Beneke, Angelika

[["dc.bibliographiccitation.firstpage","2048"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","2055"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Siegert, Isabel"],["dc.contributor.author","Schoedel, Johannes"],["dc.contributor.author","Nairz, Manfred"],["dc.contributor.author","Schatz, Valentin"],["dc.contributor.author","Dettmer, Katja"],["dc.contributor.author","Dick, Christopher"],["dc.contributor.author","Kalucka, Joanna"],["dc.contributor.author","Franke, Kristin"],["dc.contributor.author","Ehrenschwender, Martin"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Sutter, Joerg"],["dc.contributor.author","Moll, Matthias"],["dc.contributor.author","Hellerbrand, Claus"],["dc.contributor.author","Wielockx, Ben"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Lang, Roland"],["dc.contributor.author","Galy, Bruno"],["dc.contributor.author","Hentze, Matthias W."],["dc.contributor.author","Koivunen, Peppi"],["dc.contributor.author","Oefner, Peter J."],["dc.contributor.author","Bogdan, Christian"],["dc.contributor.author","Weiss, Guenter"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Jantsch, Jonathan"],["dc.date.accessioned","2018-11-07T09:47:29Z"],["dc.date.available","2018-11-07T09:47:29Z"],["dc.date.issued","2015"],["dc.description.abstract","Both hypoxic and inflammatory conditions activate transcription factors such as hypoxia-inducible factor (HIF)-1 alpha and nuclear factor (NF)-kappa B, which play a crucial role in adaptive responses to these challenges. In dendritic cells (DC), lipopolysaccharide (LPS)-induced HIF1 alpha accumulation requires NF-kappa B signaling and promotes inflammatory DC function. The mechanisms that drive LPS-induced HIF1 alpha accumulation under normoxia are unclear. Here, we demonstrate that LPS inhibits prolyl hydroxylase domain enzyme (PHD) activity and thereby blocks HIF1 alpha degradation. Of note, LPS-induced PHD inhibition was neither due to cosubstrate depletion (oxygen or alpha-ketoglutarate) nor due to increased levels of reactive oxygen species, fumarate, and succinate. Instead, LPS inhibited PHD activity through NF-kappa B-mediated induction of the iron storage protein ferritin and subsequent decrease of intracellular available iron, a critical cofactor of PHD. Thus, hypoxia and LPS both induce HIF1 alpha accumulation via PHD inhibition but deploy distinct molecular mechanisms (lack of cosubstrate oxygen versus deprivation of co-factor iron)."],["dc.identifier.doi","10.1016/j.celrep.2015.11.005"],["dc.identifier.isi","000366534300002"],["dc.identifier.pmid","26628374"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12739"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35125"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Ferritin-Mediated Iron Sequestration Stabilizes Hypoxia-Inducible Factor-1 alpha upon LPS Activation in the Presence of Ample Oxygen"],["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.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","365"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Leukocyte Biology"],["dc.bibliographiccitation.lastpage","375"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Hillemann, Annette"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Odagiri, Haruki"],["dc.contributor.author","Terada, Kazutoyo"],["dc.contributor.author","Endo, Motoyoshi"],["dc.contributor.author","Oike, Yuichi"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T09:36:09Z"],["dc.date.available","2018-11-07T09:36:09Z"],["dc.date.issued","2014"],["dc.description.abstract","On a molecular level, cells sense changes in oxygen availability through the PHDs, which regulate the protein stability of the alpha-subunit of the transcription factor HIF. Especially, PHD3 has been additionally associated with apoptotic cell death. We hypothesized that PHD3 plays a role in cell-fate decisions in macrophages. Therefore, myeloid-specific PHD3(-/-) mice were created and analyzed. PHD3(-/-) BMDM showed no altered HIF-1 alpha or HIF-2 alpha stabilization or increased HIF target gene expression in normoxia or hypoxia. Macrophage M1 and M2 polarization was unchanged likewise. Compared with macrophages from WT littermates, PHD3(-/-) BMDM exhibited a significant reduction in TUNEL-positive cells after serum withdrawal or treatment with stauro and SNAP. Under the same conditions, PHD3(-/-) BMDM also showed less Annexin V staining, which is representative for membrane disruption, and indicated a reduced early apoptosis. In an unbiased transcriptome screen, we found that Angptl2 expression was reduced in PHD3(-/-) BMDM under stress conditions. Addition of rAngptl2 rescued the antiapoptotic phenotype, demonstrating that it is involved in the PHD3-mediated response toward apoptotic stimuli in macrophages."],["dc.identifier.doi","10.1189/jlb.2HI1013-533R"],["dc.identifier.isi","000340829400003"],["dc.identifier.pmid","24626957"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32548"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.relation.issn","1938-3673"],["dc.relation.issn","0741-5400"],["dc.title","Prolyl-4-hydroxylase domain 3 (PHD3) is a critical terminator for cell survival of macrophages under stress conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","298"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cytogenetic and Genome Research"],["dc.bibliographiccitation.lastpage","301"],["dc.bibliographiccitation.volume","98"],["dc.contributor.author","Beneke, S."],["dc.contributor.author","Kappler, Roland"],["dc.contributor.author","Burkle, A."],["dc.contributor.author","Scherthan, H."],["dc.date.accessioned","2018-11-07T10:32:58Z"],["dc.date.available","2018-11-07T10:32:58Z"],["dc.date.issued","2002"],["dc.description.abstract","Poly(ADP-ribose) polymerase 1 (PARP-1) lies at the basis of a DNA-interacting protein family that maintains genome integrity. Here we describe the genomic organisation of rat PARP-1 gene (Adprt), refine its assignment to rat chromosome (RNO) 13q25-->q26 by FISH and compare its genomic organisation between rat, mouse and human. It appears that in human, mouse and rat Adprt consists of 23 similar-sized exons with well-conserved intron and exon borders. Adprt orthologs map to homologous chromosome regions at the termini of the q-arms of human and mouse chromosomes I and rat 13, with gene order being conserved between the rodents. Kimura protein distance comparison with human PARP-1 as reference revealed the bovine protein to be the least conserved with 10.3 substitutions per 100 amino acids, followed by rat (8.6) and mouse (8.4). Copyright (C) 2002 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000071052"],["dc.identifier.isi","000184000700013"],["dc.identifier.pmid","12826757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44486"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1424-8581"],["dc.title","Genomic structure, conservation and FISH mapping of the Rattus norvegicus Adprt gene"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1301"],["dc.bibliographiccitation.issue","2B"],["dc.bibliographiccitation.journal","Anticancer Research"],["dc.bibliographiccitation.lastpage","1305"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Meden, H."],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Hesse, T."],["dc.contributor.author","Novophashenny, I."],["dc.contributor.author","Wischnewsky, M."],["dc.date.accessioned","2018-11-07T09:17:46Z"],["dc.date.available","2018-11-07T09:17:46Z"],["dc.date.issued","2001"],["dc.description.abstract","Background: In patients with HER2-positive metastatic breast cancer (MBC), combined treatment of herceptin (H) and chemotherapy (CT) improves time to progression, response rates and survival compared with CT alone. Materials and Methods: We evaluated the safety and efficacy of weekly Docetaxel combined with weekly H as treatment in HER2 overexpressing MBC. Results: Preliminary toxicity data from 12 patients and 76 cycles of D and 80 cycles of H were analysed No G3/4 toxicity was observed. The most frequent non-hematologic toxicities were fatigue (2 patients G2, 2 patients G2), dyspepsia (1 patients G2, 3 patients G1), diarrhea (1 patient G2, 3 patients G1), and nausea (1 patient G2, 3 patients G1). Six partial responses have been observed in 12 patients (ORR 50%). Conclusions: The combination of weekly Docetaxel and Herceptin is well tolerated with significant anti-tumor activity."],["dc.identifier.isi","000169012400010"],["dc.identifier.pmid","11396203"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28248"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Int Inst Anticancer Research"],["dc.relation.issn","0250-7005"],["dc.title","Weekly intravenous recombinant humanized anti-P185(HER2) monoclonal antibody (herceptin) plus docetaxel in patients with metastatic breast cancer: A pilot study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e2976"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Cell Death & Disease"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Guentsch, Annemarie"],["dc.contributor.author","Hillemann, Annette"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.date.accessioned","2019-02-14T11:48:34Z"],["dc.date.available","2019-02-14T11:48:34Z"],["dc.date.issued","2017"],["dc.description.abstract","Macrophages are essential for the inflammatory response after an ischemic insult and thereby influence tissue recovery. For the oxygen sensing prolyl-4-hydroxylase domain enzyme (PHD) 2 a clear impact on the macrophage-mediated arteriogenic response after hind-limb ischemia has been demonstrated previously, which involves fine tuning a M2-like macrophage population. To analyze the role of PHD3 in macrophages, we performed hind-limb ischemia (ligation and excision of the femoral artery) in myeloid-specific PHD3 knockout mice (PHD3-/-) and analyzed the inflammatory cell invasion, reperfusion recovery and fibrosis in the ischemic muscle post-surgery. In contrast to PHD2, reperfusion recovery and angiogenesis was unaltered in PHD3-/- compared to WT mice. Macrophages from PHD3-/- mice showed, however, a dampened inflammatory reaction in the affected skeletal muscle tissues compared to WT controls. This was associated with a decrease in fibrosis and an anti-inflammatory phenotype of the PHD3-/- macrophages, as well as decreased expression of Cyp2s1 and increased PGE2-secretion, which could be mimicked by PHD3-/- bone marrow-derived macrophages in serum