Katschinski, Dörthe Magdalena

[["dc.bibliographiccitation.firstpage","700"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Microcirculation"],["dc.bibliographiccitation.lastpage","710"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Czepluch, Frauke S."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Kuschicke, Hendrik"],["dc.contributor.author","Meier, Julia"],["dc.contributor.author","Gogiraju, Rajinikanth"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2017-09-07T11:43:27Z"],["dc.date.available","2017-09-07T11:43:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Objective: The zinc finger transcription factor KLF4 is known to control diverse EC functions. Methods: The functional role of KLF4 for angiogenesis and its association with CAD was examined in HUVECs and human CECs. Results: In two different angiogenesis assays, siRNA-mediated KLF4 downregulation impaired HUVEC sprouting and network formation. Conversely, KLF4 overexpression increased HUVEC sprouting and network formation. Similar findings were observed after incubation of HUVECs with CdM from KLF4 cDNA-transfected cells, suggesting a role of paracrine factors for mediating angiogenic KLF4 effects. In this regard, VEGF expression was increased in KLF4-overexpressing HUVECs, whereas its expression was reduced in HUVECs transfected with KLF4 siRNA. To examine the relevance of our in vitro findings for human endothelial dysfunction, we analyzed the expression of KLF4 in CECs of patients with stable CAD. Flow cytometry analyses revealed decreased numbers of KLF4-positive CECs in peripheral blood from CAD patients compared to healthy controls. Conclusions: Our findings suggest that KLF4 may represent a potential biomarker for EC dysfunction. In the future, (therapeutic) modulation of KLF4 may be useful in regulating EC function during vascular disease processes."],["dc.identifier.doi","10.1111/micc.12226"],["dc.identifier.gro","3141793"],["dc.identifier.isi","000365387200003"],["dc.identifier.pmid","26214161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1135"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1549-8719"],["dc.relation.issn","1073-9688"],["dc.title","Circulating Endothelial Cells Expressing the Angiogenic Transcription Factor Kruppel-Like Factor 4 are Decreased in Patients with Coronary Artery Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3758"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","3768"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Barth, Sandra"],["dc.contributor.author","Nesper, Jutta"],["dc.contributor.author","Hasgall, Philippe A."],["dc.contributor.author","Wirthner, Renato"],["dc.contributor.author","Nytko, Katarzyna J."],["dc.contributor.author","Edlich, Frank"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Camenisch, Gieri"],["dc.date.accessioned","2018-11-07T11:02:54Z"],["dc.date.available","2018-11-07T11:02:54Z"],["dc.date.issued","2007"],["dc.description.abstract","The heterodimeric hypoxia-inducible transcription factors (HIFs) are central regulators of the response to low oxygenation. HIF-alpha subunits are constitutively expressed but rapidly degraded under normoxic conditions. Oxygen-dependent hydroxylation of two conserved prolyl residues by prolyl-4-hydroxylase domain-containing enzymes (PHDs) targets HIF-alpha for proteasomal destruction. We identified the peptidyl prolyl cis/trans isomerase FK506-binding protein 38 (FKBP38) as a novel interactor of PHD2. Yeast two-hybrid, glutathione S-transferase pull-down, coimmunoprecipitation, colocalization, and mammalian two-hybrid studies confirmed specific FKBP38 interaction with PHD2, but not with PHD1 or PHD3. PHD2 and FKBP38 associated with their N-terminal regions, which contain no known interaction motifs. Neither FKBP38 mRNA nor protein levels were regulated under hypoxic conditions or after PHD inhibition, suggesting that FKBP38 is not a HIF/PHD target. Stable RNA interference-mediated depletion of FKBP38 resulted in increased PHD hydroxylation activity and decreased HIF protein levels and transcriptional activity. Reconstitution of FKBP38 expression abolished these effects, which were independent of the peptidyl prolyl cis/trans isomerase activity. Downregulation of FKBP38 did not affect PHD2 mRNA levels but prolonged PHD2 protein stability, suggesting that FKBP38 is involved in PHD2 protein regulation."],["dc.identifier.doi","10.1128/MCB.01324-06"],["dc.identifier.isi","000246269400018"],["dc.identifier.pmid","17353276"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51495"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","The peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability"],["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","Jatho, Aline"],["dc.contributor.author","Hartmann, S."],["dc.contributor.author","Kittana, Naim"],["dc.contributor.author","Muegge, F."],["dc.contributor.author","Wuertz, Christina"],["dc.contributor.author","Tiburcy, Malte"],["dc.contributor.author","Zimmermann, Wolfram-Hubertus"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Lutz, S."],["dc.date.accessioned","2018-11-07T10:17:27Z"],["dc.date.available","2018-11-07T10:17:27Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41230"],["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","RhoA ambivalently controls prominent myofibroblast characteristics by involving distinct signaling