylinositol 3-Kinases, inflammatory bowel disease, Animals, Humans, Claudin-2, ddc:610, Intestinal Mucosa, Original Research, Desmoglein 2, PI-3-kinase, Claudin2, RC581-607, Colitis, Mice, Inbred C57BL, intestinal barrier, Gene Expression Regulation, inflammation, desmosome, Immunologic diseases. Allergy, Caco-2 Cells
Abstract

Inflammation-induced reduction of intestinal desmosomal cadherin Desmoglein 2 (Dsg2) is linked to changes of tight junctions (TJ) leading to impaired intestinal epithelial barrier (IEB) function by undefined mechanisms. We characterized the interplay between loss of Dsg2 and upregulation of pore-forming TJ protein Claudin2. Intraperitoneal application of Dsg2-stablising Tandem peptide (TP) attenuated impaired IEB function, reduction of Dsg2 and increased Claudin2 in DSS-induced colitis in C57Bl/6 mice. TP blocked loss of Dsg2-mediated adhesion and upregulation of Claudin2 in Caco2 cells challenged with TNFα. In Dsg2-deficient Caco2 cells basal expression of Claudin2 was increased which was paralleled by reduced transepithelial electrical resistance and by augmented phosphorylation of AKT\(^{Ser473}\) under basal conditions. Inhibition of phosphoinositid-3-kinase proved that PI-3-kinase/AKT-signaling is critical to upregulate Claudin2. In immunostaining PI-3-kinase dissociated from Dsg2 under inflammatory conditions. Immunoprecipitations and proximity ligation assays confirmed a direct interaction of Dsg2 and PI-3-kinase which was abrogated following TNFα application. In summary, Dsg2 regulates Claudin2 expression by sequestering PI-3-kinase to the cell borders in intestinal epithelium.

Published
2021

19. Intestinal Epithelial Barrier Maturation by Enteric Glial Cells Is GDNF-Dependent

Author

Meir, Michael, primary, Kannapin, Felix, additional, Diefenbacher, Markus, additional, Ghoreishi, Yalda, additional, Kollmann, Catherine, additional, Flemming, Sven, additional, Germer, Christoph-Thomas, additional, Waschke, Jens, additional, Leven, Patrick, additional, Schneider, Reiner, additional, Wehner, Sven, additional, Burkard, Natalie, additional, and Schlegel, Nicolas, additional

Published
2021
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21. Enteroids Generated from Patients with Severe Inflammation in Crohn’s Disease Maintain Alterations of Junctional Proteins

Author

Meir, Michael, primary, Salm, Jonas, additional, Fey, Christina, additional, Schweinlin, Matthias, additional, Kollmann, Catherine, additional, Kannapin, Felix, additional, Germer, Christoph-Thomas, additional, Waschke, Jens, additional, Beck, Christopher, additional, Burkard, Natalie, additional, Metzger, Marco, additional, and Schlegel, Nicolas, additional

Published
2020
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32. Soluble VE‐cadherin contributes to loss of VE‐cadherin‐mediated adhesion and endothelial barrier function

Author

Flemming, Sven, primary, Burkard, Natalie, additional, Renschler, Melanie, additional, Vielmuth, Franziska, additional, Meir, Michael, additional, Schick, Martin, additional, Wunder, Christian, additional, Germer, Christop‐Thomas, additional, Spindler, Volker, additional, Waschke, Jens, additional, and Schegel, Nicolas, additional

Published
2016
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34. Konditionale Überexpression der neuronalen NO-Synthase wirkt kardioprotektiv bei Ischämie-Reperfusion