starvation."],["dc.identifier.doi","10.1038/cddis.2017.375"],["dc.identifier.pmid","28796258"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16494"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/57561"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2041-4889"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Loss of PHD3 in myeloid cells dampens the inflammatory response and fibrosis after hind-limb ischemia"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","378"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Kidney International"],["dc.bibliographiccitation.lastpage","396"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Klanke, Bernd"],["dc.contributor.author","Kalucka, Joanna"],["dc.contributor.author","Schatz, Valentin"],["dc.contributor.author","Daniel, Christoph"],["dc.contributor.author","Mayer, Marleen"],["dc.contributor.author","Goppelt-Struebe, Margarete"],["dc.contributor.author","Herrmann, Martin"],["dc.contributor.author","Thorsteinsdottir, Margret"],["dc.contributor.author","Palsson, Runolfur"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Burzlaff, Nicolai"],["dc.contributor.author","Eckardt, Kai-Uwe"],["dc.contributor.author","Weidemann, Alexander"],["dc.contributor.author","Jantsch, Jonathan"],["dc.contributor.author","Willam, Carsten"],["dc.date.accessioned","2020-12-10T15:20:11Z"],["dc.date.available","2020-12-10T15:20:11Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.kint.2019.02.016"],["dc.identifier.issn","0085-2538"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72583"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Mononuclear phagocytes orchestrate prolyl hydroxylase inhibition-mediated renoprotection in chronic tubulointerstitial nephritis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e00236"],["dc.bibliographiccitation.firstpage","e00236"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","16"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Guentsch, Annemarie"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Nagarajan, Shunmugam"],["dc.contributor.author","Wielockx, Ben"],["dc.contributor.author","Raithatha, Kaamini"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.date.accessioned","2021-06-01T10:47:35Z"],["dc.date.available","2021-06-01T10:47:35Z"],["dc.date.issued","2016"],["dc.description.abstract","ABSTRACT The prolyl-4-hydroxylase domain (PHD) enzymes are regarded as the molecular oxygen sensors. There is an interplay between oxygen availability and cellular metabolism, which in turn has significant effects on the functionality of innate immune cells, such as macrophages. However, if and how PHD enzymes affect macrophage metabolism are enigmatic. We hypothesized that macrophage metabolism and function can be controlled via manipulation of PHD2. We characterized the metabolic phenotypes of PHD2-deficient RAW cells and primary PHD2 knockout bone marrow-derived macrophages (BMDM). Both showed typical features of anaerobic glycolysis, which were paralleled by increased pyruvate dehydrogenase kinase 1 (PDK1) protein levels and a decreased pyruvate dehydrogenase enzyme activity. Metabolic alterations were associated with an impaired cellular functionality. Inhibition of PDK1 or knockout of hypoxia-inducible factor 1α (HIF-1α) reversed the metabolic phenotype and impaired the functionality of the PHD2-deficient RAW cells and BMDM. Taking these results together, we identified a critical role of PHD2 for a reversible glycolytic reprogramming in macrophages with a direct impact on their function. We suggest that PHD2 serves as an adjustable switch to control macrophage behavior."],["dc.identifier.doi","10.1128/MCB.00236-16"],["dc.identifier.gro","3145080"],["dc.identifier.pmid","27795296"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85650"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.status","final"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.subject","PDK; dioxygenases; hypoxia; macrophages; prolyl-4-hydroxylase domain"],["dc.title","PHD2 Is a Regulator for Glycolytic Reprogramming in Macrophages"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Guentsch, Annemarie"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Hillemann, Annette"],["dc.contributor.author","Nagarajan, S."],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Shah, Ajay M."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:17:27Z"],["dc.date.available","2018-11-07T10:17:27Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400087"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41228"],["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","The oxygen sensor PHD2 affects cell migration, energy metabolism and mitochondrial function in macrophages"],["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","216"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:17:26Z"],["dc.date.available","2018-11-07T10:17:26Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400090"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41226"],["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 enzymes 2 and 3 differentially regulate the inflammatory response in a murine model of hind limb ischemia"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]