Schön, Margarete

[["dc.bibliographiccitation.firstpage","E4971"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E4977"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Turriani, Elisa"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Schön, Michael P."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Becker, Dorothea"],["dc.date.accessioned","2018-04-23T11:47:36Z"],["dc.date.available","2018-04-23T11:47:36Z"],["dc.date.issued","2017"],["dc.description.abstract","Recent epidemiological and clinical studies have reported a significantly increased risk for melanoma in people with Parkinson’s disease. Because no evidence could be obtained that genetic factors are the reason for the association between these two diseases, we hypothesized that of the three major Parkinson’s disease-related proteins—α-synuclein, LRRK2, and Parkin—α-synuclein might be a major link. Our data, presented here, demonstrate that α-synuclein promotes the survival of primary and metastatic melanoma cells, which is the exact opposite of the effect that α-synuclein has on dopaminergic neurons, where its accumulation causes neuronal dysfunction and death. Because this detrimental effect of α-synuclein on neurons can be rescued by the small molecule anle138b, we explored its effect on melanoma cells. We found that treatment with anle138b leads to massive melanoma cell death due to a major dysregulation of autophagy, suggesting that α-synuclein is highly beneficial to advanced melanoma because it ensures that autophagy is maintained at a homeostatic level that promotes and ensures the cell’s survival."],["dc.identifier.doi","10.1073/pnas.1700200114"],["dc.identifier.gro","3142238"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13362"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0027-8424"],["dc.title","Treatment with diphenyl–pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","528"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Cancer Research"],["dc.bibliographiccitation.lastpage","542"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Kossmann, Eugen"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Schill, Tillmann"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Möckel, Sigrid M.C."],["dc.contributor.author","Spatz, Joachim P."],["dc.contributor.author","Schön, Michael P."],["dc.date.accessioned","2020-12-10T18:37:47Z"],["dc.date.available","2020-12-10T18:37:47Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1158/1541-7786.MCR-17-0272"],["dc.identifier.eissn","1557-3125"],["dc.identifier.issn","1541-7786"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77091"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Nanoscale Tuning of VCAM-1 Determines VLA-4–Dependent Melanoma Cell Plasticity on RGD Motifs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","576"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Investigative Dermatology"],["dc.bibliographiccitation.lastpage","586"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Nieswandt, Bernhard"],["dc.contributor.author","Schoen, Margarete"],["dc.contributor.author","Pozgajova, Miroslava"],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T08:46:21Z"],["dc.date.available","2018-11-07T08:46:21Z"],["dc.date.issued","2010"],["dc.description.abstract","Platelet glycoprotein Iba (GPIb alpha) is part of the receptor complex GPIb-V-IX, which has a critical role in hemostasis, especially through interactions with the subendothelial von Willebrand factor. As there is accumulating evidence for a contribution of platelet receptors to hematogenous tumor metastasis, GPIba is an interesting molecule to study in this context. We have investigated the effect of GPIba inhibition by monovalent Fab fragments on experimental pulmonary metastasis in a syngeneic mouse model using C57BL/6 mice and B16F10 melanoma cells. The early fate of green fluorescent protein (GFP)-transfected melanoma cells under GPIba blockade was also assessed, as was the effect of GPIba inhibition on pulmonary metastasis in mice lacking P-selectin. Surprisingly and, to our knowledge previously unreported, GPIba inhibition led to a significant increase in pulmonary metastasis, and assessment of the early fate of circulating GFP-labeled B16F10 showed improved survival and pulmonary arrest of tumor cells shortly after GPIba inhibition, indicating that inhibition of a platelet protein can, in some cases, promote metastasis of a malignant tumor. In contrast, GPIba blockade in P-selectin-deficient mice had no enhancing effect on metastasis, suggesting the involvement of GPIba in the initial, P-selectin-dependent steps of metastasis. These findings suggest that GPIba contributes to the control of tumor metastasis, in addition to its role in