Author

Burkard, Natalie

Subjects
Signaltransduktion, ddc:500, Prävention, Herzhypertrophie
Abstract

Zusammenfassung: Wie früher schon gezeigt, wird der L-Typ Ca2+-Kanal durch eine induzierbare, myokardspezifische Überexpression der neuronalen Stickstoffmonoxidsynthase (nNOS) inhibiert. Gleichzeitig bewirkt diese Überexpression eine verminderte kardiale Kontraktilität1 (Burkard N. et al. (2007). Circ Res 100, 32-44). nNOS interagiert mit vielen verschiedenen Kompartimenten und Kanälen innerhalb der Zelle. In dieser Arbeit wurde gezeigt, dass eine nNOS Überexpression nach Ischämie-Reperfusion kardioprotektiv wirkt. Dieses wird durch eine Inhibition der Mitochondrienfunktion und durch eine Verminderung der reaktiven Sauerstoffspezies (ROS) ermöglicht. In einer früheren Arbeit wurde der Effekt der induzierbaren und myokardspezifischen Überexpression von nNOS unter physiologischen Bedingungen am transgenen Tiermodell untersucht. Diese Arbeit beschäftigt sich nun mit der Überexpression von nNOS unter pathophysiologischen (Ischämie-Reperfusion) Bedingungen. Ein Ischämie-Reperfusions-Schaden bewirkt bei Wildtyp-Mäusen, sowie bei transgener nNOS Überexpression eine Anreicherung von nNOS in den Mitochondrien. Elektronenmikroskopische Aufnahmen von Mausmyokard haben gezeigt, dass bei Überexpression nNOS zusätzlich in den Mitochondrien lokalisiert ist. Diese Translokation von nNOS in die Mitochondrien ist abhängig von HSP90. Ischämie- Reperfusionsexperimente an isolierten Mäuseherzen zeigten einen kardioprotektiven Effekt der nNOS Überexpression (30min post ischemia, LVDP 27.0±2.5mmHg vs. 45.2±1.9mmHg, n=12, p, Summary: I previously demonstrated that conditional overexpression of the neuronal nitric oxide synthase (nNOS) inhibited L-type Ca2+-channels and decreased myocardial contractility1 (Burkard N. et al. (2007). Circ Res 100, 32-44). However, nNOS has multiple targets within the cardiac myocyte and it is possible that interesting biological functions of this protein remain to be elucidated. In this study, I showed that nNOS overexpression has a cardioprotective effect after ischemia-reperfusion injury by inhibiting mitochondrial function and reducing the generation of reactive oxygen species (ROS). The effect of conditional nNOS overexpression in cardiac myocytes in ischemiareperfusion injury was assessed. Ischemia-reperfusion injury in WT mice resulted in nNOS accumulation in the mitochondria. Similary, transgenic nNOS overexpression caused nNOS abundance in mitochondria. Electron microscopy of mouse myocardium from nNOS overexpressing mice showed that after induction of its expression, nNOS is additionally localised in mitochondria. nNOS translocation into mitochondria was dependent on HSP90. Ischemia-reperfusion experiments in isolated hearts showed a cardioprotective effect of nNOS overexpression (30min post-ischemia, LVDP 27.0±2.5mmHg in non-induced animals vs. 45.2±1.9mmHg in nNOS overexpressing mice, n=12, p

Published
2010

35. A molecular mechanism improving the contractile state in human myocardial hypertrophy

Author

Ritter, Oliver, Bottez, Nico, Burkard, Natalie, Schulte, Hagen D., and Neyses, Ludwig

Subjects
Myosin light chains, cardiovascular system, Myocardial hypertrophy, Cardiovascular & respiratory systems [D03] [Human health sciences], Clinical Cardiology, Systèmes cardiovasculaire & respiratoire [D03] [Sciences de la santé humaine]
Abstract

