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.firstpage","114"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Genes & Development"],["dc.bibliographiccitation.lastpage","119"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Donlin, Laura T."],["dc.contributor.author","Andresen, Christian"],["dc.contributor.author","Just, Steffen"],["dc.contributor.author","Rudensky, Eugene"],["dc.contributor.author","Pappas, Christopher T."],["dc.contributor.author","Kruger, Martina"],["dc.contributor.author","Jacobs, Erica Y."],["dc.contributor.author","Unger, Andreas"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Dobenecker, Marc-Werner"],["dc.contributor.author","Voelkel, Tobias"],["dc.contributor.author","Chait, Brian T."],["dc.contributor.author","Gregorio, Carol C."],["dc.contributor.author","Rottbauer, Wolfgang"],["dc.contributor.author","Tarakhovsky, Alexander"],["dc.contributor.author","Linke, Wolfgang A."],["dc.date.accessioned","2018-11-07T09:14:23Z"],["dc.date.available","2018-11-07T09:14:23Z"],["dc.date.issued","2012"],["dc.description.abstract","Protein lysine methylation is one of the most widespread post-translational modifications in the nuclei of eukaryotic cells. Methylated lysines on histones and nonhistone proteins promote the formation of protein complexes that control gene expression and DNA replication and repair. In the cytoplasm, however, the role of lysine methylation in protein complex formation is not well established. Here we report that the cytoplasmic protein chaperone Hsp90 is methylated by the lysine methyltransferase Smyd2 in various cell types. In muscle, Hsp90 methylation contributes to the formation of a protein complex containing Smyd2, Hsp90, and the sarcomeric protein titin. Deficiency in Smyd2 results in the loss of Hsp90 methylation, impaired titin stability, and altered muscle function. Collectively, our data reveal a cytoplasmic protein network that employs lysine methylation for the maintenance and function of skeletal muscle."],["dc.identifier.doi","10.1101/gad.177758.111"],["dc.identifier.isi","000300157100003"],["dc.identifier.pmid","22241783"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27395"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","0890-9369"],["dc.title","Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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","79"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","80"],["dc.bibliographiccitation.volume","213"],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Hesse, Amke Rena"],["dc.contributor.author","Levent, Elif"],["dc.contributor.author","Tiburcy, Malte"],["dc.contributor.author","Heinze, Eva"],["dc.contributor.author","Burzlaff, Nicolai"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Eckardt, K. U."],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T09:59:51Z"],["dc.date.available","2018-11-07T09:59:51Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362554200170"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37684"],["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","Pre- and post-conditional inhibition of prolyl-4-hydroxylase domain enzymes protects the heart from an ischemic insult"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","noac212"],["dc.bibliographiccitation.journal","Neuro-Oncology"],["dc.contributor.author","Stejerean-Todoran, Ioana"],["dc.contributor.author","Gimotty, Phyllis A"],["dc.contributor.author","Watters, Andrea"],["dc.contributor.author","Brafford, Patricia"],["dc.contributor.author","Krepler, Clemens"],["dc.contributor.author","Godok, Tetiana"],["dc.contributor.author","Li, Haiyin"],["dc.contributor.author","Bonilla del Rio, Zuriñe"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Katschinski, Dörthe M"],["dc.contributor.author","Vultur, Adina"],["dc.date.accessioned","2022-10-04T10:21:38Z"],["dc.date.available","2022-10-04T10:21:38Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n \n Background\n Melanoma, the deadliest of skin cancers, has a high propensity to form brain metastases that are associated with a markedly worsened prognosis. In spite of recent therapeutic advances, melanoma brain lesions remain a clinical challenge, biomarkers predicting brain dissemination are not clear and differences with other metastatic sites are poorly understood.\n \n \n Methods\n We examined a genetically diverse panel of human-derived melanoma brain metastasis (MBM) and extracranial cell lines using targeted sequencing, a Reverse Phase Protein Array, protein expression analyses, and functional studies in vitro and in vivo.\n \n \n Results\n Brain-specific genetic alterations were not detected; however, MBM cells in vitro displayed lower proliferation rates and MBM-specific protein expression patterns associated with proliferation, DNA damage, adhesion, and migration. MBM lines displayed higher levels of RAC1 expression, involving a distinct RAC1-PAK1-JNK1 signaling network. RAC1 knockdown or treatment with small molecule inhibitors contributed to a less aggressive MBM phenotype in vitro, while RAC1 knockdown in vivo led to reduced tumor volumes and delayed tumor appearance. Proliferation, adhesion, and migration were higher in MBM vs. non-MBM lines in the presence of insulin or brain-derived factors and were affected by RAC1 levels.