Zieseniß, Anke

[["dc.bibliographiccitation.firstpage","91"],["dc.bibliographiccitation.journal","Hypoxia"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Hoogewijs, David"],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Zwenger, Eveline"],["dc.contributor.author","Krull, Sabine"],["dc.date.accessioned","2020-12-10T18:43:00Z"],["dc.date.available","2020-12-10T18:43:00Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.2147/HP.S97681"],["dc.identifier.eissn","2324-1128"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78158"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Oxygen-dependent regulation of aquaporin-3 expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","jcs223230"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Leinhos, Lisa"],["dc.contributor.author","Peters, Johannes"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Helbig, Lena"],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Levay, Magdolna"],["dc.contributor.author","van Belle, Gijsbert J."],["dc.contributor.author","Ridley, Anne J."],["dc.contributor.author","Lutz, Susanne"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2020-12-10T18:41:53Z"],["dc.date.available","2020-12-10T18:41:53Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1242/jcs.223230"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77715"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Hypoxia suppresses myofibroblast differentiation by changing RhoA activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11185"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","11194"],["dc.bibliographiccitation.volume","286"],["dc.contributor.author","Hoelscher, Marion"],["dc.contributor.author","Silter, Monique"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","von Ahlen, Melanie"],["dc.contributor.author","Hesse, Amke"],["dc.contributor.author","Schwartz, Peter J."],["dc.contributor.author","Wielockx, Ben"],["dc.contributor.author","Breier, Georg"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T08:57:35Z"],["dc.date.available","2018-11-07T08:57:35Z"],["dc.date.issued","2011"],["dc.description.abstract","Prolylhydroxylase domain proteins (PHD) are cellular oxygen- sensing molecules that regulate the stability of the alpha-subunit of the transcription factor hypoxia inducible factor (HIF)-1. HIF-1 affects cardiac development as well as adaptation of the heart toward increased pressure overload or myocardial infarction. We have disrupted PHD2 in cardiomyocytes (cPhd(-/-)) using Phd2(flox/flox) mice in combination with MLCvCre mice, which resulted in HIF-1 alpha stabilization and activation of HIF target genes in the heart. Although cPhd2(-/-) mice showed no gross abnormalities in cardiac filament structure or function, we observed a significant increased cardiac capillary area in those mice. cPhd2(-/-) mice did not respond differently to increased mechanical load by transverse aortic constriction compared with their wild-type (wt) littermates. After ligation of the left anterior descending artery, however, the area at risk and area of necrosis were significantly smaller in the cPhd2(-/-) mice compared with Phd2 wt mice in line with the described pivotal role of HIF-1 alpha for tissue protection in case of myocardial infarction. This correlated with a decreased number of apoptotic cells in the infarcted myocardium in the cPhd2(-/-) mice and significantly improved cardiac function 3 weeks after myocardial infarction."],["dc.identifier.doi","10.1074/jbc.M110.186809"],["dc.identifier.isi","000288797100029"],["dc.identifier.pmid","21270129"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23434"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Cardiomyocyte-specific Prolyl-4-hydroxylase Domain 2 Knock Out Protects from Acute Myocardial Ischemic Injury"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","213"],["dc.contributor.author","Helbig, L."],["dc.contributor.author","Peters, J."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T09:59:52Z"],["dc.date.available","2018-11-07T09:59:52Z"],["dc.date.issued","2015"],["dc.format.extent","80"],["dc.identifier.isi","000362554200172"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37685"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Remodeling of the actin cytoskeleton in hypoxia: an emerging role for ArhGAP29"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","843"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cellular Physiology and Biochemistry"],["dc.bibliographiccitation.lastpage","851"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Hesse, Amke Rena"],["dc.contributor.author","Jatho, Aline"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Hoelscher, Marion"],["dc.contributor.author","Vogel, Sabine"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:03:08Z"],["dc.date.available","2018-11-07T10:03:08Z"],["dc.date.issued","2015"],["dc.description.abstract","Aims: The prolyl-4-hydroxylase domain (PHD) enzymes are representing novel therapeutic targets for ischemic tissue protection. Whereas the consequences of a knock out of the PHDs have been analyzed in the context of cardioprotection, the implications of PHD overexpression is unknown so far. Methods and Results: We generated cardiomyocyte-specific PHD3 transgenic mice (cPhd3tg). Resting cPhd3tg mice did not show constitutive accumulation of HIF-l alpha or HIF-2 alpha or changes in HIF target gene expression in the heart. Cardiac function was followed up for 14 months in these mice and found to be unchanged. After challenging the cPhd3tg mice with ligation of the left anterior descending artery, HIF-1 alpha/-2 alpha accumulation in the left ventricles was blunted. This was associated with a significantly increased infarct size of the cPhd3tg compared to wild type mice. Conclusion: Whereas overexpression of PHD3 in the resting state does not significantly influence cardiac function, it is crucial for the cardiac response to ischemia by affecting HIF alpha accumulation in the ischemic tissue. Copyright (C) 2015 S Karger AG, Basel"],["dc.description.sponsorship","Deutsche Zentrum fur Herz Kreislaufforschung (DZHK)"],["dc.identifier.doi","10.1159/000430260"],["dc.identifier.isi","000357833400002"],["dc.identifier.pmid","26044310"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38386"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1421-9778"],["dc.relation.issn","1015-8987"],["dc.title","Cardiomyocyte-Specific Transgenic Expression of Prolyl-4-Hydroxylase Domain 3 Impairs the Myocardial Response to Ischemia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","219"],["dc.contributor.author","Ohs, A."],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T10:26:37Z"],["dc.date.available","2018-11-07T10:26:37Z"],["dc.date.issued","2017"],["dc.format.extent","54"],["dc.identifier.isi","000395770300104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43081"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Changes of nuclear actin levels in hypoxia"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e69128"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Vogel, Sabine"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Leisering, Pia"],["dc.contributor.author","Lutz, Susanne"],["dc.contributor.author","Wuertz, Christina M."