BACKGROUND: Various molecular mechanisms are operative in altering the sarcomeric function of the heart under increased hemodynamic workload. Expression of the atrial isoform (ALC-1) of the essential myosin light chain, a shift from alpha-myosin heavy chain (MHC) to beta-MHC, increased phosphorylation of the regulatory myosin light chains and increased troponin I (TnI) phosphorylation have been reported to modulate cardiac contractility in rodents. METHODS: TO ASSESS A POSSIBLE CONTRIBUTION OF THESE SARCOMERIC PROTEINS TO CARDIAC PERFORMANCE IN HUMAN MYOCARDIAL HYPERTROPHY, TWO DIFFERENT FORMS OF CARDIAC HYPERTROPHY WERE INVESTIGATED: 19 patients with hypertropic obstructive cardiomyopathy (HOCM) and 13 patients with aortic stenosis (AS) with marked left ventricular hypertrophy and normal systolic function. RESULTS: There was no change in MHC gene expression, regulatory myosin light chain or TnI phosphorylation status in normal heart (NH), HOCM and AS patients. However, patients with hypertrophied myocardium expressed ALC-1 that was not detectable in NH. ALC-1 protein expression correlated positively with the left ventricular ejection fraction. In patients with hypertrophied myocardium, there was a mean ALC-1 protein expression of 12.7+/-3% (range 3.6% to 32%). CONCLUSION: In humans, ALC-1 expression is in vivo a powerful molecular mechanism of the sarcomere to maintain or improve myocardial contractility under increased hemodynamic demands.

Published
2002

36. Conditional neuronal nitric oxide synthase overexpression impairs myocardial contractility.

Author

Burkard, Natalie, Rokita, Adam G., Kaufmann, Susann G., Hallhuber, Matthias, Wu, Rongxue, Hu, Kai, Hofmann, Ulrich, Bonz, Andreas, Frantz, Stefan, Cartwright, Elizabeth J., Neyses, Ludwig, Maier, Lars S., Maier, Sebastian K. G., Renne, Thomas, Schuh, Kai, Ritter, Oliver, Burkard, Natalie, Rokita, Adam G., Kaufmann, Susann G., Hallhuber, Matthias, Wu, Rongxue, Hu, Kai, Hofmann, Ulrich, Bonz, Andreas, Frantz, Stefan, Cartwright, Elizabeth J., Neyses, Ludwig, Maier, Lars S., Maier, Sebastian K. G., Renne, Thomas, Schuh, Kai, and Ritter, Oliver

Abstract

The role of the neuronal NO synthase (nNOS or NOS1) enzyme in the control of cardiac function still remains unclear. Results from nNOS(-/-) mice or from pharmacological inhibition of nNOS are contradictory and do not pay tribute to the fact that probably spatial confinement of the nNOS enzyme is of major importance. We hypothesize that the close proximity of nNOS and certain effector molecules like L-type Ca(2+)-channels has an impact on myocardial contractility. To test this, we generated a new transgenic mouse model allowing conditional, myocardial specific nNOS overexpression. Western blot analysis of transgenic nNOS overexpression showed a 6-fold increase in nNOS protein expression compared with noninduced littermates (n=12; P<0.01). Measuring of total NOS activity by conversion of [(3)H]-l-arginine to [(3)H]-l-citrulline showed a 30% increase in nNOS overexpressing mice (n=18; P<0.05). After a 2 week induction, nNOS overexpression mice showed reduced myocardial contractility. In vivo examinations of the nNOS overexpressing mice revealed a 17+/-3% decrease of +dp/dt(max) compared with noninduced mice (P<0.05). Likewise, ejection fraction was reduced significantly (42% versus 65%; n=15; P<0.05). Interestingly, coimmunoprecipitation experiments indicated interaction of nNOS with SR Ca(2+)ATPase and additionally with L-type Ca(2+)- channels in nNOS overexpressing animals. Accordingly, in adult isolated cardiac myocytes, I(Ca,L) density was significantly decreased in the nNOS overexpressing cells. Intracellular Ca(2+)-transients and fractional shortening in cardiomyocytes were also clearly impaired in nNOS overexpressing mice versus noninduced littermates. In conclusion, conditional myocardial specific overexpression of nNOS in a transgenic animal model reduced myocardial contractility. We suggest that nNOS might suppress the function of L-type Ca(2+)-channels and in turn reduces Ca(2+)-transients which accounts for the negative inotropic effect.