\n \n \n Conclusions\n Our findings indicate that despite their genetic variability, MBM engage specific molecular processes such as RAC1 signaling to adapt to the brain microenvironment and this can be used for the molecular characterization and treatment of brain metastases."],["dc.identifier.doi","10.1093/neuonc/noac212"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114462"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.eissn","1523-5866"],["dc.relation.issn","1522-8517"],["dc.title","A distinct pattern of growth and RAC1 signaling in melanoma brain metastasis cells"],["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.firstpage","33756"],["dc.bibliographiccitation.issue","44"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","33763"],["dc.bibliographiccitation.volume","285"],["dc.contributor.author","Vogel, Sabine"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Schnelle, Moritz"],["dc.contributor.author","Le-Huu, Sinja"],["dc.contributor.author","von Ahlen, Melanie"],["dc.contributor.author","Malz, Cordula R."],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T08:37:53Z"],["dc.date.available","2018-11-07T08:37:53Z"],["dc.date.issued","2010"],["dc.description.abstract","Cells are responding to hypoxia via prolyl-4-hydroxylase domain (PHD) enzymes, which are responsible for oxygen-dependent hydroxylation of the hypoxia-inducible factor (HIF)-1 alpha subunit. To gain further insight into PHD function, we generated knockdown cell models for the PHD2 isoform, which is the main isoform regulating HIF-1 alpha hydroxylation and thus stability in normoxia. Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining. A similar effect could be observed in the stably transfected PHD2 knockdown cell clones 1B6 and 3B7. F-actin is at least in part responsible for shaping cell morphology as well as regulating cell migration. Cell migration was impaired significantly as a consequence of PHD2 knockdown in a scratch assay. Mechanistically, PHD2 knockdown resulted in activation of the RhoA (Ras homolog gene family member A)/Rho-associated kinase pathway with subsequent phosphorylation of cofilin. Because cofilin phosphorylation impairs its actin-severing function, this may explain the F-actin phenotype, thereby providing a functional link between PHD2-dependent signaling and cell motility."],["dc.identifier.doi","10.1074/jbc.M110.132985"],["dc.identifier.isi","000283354000021"],["dc.identifier.pmid","20801873"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6193"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18648"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Prolyl Hydroxylase Domain (PHD) 2 Affects Cell Migration and F-actin Formation via RhoA/Rho-associated Kinase-dependent Cofilin Phosphorylation"],["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.firstpage","569"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","577"],["dc.bibliographiccitation.volume","459"],["dc.contributor.author","Silter, Monique"],["dc.contributor.author","Koegler, Harald"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Wilting, Joerg"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Rokita, Adam G."],["dc.contributor.author","Breves, Gerhard"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T08:45:42Z"],["dc.date.available","2018-11-07T08:45:42Z"],["dc.date.issued","2010"],["dc.description.abstract","The hypoxia-inducible factor (HIF)-1 is critically involved in the cellular adaptation to a decrease in oxygen availability. The influence of HIF-1 alpha for the development of cardiac hypertrophy and cardiac function that occurs in response to sustained pressure overload has been mainly attributed to a challenged cardiac angiogenesis and cardiac hypertrophy up to now. Hif-1 alpha (+/+) and Hif-1 alpha (+/-) mice were studied regarding left ventricular hypertrophy and cardiac function after being subjected to transverse aortic constriction (TAC). After TAC, both Hif-1 alpha (+/+) and Hif-1 alpha (+/-) mice developed left ventricular hypertrophy with increased posterior wall thickness, septum thickness and increased left ventricular weight to a similar extent. No significant difference in cardiac vessel density was observed between Hif-1 alpha (+/+) and Hif-1 alpha (+/-) mice. However, only the Hif-1 alpha (+/-) mice developed severe heart failure as revealed by a significantly reduced fractional shortening mostly due to increased end-systolic left ventricular diameter. On the single cell level this correlated with reduced myocyte shortenings, decreased intracellular Ca2+-transients and SR-Ca2+ content in myocytes of Hif-1a (+/-) mice. Thus, HIF-1 alpha can be critically involved in the preservation of cardiac function after chronic pressure overload without affecting cardiac hypertrophy. This effect is mediated via HIF-dependent modulation of cardiac calcium handling and contractility."],["dc.identifier.doi","10.1007/s00424-009-0748-x"],["dc.identifier.isi","000274904800005"],["dc.identifier.pmid","19898976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/4150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20508"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Impaired Ca2+-handling in HIF-1 alpha(+/-) mice as a consequence of pressure overload"],["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"]]