hemostasis."],["dc.identifier.doi","10.1038/jid.2009.278"],["dc.identifier.isi","000273841300034"],["dc.identifier.pmid","19727118"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20670"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0022-202X"],["dc.title","Inhibition of Platelet GPIb alpha and Promotion of Melanoma Metastasis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","579"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.lastpage","584"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Schneider, Philine"],["dc.contributor.author","Schoen, Margarete"],["dc.contributor.author","Pletz, Nadin"],["dc.contributor.author","Seitz, Cornelia S."],["dc.contributor.author","Liu, Ningshu"],["dc.contributor.author","Ziegelbauer, Karl"],["dc.contributor.author","Zachmann, Karolin"],["dc.contributor.author","Emmert, Steffen"],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T09:37:04Z"],["dc.date.available","2018-11-07T09:37:04Z"],["dc.date.issued","2014"],["dc.description.abstract","Due to its almost universal resistance to chemotherapy, metastasized melanoma remains a major challenge in clinical oncology. Given that phosphatidyl inositol-3 kinase (PI3K) activation in melanoma cells is associated with poor prognosis, disease progression and resistance to chemotherapy, the PI3K-Akt signalling pathway is a promising therapeutic target for melanoma treatment. We analysed six human melanoma cell lines for their constitutive activation of Akt and then tested two representative lines, A375 and LOX, for their susceptibility to PI3K-inhibition by the highly specific small molecule inhibitor, BAY 80-6946. In addition, the effect of BAY 80-6946 on A375 and LOX melanoma cells was assessed in vivo in a xenotransplantation mouse model. We provide experimental evidence that specifically inhibiting the PI3K pathway and phosphorylation of Akt by this novel compound results in antitumoral activities including inhibition of proliferation, induction of apoptosis and cell cycle arrest in vitro and in vivo. However, the susceptibility did not show a clear-cut pattern and differed between the melanoma cell lines tested, resulting in in vivo growth inhibition of A375 but not LOX melanoma cells. Thus, in some cases BAY 80-6946 or related compounds may be a valuable addition to the therapeutic armamentarium."],["dc.description.sponsorship","Wilhelm Sander Stiftung"],["dc.identifier.doi","10.1111/exd.12470"],["dc.identifier.isi","000340536100013"],["dc.identifier.pmid","24942196"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32754"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","The novel PI3 kinase inhibitor, BAY 80-6946, impairs melanoma growth in vivo and in vitro"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2510"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Investigative Dermatology"],["dc.bibliographiccitation.lastpage","2520"],["dc.bibliographiccitation.volume","134"],["dc.contributor.author","Forkel, Susann"],["dc.contributor.author","Schoen, Margarete"],["dc.contributor.author","Hildmann, Annette"],["dc.contributor.author","Classen, Anna"],["dc.contributor.author","John, Swen-Malte"],["dc.contributor.author","Danker, Kerstin"],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T09:34:46Z"],["dc.date.available","2018-11-07T09:34:46Z"],["dc.date.issued","2014"],["dc.description.abstract","Psoriasis, a tumor necrosis factor alpha (TNF alpha)-governed inflammatory disorder with prominent dysregulation of cutaneous vascular functions, has evolved into a model disorder for studying anti-inflammatory therapies. We present experimental in vitro and in vivo data on 1-O-octadecyl-2-O-(2-(myo-inositolyl)-ethyl)-sn-glycero-3-(R/S)-phosphatidyl-choline (Ino-C2-PAF), the lead compound of a class of synthetic glycosylated phospholipids, in anti-inflammatory therapy. Ino-C2-PAF strongly induced apoptosis only in TNF alpha-stimulated, but not in untreated human vascular endothelial cells. Moreover, TNF alpha-induced endothelial adhesion molecules that mediated the rolling and firm adhesion of leukocytes (vascular cell adhesion protein-1 (VCAM-1), E-selectin, and ICAM-1) were selectively downregulated by Ino-C2-PAF. Similarly, expression of L-selectin, VCAM-1 receptor alpha(4)beta(1) integrin, and lymphocyte function-associated antigen-1 on human peripheral blood mononuclear cells was reduced without induction of apoptosis. Functionally, these changes were accompanied by significant impairment of rolling and adhesion of human peripheral blood lymphocytes on TNF alpha-activated endothelial cells in a dynamic flow chamber system. When the therapeutic potential of Ino-C2-PAF was assessed in two complementary mouse models of psoriasis, K5.hTGF beta 1 transgenic and JunB/c-Jun-deficient mice, Ino-C2-PAF led to significant alleviation of the clinical symptoms and normalized the pathological cutaneous changes including