Published
2007

37. Inhibition of nuclear import of calcineurin prevents myocardial hypertrophy.

Author

Hallhuber, Matthias, Burkard, Natalie, Wu, Rongxue, Buch, Mamta H., Engelhardt, Stefan, Hein, Lutz, Neyses, Ludwig, Schuh, Kai, Ritter, Oliver, Hallhuber, Matthias, Burkard, Natalie, Wu, Rongxue, Buch, Mamta H., Engelhardt, Stefan, Hein, Lutz, Neyses, Ludwig, Schuh, Kai, and Ritter, Oliver

Abstract

The time that transcription factors remain nuclear is a major determinant for transcriptional activity. It has recently been demonstrated that the phosphatase calcineurin is translocated to the nucleus with the transcription factor nuclear factor of activated T cells (NF-AT). This study identifies a nuclear localization sequence (NLS) and a nuclear export signal (NES) in the sequence of calcineurin. Furthermore we identified the nuclear cargo protein importinbeta(1) to be responsible for nuclear translocation of calcineurin. Inhibition of the calcineurin/importin interaction by a competitive peptide (KQECKIKYSERV), which mimicked the calcineurin NLS, prevented nuclear entry of calcineurin. A noninhibitory control peptide did not interfere with the calcineurin/importin binding. Using this approach, we were able to prevent the development of myocardial hypertrophy. In angiotensin II-stimulated cardiomyocytes, [(3)H]-leucine incorporation (159%+/-9 versus 111%+/-11; P<0.01) and cell size were suppressed significantly by the NLS peptide compared with a control peptide. The NLS peptide inhibited calcineurin/NF-AT transcriptional activity (227%+/-11 versus 133%+/-8; P<0.01), whereas calcineurin phosphatase activity was unaffected (298%+/-9 versus 270%+/-11; P=NS). We conclude that calcineurin is not only capable of dephosphorylating NF-AT, thus enabling its nuclear import, but the presence of calcineurin in the nucleus is also important for full NF-AT transcriptional activity.

Published
2006

38. Targeted proteolysis sustains calcineurin activation.

Author

Burkard, Natalie, Becher, Jan, Heindl, Cornelia, Neyses, Ludwig, Schuh, Kai, Ritter, Oliver, Burkard, Natalie, Becher, Jan, Heindl, Cornelia, Neyses, Ludwig, Schuh, Kai, and Ritter, Oliver

Abstract

BACKGROUND: Calcineurin (CnA) is important in the regulation of myocardial hypertrophy. We demonstrated that targeted proteolysis of the CnA autoinhibitory domain under pathological myocardial workload leads to increased CnA activity in human myocardium. Here, we investigated the proteolytic mechanism leading to activation of CnA. METHODS AND RESULTS: In patients with diseased myocardium, we found strong nuclear translocation of CnA. In contrast, in normal human myocardium, there was a cytosolic distribution of CnA. Stimulation of rat cardiomyocytes with angiotensin (Ang) II increased calpain activity significantly (433+/-11%; P<0.01; n=6) and caused proteolysis of the autoinhibitory domain of CnA. Inhibition of calpain by a membrane-permeable calpain inhibitor prevented proteolysis. We identified the cleavage site of calpain in the human CnA sequence at amino acid 424. CnA activity was increased after Ang II stimulation (310+/-29%; P<0.01; n=6) and remained high after removal of Ang II (214+/-17%; P<0.01; n=6). Addition of a calpain inhibitor to the medium decreased CnA activity (110+/-19%; P=NS; n=6) after removal of Ang II. Ang II stimulation of cardiomyocytes also translocated CnA into the nucleus as demonstrated by immunohistochemical staining and transfection assays with GFP-tagged CnA. Calpain inhibition and therefore suppression of calpain-mediated proteolysis of CnA enabled CnA exit from the nucleus. CONCLUSIONS: Ang II stimulation of cardiomyocytes increased calpain activity, leading to proteolysis of the autoinhibitory domain of CnA. This causes an increase in CnA activity and results in nuclear translocation of CnA. Loss of the autoinhibitory domain renders CnA constitutively nuclear and active, even after removal of the hypertrophic stimulus.

