Ströbel, Philipp

[["dc.bibliographiccitation.firstpage","89580"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Oncotarget"],["dc.bibliographiccitation.lastpage","89594"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Belharazem, Djeda"],["dc.contributor.author","Grass, Albert"],["dc.contributor.author","Paul, Cornelia"],["dc.contributor.author","Vitacolonna, Mario"],["dc.contributor.author","Schalke, Berthold"],["dc.contributor.author","Rieker, Ralf J."],["dc.contributor.author","Körner, Daniel"],["dc.contributor.author","Jungebluth, Philipp"],["dc.contributor.author","Simon-Keller, Katja"],["dc.contributor.author","Hohenberger, Peter"],["dc.contributor.author","Roessner, Eric M."],["dc.contributor.author","Wiebe, Karsten"],["dc.contributor.author","Gräter, Thomas"],["dc.contributor.author","Kyriss, Thomas"],["dc.contributor.author","Ott, German"],["dc.contributor.author","Geserick, Peter"],["dc.contributor.author","Leverkus, Martin"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Marx, Alexander"],["dc.date.accessioned","2019-12-17T11:02:35Z"],["dc.date.accessioned","2021-10-27T13:21:59Z"],["dc.date.available","2019-12-17T11:02:35Z"],["dc.date.available","2021-10-27T13:21:59Z"],["dc.date.issued","2017"],["dc.description.abstract","The anti-apoptotic cellular FLICE-like inhibitory protein cFLIP plays a pivotal role in normal tissues homoeostasis and the development of many tumors, but its role in normal thymus (NT), thymomas and thymic carcinomas (TC) is largely unknown. Expression, regulation and function of cFLIP were analyzed in biopsies of NT, thymomas, thymic squamous cell carcinomas (TSCC), thymic epithelial cells (TECs) derived thereof and in the TC line 1889c by qRT-PCR, western blot, shRNA techniques, and functional assays addressing survival, senescence and autophagy. More than 90% of thymomas and TSCCs showed increased cFLIP expression compared to NT. cFLIP expression declined with age in NTs but not in thymomas. During short term culture cFLIP expression levels declined significantly slower in neoplastic than non-neoplastic primary TECs. Down-regulation of cFLIP by shRNA or NF-κB inhibition accelerated senescence and induced autophagy and cell death in neoplastic TECs. The results suggest a role of cFLIP in the involution of normal thymus and the development of thymomas and TSCC. Since increased expression of cFLIP is a known tumor escape mechanism, it may serve as tissue-based biomarker in future clinical trials, including immune checkpoint inhibitor trials in the commonly PD-L1high thymomas and TCs."],["dc.identifier.doi","10.18632/oncotarget.15929"],["dc.identifier.eissn","1949-2553"],["dc.identifier.pmid","29163772"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17003"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92059"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","1949-2553"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.subject.ddc","610"],["dc.title","Increased cFLIP expression in thymic epithelial tumors blocks autophagy via NF-κB signalling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e85"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","International Journal of Surgery. Oncology"],["dc.bibliographiccitation.lastpage","5"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Saha, Shekhar"],["dc.contributor.author","Yao, Sha"],["dc.contributor.author","Elakad, Omar"],["dc.contributor.author","Lois, Anna-Maria"],["dc.contributor.author","Henric-Petri, Hannah"],["dc.contributor.author","Buentzel, Judith"],["dc.contributor.author","Hinterthaner, Marc"],["dc.contributor.author","Danner, Bernhard C."],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Emmert, Alexander"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.date.accessioned","2020-06-09T11:55:48Z"],["dc.date.accessioned","2021-10-27T13:22:15Z"],["dc.date.available","2020-06-09T11:55:48Z"],["dc.date.available","2021-10-27T13:22:15Z"],["dc.date.issued","2020"],["dc.description.abstract","Background: UDP-glucose-6-dehydrogenase (UGDH) plays an important role in the production of hyaluronic acid, an extracellular matrix component that is responsible for the promotion of normal cellular growth and migration. Increased levels of UGDH have been linked to the progression of epithelial cancers, such as those of the breast, colon and prostate. Therefore we aimed to analyze if the expression level of UGDH does also influence patients survival of lung cancer patients. Methods: UGDH expression levels were analyzed by immunohistochemistry in 96 samples of pulmonary adenocarcinoma (AC), 84 cases of squamous cell lung carcinoma (SQCLC) and 33 samples of small cell lung cancer (SCLC) and correlated with clinicopathologic characteristics and patient outcome. Results: UGDH was expressed in 62.5% cases of AC, 70.2% cases of SQCLC, and 48.5% cases of SCLC. In AC, expression of UGDH was significantly associated with lymph node metastasis and worse overall survival of the affected patients. However, UGDH expression had no significant correlation to prognosis in SQCLC or SCLC patients. Conclusions: In our study, expression of UGDH was associated with worse prognosis of patients with pulmonary adenocarcinoma so that expression of UGDH might help to guide treatment decisions. Furthermore, UGDH might present a potential novel drug target in AC as it displays inhibitable catalytic activity."