Katschinski, Dörthe Magdalena

[["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.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.journal","Journal of Cellular Physiology"],["dc.contributor.author","Bapst, Andreas M."],["dc.contributor.author","Knöpfel, Thomas"],["dc.contributor.author","Nolan, Karen A."],["dc.contributor.author","Imeri, Faik"],["dc.contributor.author","Schuh, Claus D."],["dc.contributor.author","Hall, Andrew M."],["dc.contributor.author","Guo, Jia"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Wenger, Roland H."],["dc.date.accessioned","2022-02-01T10:31:10Z"],["dc.date.available","2022-02-01T10:31:10Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1002/jcp.30677"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98796"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation.eissn","1097-4652"],["dc.relation.issn","0021-9541"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Neurogenic and pericytic plasticity of conditionally immortalized cells derived from renal erythropoietin‐producing cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3886"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Current Pharmaceutical Design"],["dc.bibliographiccitation.lastpage","3894"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T11:22:30Z"],["dc.date.available","2018-11-07T11:22:30Z"],["dc.date.issued","2009"],["dc.description.abstract","Protein stability of hypoxia-inducible factor (HIF) alpha subunits is regulated by the oxygen-sensing prolyl-4-hydroxylase domain (PHD) enzymes. Under oxygen-limited conditions, HIF alpha subunits are stabilized and form active HIF transcription factors that induce a large number of genes involved in adaptation to hypoxic conditions with physiological implications for erythropoiesis, angiogenesis, cardiovascular function and cellular metabolism. Oxygen-sensing is regulated by the co-substrate-dependent activity and hypoxia-inducible abundance of the PHD enzymes which trigger HIF alpha stability even under low oxygen conditions. Because HIF alpha itself is notoriously reluctant to the development of antagonists, an increase in PHD activity would offer an interesting alternative to the development of drugs that interfere specifically with the HIF signalling pathway. Interestingly, among the recently discovered PHD interacting proteins were not only novel downstream targets but also upstream regulators of PHDs. Their PHD isoform-specific interaction offers the possibility to target distinct PHD isoforms and their non-identical downstream signalling pathways. This review summarizes our current knowledge on PHD interacting proteins, including upstream regulators, chaperonins, scaffolding proteins, and novel downstream transcription factors."],["dc.identifier.isi","000271385300008"],["dc.identifier.pmid","19671040"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56007"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Bentham Science Publ Ltd"],["dc.relation.issn","1381-6128"],["dc.title","HIF Prolyl-4-hydroxylase Interacting Proteins: Consequences for Drug Targeting"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3731"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","3738"],["dc.bibliographiccitation.volume","580"],["dc.contributor.author","Haegele, Sonja"],["dc.contributor.author","Behnam, Babak"],["dc.contributor.author","Borter, Emanuela"],["dc.contributor.author","Wolfe, Jonathan"],["dc.contributor.author","Paasch, Uwe"],["dc.contributor.author","Lukashev, Dmitriy"],["dc.contributor.author","Sitkovsky, Michail"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T09:40:28Z"],["dc.date.available","2018-11-07T09:40:28Z"],["dc.date.issued","2006"],["dc.description.abstract","The hypoxia-inducible factor (HIF)-1 is a transcriptional regulator of genes involved in oxygen homeostasis. We previously described testis-specific isoforms of HIF-1 alpha (mHIF-1 alpha I.1 and hHIF-1 alpha Te). Using mHIF-1 alpha exon I.1 knock-out mice we confirmed the specific expression of mHIF-1 alpha I.1 in the sperm tail. A protein-protein interaction between HIF-1 alpha and the testis specific gene antigen 10 (TSGA10) was identified by yeast two-hybrid screening. TSGA10 is expressed in testis but also in other organs and malignant tissues. Immunofluorescence analysis indicated that the C-terminal part of TSGA10 accumulates in the midpiece of spermatozoa, where it co-localizes with HIF-1 alpha. HIF-1 alpha nuclear localization and HIF-1 transcriptional activity were significantly affected by overexpressed TSGA10. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.febslet.2006.05.058"],["dc.identifier.isi","000238691600025"],["dc.identifier.pmid","16777103"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33513"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0014-5793"],["dc.title","TSGA10 prevents nuclear localization of the hypoxia-inducible factor (HIF)-1 alpha"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1343"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","1358"],["dc.bibliographiccitation.volume","471"],["dc.contributor.author","Fandrey, Joachim"],["dc.contributor.author","Schödel, Johannes"],["dc.contributor.author","Eckardt, Kai-Uwe"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Wenger, Roland H."],["dc.date.accessioned","2020-12-10T14:10:36Z"],["dc.date.available","2020-12-10T14:10:36Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00424-019-02334-8"],["dc.identifier.eissn","1432-2013"],["dc.identifier.issn","0031-6768"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70811"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Now a Nobel gas: oxygen"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.issue","1-4"],["dc.bibliographiccitation.journal","Cellular Physiology and Biochemistry"],["dc.bibliographiccitation.lastpage","240"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Eckhardt, Katrin"],["dc.contributor.author","Troeger, Juliane"],["dc.contributor.author","Reissmann, Jana"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Wagner, Klaus F."],["dc.contributor.author","Stengel, Petra"],["dc.contributor.author","Paasch, Uwe"],["dc.contributor.author","Hunziker, Peter"],["dc.contributor.author","Borter, Emanuela"],["dc.contributor.author","Barth, Sandra"],["dc.contributor.author","Schlaefli, Philipp"],["dc.contributor.author","Spielmann, Patrick"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Wenger, Roland H."],["dc.date.accessioned","2018-11-07T11:06:11Z"],["dc.date.available","2018-11-07T11:06:11Z"],["dc.date.issued","2007"],["dc.description.abstract","PASKIN links energy flux and protein synthesis in yeast, regulates glycogen synthesis in mammals, and has been implicated in glucose-stimulated insulin production in pancreatic beta-cells. Using newly generated monoclonal antibodies, PASKIN was localized in the nuclei of human testis germ cells and in the midpiece of human sperm tails. A speckle-like nuclear pattern was observed for endogenous PASKIN in HeLa cells in addition to its cytoplasmic localization. By yeast two-hybrid screening, we identified the multifunctional eukaryotic translation elongation factor eEF1A1 as a novel interaction partner of PASKIN. This interaction was mapped to the PAS A and kinase domains of PASKIN and to the C-terminus of eEF1A1 using mammalian two-hybrid and GST pull-down assays. Kinase assays, mass spectrometry and site-directed mutagenesis revealed PASKIN auto-phosphorylation as well as eEF1A1 target phosphorylation mainly but not exclusively at Thr432. Wild-type but not kinase-inactive PASKIN increased the in vitro translation of a reporter cRNA. Whereas eEF1A1 did not localize to the nucleus, it co-localizes with PASKIN to the cytoplasm of HeLa cells. The two proteins also showed a remarkably similar localization in the midpiece of the sperm tail. These data suggest regulation of eEF1A1 by PASKIN-dependent phosphorylation in somatic as well as in sperm cells. Copyright (c) 2007 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000104169"],["dc.identifier.isi","000247527600021"],["dc.identifier.pmid","17595531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52246"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1015-8987"],["dc.title","Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","43"],["dc.bibliographiccitation.lastpage","60"],["dc.bibliographiccitation.seriesnr","435"],["dc.contributor.author","Wirthner, Renato"],["dc.contributor.author","Balamurugan, Kuppusamy"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Barth, Sandra"],["dc.contributor.author","Spielmann, Patrick"],["dc.contributor.author","Oehme, Felix"],["dc.contributor.author","Flarnme, Ingo"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Camenisch, Gieri"],["dc.date.accessioned","2018-11-07T11:07:19Z"],["dc.date.available","2018-11-07T11:07:19Z"],["dc.date.issued","2007"],["dc.description.abstract","The