routes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3610"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Blood"],["dc.bibliographiccitation.lastpage","3617"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Koditz, Jens"],["dc.contributor.author","Nesper, Jutta"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Franke, Corinna"],["dc.contributor.author","Myllyharju, Johanna"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:53:15Z"],["dc.date.available","2018-11-07T10:53:15Z"],["dc.date.issued","2007"],["dc.description.abstract","The activating transcription factor-4 (ATF-4) is translationally induced under anoxic conditions, mediates part of the unfolded protein response following endoplasmic reticulum (ER) stress, and is a critical regulator of cell fate. Here, we identified the zipper 11 domain of ATF-4 to interact with the oxygen sensor prolyl-4-hydroxylase domain 3 (PHD3). The PHD inhibitors dimethyloxalylglycine (DMOG) and hypoxia, or proteasomal inhibition, all induced ATF-4 protein levels. Hypoxic induction of ATF-4 was due to increased protein stability, but was independent of the ubiquitin ligase von Hippel-Lindau protein (pVHL).,A novel oxygen-dependent degradation (ODD) domain was identified adjacent to the zipper 11 domain. Mutations of 5 prolyl residues within this ODD domain or siRNA-mediated down-regulation of PHD3, but not of PHD2, was sufficient to stabilize ATF-4 under normoxic conditions. These data demonstrate that PHD-dependent oxygen-sensing recruits both the hypoxia-inducible factor (HIF) and ATF-4 systems, and hence not only confers adaptive responses but also cell fate decisions."],["dc.identifier.doi","10.1182/blood-2007-06-094441"],["dc.identifier.isi","000250946300026"],["dc.identifier.pmid","17684156"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49312"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Hematology"],["dc.relation.issn","0006-4971"],["dc.title","Oxygen-dependent ATF-4 stability is mediated by the PHD3 oxygen sensor"],["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","407"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","414"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T08:30:49Z"],["dc.date.available","2018-11-07T08:30:49Z"],["dc.date.issued","2009"],["dc.description.abstract","The prolyl-4-hydroxylase domain (PHD) 1-3 enzymes have been identified based on their ability to regulate the stability of hypoxia-inducible factor a subunits and thus to modify hypoxia-inducible gene expression. Transgenic mouse models provided insights into the isoform-specific functions of these oxygen sensors with physiological implications for angiogenesis, erythropoiesis/oxygen transport, cardiovascular function, metabolism and tissue homeostasis. This knowledge is important for the ongoing development of small molecule PHD inhibitors that are currently tested in preclinical and clinical trials for the treatment of anaemia and for cytoprotection. This review aims at summarizing the insights obtained from key mouse knock-out models as well as first experiences in the therapeutic application of PHD inhibitors."],["dc.identifier.doi","10.1111/j.1748-1716.2008.01952.x"],["dc.identifier.isi","000263965500001"],["dc.identifier.pmid","19183336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16983"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","1748-1708"],["dc.title","In vivo functions of the prolyl-4-hydroxylase domain oxygen sensors: direct route to the treatment of anaemia and the protection of ischaemic tissues"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Annals of Oncology"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Kozlova, Nina"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Kristiansen, Glen"],["dc.contributor.author","Kietzmann, Thomas"],["dc.date.accessioned","2018-11-07T10:07:18Z"],["dc.date.available","2018-11-07T10:07:18Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1093/annonc/mdw362.27"],["dc.identifier.isi","000393912500028"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39250"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.conference","41st Congress of the European-Society-for-Medical-Oncology (ESMO)"],["dc.relation.eventlocation","Copenhagen, DENMARK"],["dc.relation.issn","1569-8041"],["dc.relation.issn","0923-7534"],["dc.title","Hypoxia inducible factor prolyl hydroxylase 2 (PHD2) is a direct regulator of epidermal growth factor receptor (EGFR) signaling in breast cancer"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","101071"],["dc.bibliographiccitation.journal","Redox Biology"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Shokhina, Arina G."],["dc.contributor.author","Kostyuk, Alexander I."],["dc.contributor.author","Ermakova, Yulia G."],["dc.contributor.author","Panova, Anastasiya S."],["dc.contributor.author","Staroverov, Dmitry B."],["dc.contributor.author","Egorov, Evgeny S."],["dc.contributor.author","Baranov, Mikhail S."],["dc.contributor.author","van Belle, Gijsbert J."],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Belousov, Vsevolod V."],["dc.contributor.author","Bilan, Dmitry S."],["dc.date.accessioned","2020-12-10T15:21:03Z"],["dc.date.available","2020-12-10T15:21:03Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.redox.2018.101071"],["dc.identifier.issn","2213-2317"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72897"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Red fluorescent redox-sensitive biosensor Grx1-roCherry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:17:29Z"],["dc.date.available","2018-11-07T10:17:29Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400056"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41236"],["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","Prolyl-4-hydroxylase domain (PHD) is a critical terminator for cell survival of macrophages under stress conditions"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]