Published
2005

40. Feasibility of Contrast-Enhanced and Nonenhanced MRI for Intraprocedural and Postprocedural Lesion Visualization in Interventional Electrophysiology

Author

Nordbeck, Peter, primary, Hiller, Karl-Heinz, additional, Fidler, Florian, additional, Warmuth, Marcus, additional, Burkard, Natalie, additional, Nahrendorf, Matthias, additional, Jakob, Peter M., additional, Quick, Harald H., additional, Ertl, Georg, additional, Bauer, Wolfgang R., additional, and Ritter, Oliver, additional

Published
2011
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42. AT2 receptor activation regulates myocardial eNOS expression via the calcineurin-NF-AT pathway.

Author

Ritter, Oliver, Schuh, Kai, Brede, Marc, Rothlein, Nicola, Burkard, Natalie, Hein, Lutz, Neyses, Ludwig, Ritter, Oliver, Schuh, Kai, Brede, Marc, Rothlein, Nicola, Burkard, Natalie, Hein, Lutz, and Neyses, Ludwig

Abstract

The role of AT2-receptors has recently been subject of considerable debate. We investigated the influence of AT2-stimulation/inhibition on myocardial endothelial NO-synthase (eNOS, NOS-III) promoter activity and eNOS protein expression. Stimulation of rat cardiomyocytes with angiotensin II (AngII) increased eNOS protein expression 3.3-fold. This was blocked by Cyclosporin A (CsA). Inhibition of the AT1-receptor did not reduce AngII-mediated eNOS protein expression, whereas AT2 stimulation increased it 2.4-fold and AT2 inhibition suppressed it. The modulatory effects of the AT2-receptor on eNOS expression was confirmed in mice with a genetic deletion of the AT2-receptor (AT2-KO). In gel shift assays two putative NF-AT sites in a 1.6 kb eNOS promoter fragment showed NF-AT binding and a supershift by NF-AT2(-c1)-specific antibodies. Stimulation of transfected cells with AngII or specific AT2-receptor agonists resulted in a significant increase in eNOS promoter activity, which was blocked by CsA, MCIP1, and mutation of an upstream NF-AT site. CONCLUSION: 1) AngII-stimulation of the myocardium, both in vivo and in vitro, is accompanied by increased expression of eNOS. 2) This effect is mediated by the calcineurin pathway and is induced by the AT2-receptor. 3) These results define a calcineurin/NF-AT/eNOS pathway as downstream effector of AT2-receptor activation in the myocardium.

Published
2003

43. Conditional Overexpression of Neuronal Nitric Oxide Synthase Is Cardioprotective in Ischemia/Reperfusion

Author

Burkard, Natalie, primary, Williams, Tatjana, additional, Czolbe, Martin, additional, Blömer, Nadja, additional, Panther, Franziska, additional, Link, Martin, additional, Fraccarollo, Daniela, additional, Widder, Julian D., additional, Hu, Kai, additional, Han, Hong, additional, Hofmann, Ulrich, additional, Frantz, Stefan, additional, Nordbeck, Peter, additional, Bulla, Jan, additional, Schuh, Kai, additional, and Ritter, Oliver, additional

Published
2010
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44. Impact of imaging landmark on the risk of MRI-related heating near implanted medical devices like cardiac pacemaker leads

Author

Nordbeck, Peter, primary, Ritter, Oliver, additional, Weiss, Ingo, additional, Warmuth, Marcus, additional, Gensler, Daniel, additional, Burkard, Natalie, additional, Herold, Volker, additional, Jakob, Peter M., additional, Ertl, Georg, additional, Ladd, Mark E., additional, Quick, Harald H., additional, and Bauer, Wolfgang R., additional

Published
2010
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47. Conditional Neuronal Nitric Oxide Synthase Overexpression Impairs Myocardial Contractility

Author

Burkard, Natalie, primary, Rokita, Adam G., additional, Kaufmann, Susann G., additional, Hallhuber, Matthias, additional, Wu, Rongxue, additional, Hu, Kai, additional, Hofmann, Ulrich, additional, Bonz, Andreas, additional, Frantz, Stefan, additional, Cartwright, Elizabeth J., additional, Neyses, Ludwig, additional, Maier, Lars S., additional, Maier, Sebastian K.G., additional, Renné, Thomas, additional, Schuh, Kai, additional, and Ritter, Oliver, additional

Published
2007
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