vascularization. There were no overt adverse effects. These findings suggested that Ino-C2-PAF is a potential candidate in the therapy of inflammatory skin diseases that include abnormal vascular functions."],["dc.identifier.doi","10.1038/jid.2014.170"],["dc.identifier.isi","000342200400012"],["dc.identifier.pmid","24714204"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32248"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1523-1747"],["dc.relation.issn","0022-202X"],["dc.title","Inositoylated Platelet-Activating Factor (Ino-C2-PAF) Modulates Dynamic Lymphocyte-Endothelial Cell Interactions and Alleviates Psoriasis-Like Skin Inflammation in Two Complementary Mouse Models"],["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 Investigative Dermatology"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Pletz, Nadin"],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Ziegelbauer, Karl"],["dc.contributor.author","Emmert, Steffen"],["dc.contributor.author","Liu, Ningshu"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Schoen, Margarete"],["dc.date.accessioned","2018-11-07T08:52:43Z"],["dc.date.available","2018-11-07T08:52:43Z"],["dc.date.issued","2011"],["dc.format.extent","S37"],["dc.identifier.isi","000294361300222"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22240"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.publisher.place","New york"],["dc.relation.conference","41st Annual Meeting of the European-Society-for-Dermatological-Research"],["dc.relation.eventlocation","Barcelona, SPAIN"],["dc.relation.issn","0022-202X"],["dc.title","Doxorubicin-induced activation of NF-kappa B in melanoma cells is abrogated by specific inhibition of IKK beta, but not IKK alpha"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S287"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Investigative Dermatology"],["dc.bibliographiccitation.volume","137"],["dc.contributor.author","Lorenz, V.N."],["dc.contributor.author","Priebe, M.K."],["dc.contributor.author","Dewert, N."],["dc.contributor.author","Amschler, K."],["dc.contributor.author","Erpenbeck, L."],["dc.contributor.author","Schön, M."],["dc.contributor.author","Seitz, C.S."],["dc.date.accessioned","2020-12-10T14:25:10Z"],["dc.date.available","2020-12-10T14:25:10Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.jid.2017.07.752"],["dc.identifier.issn","0022-202X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72467"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","555 c-Rel suppression influences cell cycle regulation of human melanoma cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","301"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.lastpage","304"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Pletz, Nadin"],["dc.contributor.author","Schoen, Margarete"],["dc.contributor.author","Ziegelbauer, Karl"],["dc.contributor.author","Emmert, Steffen"],["dc.contributor.author","Liu, Ningshu"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T09:11:39Z"],["dc.date.available","2018-11-07T09:11:39Z"],["dc.date.issued","2012"],["dc.description.abstract","Drug resistance is arguably the most important challenge in cancer therapy. Here, doxorubicin induced profound of NF-kappa B activation in melanoma cells with a maximum (3.5-fold) at concentrations relevant in vivo. This was followed by transcriptional induction of several gene products involved in tumor progression. A novel IKKa inhibitor (BAY32-5915) was identified and characterized, and doxorubicin-induced NF-kappa B activation was assessed following inhibition of IKKa or IKK beta by small-molecular compounds. While the IKKa inhibitor did not affect doxorubicin-induced NF-kappa B activation, this process was completely abrogated when the IKK beta inhibitor, KINK-1, was used. Moreover, inhibition of IKK beta, but not IKKa, led to significantly increased apoptosis in response to doxorubicin. Our results indicate that the net outcome of chemotherapy is difficult to predict and may even involve mechanisms conferring chemoresistance. In case of doxorubicin-induced NF-kappa B activation, blocking IKK beta, but not IKK alpha, by small molecules can antagonize this activity and, thus, increase chemosensitivity."],["dc.identifier.doi","10.1111/j.1600-0625.2012.01440.x"],["dc.identifier.isi","000301532600012"],["dc.identifier.pmid","22320445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26770"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Doxorubicin-induced activation of NF-kappa B in melanoma cells is abrogated by inhibition of IKK beta, but not by a novel IKK alpha inhibitor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1073"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Investigative