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2020"],["dc.identifier.doi","10.1097/IJ9.0000000000000085"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17377"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92078"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","2471-3864"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.title","UDP-glucose 6-dehydrogenase expression as a predictor of survival in patients with pulmonary adenocarcinoma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Schneider, Constanze"],["dc.contributor.author","Thomas, Dominique"],["dc.contributor.author","Knecht, Kirsten M."],["dc.contributor.author","Buzovetsky, Olga"],["dc.contributor.author","Kaderali, Lars"],["dc.contributor.author","Schliemann, Christoph"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Angenendt, Linus"],["dc.contributor.author","Hartmann, Wolfgang"],["dc.contributor.author","Wardelmann, Eva"],["dc.contributor.author","Rothenburger, Tamara"],["dc.contributor.author","Mohr, Sebastian"],["dc.contributor.author","Scheich, Sebastian"],["dc.contributor.author","Comoglio, Federico"],["dc.contributor.author","Wilke, Anne"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Michaelis, Martin"],["dc.contributor.author","Ferreirós, Nerea"],["dc.contributor.author","Geisslinger, Gerd"],["dc.contributor.author","Xiong, Yong"],["dc.contributor.author","Keppler, Oliver T."],["dc.contributor.author","Cinatl, Jindrich"],["dc.date.accessioned","2019-11-25T13:37:34Z"],["dc.date.accessioned","2021-10-27T13:21:34Z"],["dc.date.available","2019-11-25T13:37:34Z"],["dc.date.available","2021-10-27T13:21:34Z"],["dc.date.issued","2019"],["dc.description.abstract","Hypomethylating agents decitabine and azacytidine are regarded as interchangeable in the treatment of acute myeloid leukemia (AML). However, their mechanisms of action remain incompletely understood, and predictive biomarkers for HMA efficacy are lacking. Here, we show that the bioactive metabolite decitabine triphosphate, but not azacytidine triphosphate, functions as activator and substrate of the triphosphohydrolase SAMHD1 and is subject to SAMHD1-mediated inactivation. Retrospective immunohistochemical analysis of bone marrow specimens from AML patients at diagnosis revealed that SAMHD1 expression in leukemic cells inversely correlates with clinical response to decitabine, but not to azacytidine. SAMHD1 ablation increases the antileukemic activity of decitabine in AML cell lines, primary leukemic blasts, and xenograft models. AML cells acquire resistance to decitabine partly by SAMHD1 up-regulation. Together, our data suggest that SAMHD1 is a biomarker for the stratified use of hypomethylating agents in AML patients and a potential target for the treatment of decitabine-resistant leukemia."],["dc.identifier.doi","10.1038/s41467-019-11413-4"],["dc.identifier.pmid","31375673"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16724"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92032"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Selective inactivation of hypomethylating agents by SAMHD1 provides a rationale for therapeutic stratification in AML"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16951"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Oncotarget"],["dc.bibliographiccitation.lastpage","16961"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bremmer, Felix"],["dc.contributor.author","Jarry, Hubertus"],["dc.contributor.author","Unterkircher, Valerie"],["dc.contributor.author","Kaulfuss, Silke"],["dc.contributor.author","Burfeind, Peter"],["dc.contributor.author","Radzun, Heinz-Joachim"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Thelen, Paul"],["dc.date.accessioned","2019-07-09T11:45:18Z"],["dc.date.available","2019-07-09T11:45:18Z"],["dc.date.issued","2018"],["dc.description.abstract","Novel treatments for castration-resistant prostate cancer (CRPC) such as abiraterone acetate (AA) or enzalutamide effectively target the androgen pathway to arrest aberrant signalling and cell proliferation. Testosterone is able to inhibit tumour cell growth in CRPC. Estrogen receptor-beta (ERβ) binds the testosteronemetabolites 3β-androstanediol and 3α-androstanediol in parallel to the canonical estradiol. In the prostate it is widely accepted that ERβ regulates estrogen signalling, mediating anti-proliferative effects. We used the prostate cancer cell lines LNCaP, PC-3, VCaP, and the non-neoplastic BPH-1. VCaP cells were treated with 1 nmol/L testosterone over 20 passages, yielding the cell line VCaPrev, sensitive to hormone therapies. In contrast, LNCaP cells were grown for more than 100 passages yielding a high passage therapy resistant cell line (hiPLNCaP). VCaP and hiPLNCaP cell lines were treated with 5 μmol/L AA for more than 20 passages, respectively, generating the AAtolerant- subtypes VCaPAA and hiPLNCaPAA. Cell lines were treated with testosterone, dihydrotestosterone (DHT), R1881, and the androgen-metabolites 3β-androstanediol and 3α-androstanediol. 3β-androstanediol or 3α-androstanediol significantly reduced proliferation in all cell lines except the BPH-1 and androgen receptor-negative PC-3 and markedly downregulated AR and estrogen receptor alpha (ERα). Whereas ERβ expression was increased in all cell lines except BPH-1 or PC-3. In summary, 3β-adiol or 3α-adiol, as well as DHT and R1881, significantly reduced tumour cell growth in CRPC cells. Thus, these compounds represent novel potential therapeutic approaches to overcome drug-resistance in CRPC, especially with regard to AR-V7 function in therapy resistance. Furthermore, these data confirm the tumour suppressor properties of ERβ in CRPC."],["dc.identifier.doi","10.18632/oncotarget.24763"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59207"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1949-2553"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.subject.ddc","610"],["dc.title","Testosterone metabolites inhibit proliferation of castration- and therapy-resistant prostate cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]