prolyl-4-hydroxylase domain (PHD) oxygen sensor proteins hydroxylate hypoxia-inclucible transcription factor (HIF)-alpha (alpha) subunits, leading to their subsequent ubiquitinylation and degradation. Since oxygen is a necessary cosubstrate, a reduction in oxygen availability (hypoxia) decreases PHD activity and, subsequently, HIF-alpha hydroxytation. Non-hydroxylated HIF-alpha cannot be bound by the ubiquitin ligase von Hippel-Lindau tumor suppressor protein (pVHL), and HIF-alpha proteins thus become stabilized. HIF-alpha then heterodimerizes with HIF-beta (beta) to form the functionally active HIF transcription factor complex, which targets approximately 200 genes involved in adaptation to hypoxia. The three HIF-alpha PHDs are of a different nature compared with the prototype collagen prolyl-4-hydroxylase, which hydroxylates a mass protein rather than a rare transcription factor. Thus, novel assays had to be developed to express and purify functionally active PHDs and to measure PHD activity in vitro. A need also exists for such assays to functionally distinguish the three different PHDs in terms of substrate specificity and drug function. We provide a detailed description of the expression and purification of the PHDs as well as of an HIF-alpha-dependent and a HIF-alpha-independent PHD assay."],["dc.identifier.doi","10.1016/S0076-6879(07)35003-9"],["dc.identifier.isi","000251162300003"],["dc.identifier.pmid","17998048"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52530"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Academic Press Inc"],["dc.publisher.place","San diego"],["dc.relation.crisseries","Methods in Enzymology"],["dc.relation.isbn","978-0-12-373970-4"],["dc.relation.ispartof","OXYGEN BIOLOGY AND HYPOXIA"],["dc.relation.ispartofseries","Methods in Enzymology; 435"],["dc.relation.issn","0076-6879"],["dc.title","Determination and modulation of prolyl-4-hydroxylase domain oxygen sensor activity"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","284"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Oncogene"],["dc.bibliographiccitation.lastpage","289"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Ameri, K."],["dc.contributor.author","Hammond, E. M."],["dc.contributor.author","Culmsee, C."],["dc.contributor.author","Raida, M."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Wagner, Edward J."],["dc.contributor.author","Davis, Roger J."],["dc.contributor.author","Hai, T."],["dc.contributor.author","Denko, N."],["dc.contributor.author","Harris, A. L."],["dc.date.accessioned","2018-11-07T11:07:16Z"],["dc.date.available","2018-11-07T11:07:16Z"],["dc.date.issued","2007"],["dc.description.abstract","Solid tumors often have an inadequate blood supply, which results in large regions that are subjected to hypoxic or anoxic stress. Hypoxia-inducible factor-1 (HIF-1) is a transcription factor that regulates much of the transcriptional response of cells to hypoxia. Activating transcription factor 3 (ATF3) is another transcription factor that responds to a variety of stresses and is often upregulated in cancer. We investigated the regulation of ATF3 by oxygen deprivation. ATF3 induction occurred most robustly under anoxia, is common, and it is not dependent on presence of HIF-1 or p53, but is sensitive to the inhibition of c-Jun NH2-terminal kinase activation and the antioxidant N-acetylcystein. ATF3 could also be induced by desferrioxamine but not by the mitochondrial poison cyanide or the nonspecific 2-oxoglutarate dioxygenase inhibitor dimethyloxalylglycine. We also show that anoxic ATF3 mRNA is more stable than normoxic mRNA providing a mechanism for this induction. Thus, this study demonstrates that the regulation of ATF3 under anoxia is independent of 2-oxoglutarate dioxygenase, HIF-1 and p53, presumably involving multiple regulatory pathways."],["dc.description.sponsorship","NIDDK NIH HHS [DK59605]"],["dc.identifier.doi","10.1038/sj.onc.1209781"],["dc.identifier.isi","000243398300012"],["dc.identifier.pmid","16847457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52519"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0950-9232"],["dc.title","Induction of activating transcription factor 3 by anoxia is independent of p53 and the hypoxic HIF signalling pathway"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]