Dermatology"],["dc.bibliographiccitation.lastpage","1086"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Pletz, Nadin"],["dc.contributor.author","Wallbrecht, Katrin"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Schoen, Margarete"],["dc.date.accessioned","2018-11-07T08:44:36Z"],["dc.date.available","2018-11-07T08:44:36Z"],["dc.date.issued","2010"],["dc.description.abstract","Metastasized melanoma is almost universally resistant to chemotherapy. Given that constitutive or drug-induced upregulation of NF-kappa B activity is associated with this chemoresistance, NF-kappa B inhibition may increase the susceptibility to antitumoral therapy. On the cellular level, two principles of NF-kappa B inhibition, proteasome inhibition by bortezomib and I kappa B kinase-beta (IKK beta) inhibition by the kinase inhibitor of NF-kappa B-1 (KINK-1), significantly increased the antitumoral efficacy of camptothecin. When combined with camptothecin, either of the two NF-kappa B-inhibiting principles synergistically influenced progression-related in vitro functions, including cell growth, apoptosis, and invasion through an artificial basement membrane. In addition, when C57BL/6 mice were intravenously injected with B16F10 melanoma cells, the combination of cytostatic treatment with either of the NF-kappa B-inhibiting compounds revealed significantly reduced pulmonary metastasis compared to either treatment alone. However, on the molecular level, nuclear translocation of p65, cell cycle analysis, and expression of NF-kappa B-dependent gene products disclosed distinctly different molecular mechanisms, resulting in the same functional effect. That proteasome inhibition and IKK beta inhibition affect distinct molecular pathways downstream of NF-kappa B, both leading to increased chemosensitivity, is previously unreported. Thus, it is conceivable that switching the two principles of NF-kappa B inhibition, once resistance to one of the agents occurs, will improve future treatment regimens."],["dc.identifier.doi","10.1038/jid.2009.365"],["dc.identifier.isi","000276251000024"],["dc.identifier.pmid","19940859"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20238"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0022-202X"],["dc.title","NF-kappa B Inhibition through Proteasome Inhibition or IKK beta Blockade Increases the Susceptibility of Melanoma Cells to Cytostatic Treatment through Distinct Pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16856"],["dc.bibliographiccitation.issue","42"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","16861"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Koepper, Frederik"],["dc.contributor.author","Bierwirth, Cathrin"],["dc.contributor.author","Schoen, Margarete"],["dc.contributor.author","Kunze, Meike"],["dc.contributor.author","Elvers, Ingegerd"],["dc.contributor.author","Kranz, Dominique"],["dc.contributor.author","Saini, Priyanka"],["dc.contributor.author","Menon, Manoj B."],["dc.contributor.author","Walter, David"],["dc.contributor.author","Sorensen, Claus Storgaard"],["dc.contributor.author","Gaestel, Matthias"],["dc.contributor.author","Helleday, Thomas"],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Dobbelstein, Matthias"],["dc.date.accessioned","2018-11-07T09:18:38Z"],["dc.date.available","2018-11-07T09:18:38Z"],["dc.date.issued","2013"],["dc.description.abstract","DNA damage can obstruct replication forks, resulting in replicative stress. By siRNA screening, we identified kinases involved in the accumulation of phosphohistone 2AX (gamma H2AX) upon UV irradiation-induced replication stress. Surprisingly, the strongest reduction of phosphohistone 2AX followed knockdown of the MAP kinase-activated protein kinase 2 (MK2), a kinase currently implicated in p38 stress signaling and G2 arrest. Depletion or inhibition of MK2 also protected cells from DNA damage-induced cell death, and mice deficient for MK2 displayed decreased apoptosis in the skin upon UV irradiation. Moreover, MK2 activity was required for damage response, accumulation of ssDNA, and decreased survival when cells were treated with the nucleoside analogue gemcitabine or when the checkpoint kinase Chk1 was antagonized. By using DNA fiber assays, we found that MK2 inhibition or knockdown rescued DNA replication impaired by gemcitabine or by Chk1 inhibition. This rescue strictly depended on transiesion DNA polymerases. In conclusion, instead of being an unavoidable consequence of DNA damage, alterations of replication speed and origin firing depend on MK2-mediated signaling."],["dc.identifier.doi","10.1073/pnas.1304355110"],["dc.identifier.isi","000325634200042"],["dc.identifier.pmid","24082115"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28446"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Damage-induced DNA replication stalling relies on MAPK-activated protein kinase 2 activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]