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T09:22:20Z"],["dc.date.available","2018-11-07T09:22:20Z"],["dc.date.issued","2013"],["dc.description.abstract","Cells can adapt to hypoxia by various mechanisms. Yet, hypoxia-induced effects on the cytoskeleton-based cell architecture and functions are largely unknown. Here we present a comprehensive analysis of the architecture and function of L929 fibroblasts under hypoxic conditions (1% O-2). Cells cultivated in hypoxia showed striking morphological differences as compared to cells cultivated under normoxic conditions (20% O-2). These changes include an enlargement of cell area and volume, increased numbers of focal contacts and loss of cell polarization. Furthermore the beta- and gamma-actin distribution is greatly altered. These hypoxic adjustments are associated with enhanced cell spreading and a decline of cell motility in wound closure and single cell motility assays. As the hypoxia-inducible factor-1 alpha (HIF-1 alpha) is stabilised in hypoxia and plays a pivotal role in the transcriptional response to changes in oxygen availability we used an shRNA-approach to examine the role of HIF-1 alpha in cytoskeleton-related architecture and functions. We show that the observed increase in cell area, actin filament rearrangement, decrease of single cell migration in hypoxia and the maintenance of p-cofilin levels is dependent on HIF-1 alpha stabilisation."],["dc.identifier.doi","10.1371/journal.pone.0069128"],["dc.identifier.isi","000324146200061"],["dc.identifier.pmid","23874890"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9965"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29319"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Hypoxia Modulates Fibroblastic Architecture, Adhesion and Migration: A Role for HIF-1 alpha in Cofilin Regulation and Cytoplasmic Actin Distribution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","77"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cardiovascular Research"],["dc.bibliographiccitation.lastpage","86"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Hoelscher, Marion"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Hesse, Amke"],["dc.contributor.author","Silter, Monique"],["dc.contributor.author","Lin, Yun"],["dc.contributor.author","Pichler, Bernd J."],["dc.contributor.author","Thistlethwaite, Patricia"],["dc.contributor.author","El-Armouche, Ali"],["dc.contributor.author","Maier, Lars. S."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T09:11:48Z"],["dc.date.available","2018-11-07T09:11:48Z"],["dc.date.issued","2012"],["dc.description.abstract","The hypoxia-inducible factor-1 (HIF-1) is the master modulator of hypoxic gene expression. The effects of chronically stabilized cardiac HIF-1 and its role in the diseased heart are not precisely known. The aims of this study were as follows: (i)to elucidate consequences of HIF-1 stabilization in the heart; (ii)to analyse long-term effects of HIF-1 stabilization with ageing and the ability of the HIF-1 overexpressing hearts to respond to increased mechanical load; and (iii)to analyse HIF-1 protein levels in failing heart samples. In a cardiac-specific HIF-1 transgenic mouse model, constitutive expression of HIF-1 leads to changes in capillary area and shifts the cardiac metabolism towards glycolysis with a net increase in glucose uptake. Furthermore, Ca-2 handling is altered, with increased Ca-2 transients and faster intracellular [Ca-2] decline. These changes are associated with decreased expression of sarcoplasmic/endoplasmic reticulum calcium ATPase 2a but elevated phosphorylation of phospholamban. HIF-1 transgenic mice subjected to transverse aortic constriction exhibited profound cardiac decompensation. Moreover, cardiomyopathy was also seen in ageing transgenic mice. In parallel, we found an increased stabilization of HIF-1 in heart samples of patients with end-stage heart failure. Changes induced with transgenic cardiac HIF-1 possibly mediate beneficial effects in the short term; however, with increased mechanical load and ageing they become detrimental for cardiac function. Together with the finding of increased HIF-1 protein levels in samples from human patients with cardiomyopathy, these data indicate that chronic HIF-1 stabilization drives autonomous pathways that add to disease progression."],["dc.identifier.doi","10.1093/cvr/cvs014"],["dc.identifier.isi","000301983100012"],["dc.identifier.pmid","22258630"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26804"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0008-6363"],["dc.title","Unfavourable consequences of chronic cardiac HIF-1 stabilization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Peters, J."],["dc.contributor.author","Huettner, C."],["dc.contributor.author","Helbig, L."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T10:17:28Z"],["dc.date.available","2018-11-07T10:17:28Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400432"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41232"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","ArhGAP29 fine tunes RhoA activity and its downstream signaling in hypoxia"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","210"],["dc.contributor.author","Peters, J."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Vogel, S."],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2018-11-07T09:42:48Z"],["dc.date.available","2018-11-07T09:42:48Z"],["dc.date.issued","2014"],["dc.format.extent","130"],["dc.identifier.isi","000332259900335"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34038"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Remodeling of the actin cytoskeleton in hypoxia: An emerging role for ArhGAP29"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]