Alves, Frauke

[["dc.bibliographiccitation.firstpage","2540"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","International Journal of Cancer"],["dc.bibliographiccitation.lastpage","2552"],["dc.bibliographiccitation.volume","139"],["dc.contributor.author","Giannuzzo, Andrea"],["dc.contributor.author","Saccomano, Mara"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Ellegaard, Maria"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Novak, Ivana"],["dc.date.accessioned","2018-11-07T10:05:36Z"],["dc.date.available","2018-11-07T10:05:36Z"],["dc.date.issued","2016"],["dc.description.abstract","The ATP-gated receptor P2X7 (P2X7R) is involved in regulation of cell survival and has been of interest in cancer field. Pancreatic ductal adenocarcinoma (PDAC) is a deadly cancer and new markers and therapeutic targets are needed. PDAC is characterized by a complex tumour microenvironment, which includes cancer and pancreatic stellate cells (PSCs), and potentially high nucleotide/side turnover. Our aim was to determine P2X7R expression and function in human pancreatic cancer cells in vitro as well as to perform in vivo efficacy study applying P2X7R inhibitor in an orthotopic xenograft mouse model of PDAC. In the in vitro studies we show that human PDAC cells with luciferase gene (PancTu-1 Luc cells) express high levels of P2X7R protein. Allosteric P2X7R antagonist AZ10606120 inhibited cell proliferation in basal conditions, indicating that P2X7R was tonically active. Extracellular ATP and BzATP, to which the P2X7R is more sensitive, further affected cell survival and confirmed complex functionality of P2X7R. PancTu-1 Luc migration and invasion was reduced by AZ10606120, and it was stimulated by PSCs, but not by PSCs from P2X7(-/-) animals. PancTu-1 Luc cells were orthotopically transplanted into nude mice and tumour growth was followed noninvasively by bioluminescence imaging. AZ10606120-treated mice showed reduced bioluminescence compared to saline-treated mice. Immunohistochemical analysis confirmed P2X7R expression in cancer and PSC cells, and in metaplastic/neoplastic acinar and duct structures. PSCs number/activity and collagen deposition was reduced in AZ10606120-treated tumours. What's new? Pancreatic ductal adenocarcinoma (PDAC) is one the most difficult types of cancer to detect and treat, challenges that could be overcome through the discovery and development of novel markers and therapeutic strategies. Here, the P2X7 receptor, which regulates cell survival, is shown to also support cell proliferation, migration and invasion in human P2X7R-expressing PDAC cells. Treatment of orthotopic PDAC tumor-bearing mice with the P2X7R-specific inhibitor, AZ10606120, resulted in decreased tumor bioluminescence and reductions in pancreatic stellate cells and collagen deposition. Targeting of P2X7R warrants further investigation as a promising therapeutic approach in pancreatic cancer."],["dc.identifier.doi","10.1002/ijc.30380"],["dc.identifier.isi","000384646200017"],["dc.identifier.pmid","27513892"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13821"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38927"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1097-0215"],["dc.relation.issn","0020-7136"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Targeting of the P2X7 receptor in pancreatic cancer and stellate cells"],["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.firstpage","6367"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Theranostics"],["dc.bibliographiccitation.lastpage","6383"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Markus, M. Andrea"],["dc.contributor.author","Heck, Joachim G."],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Gorpas, Dimitris"],["dc.contributor.author","Feldmann, Claus"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2019-07-09T11:49:44Z"],["dc.date.available","2019-07-09T11:49:44Z"],["dc.date.issued","2018"],["dc.description.abstract","Treatment of inflammatory disorders with glucocorticoids (GCs) is often accompanied by severe adverse effects. Application of GCs via nanoparticles (NPs), especially those using simple formulations, could possibly improve their delivery to sites of inflammation and therefore their efficacy, minimising the required dose and thus reducing side effects. Here, we present the evaluation of NPs composed of GC betamethasone phosphate (BMP) and the fluorescent dye DY-647 (BMP-IOH-NPs) for improved treatment of inflammation with simultaneous in vivo monitoring of NP delivery. Methods: BMP-IOH-NP uptake by MH-S macrophages was analysed by fluorescence and electron microscopy. Lipopolysaccharide (LPS)-stimulated cells were treated for 48 h with BMP-IOH-NPs (1×10-5-1×10-9 M), BMP or dexamethasone (Dexa). Drug efficacy was assessed by measurement of interleukin 6. Mice with Zymosan-A-induced paw inflammation were intraperitoneally treated with BMP-IOH-NPs (10 mg/kg) and mice with ovalbumin (OVA)-induced allergic airway inflammation (AAI) were treated intranasally with BMP-IOH-NPs, BMP or Dexa (each 2.5 mg/kg). Efficacy was assessed in vivo by paw volume measurements with µCT and ex vivo by measurement of paw weight for Zymosan-A-treated mice, or in the AAI model by in vivo x-ray-based lung function assessment and by cell counts in the bronchoalveolar lavage (BAL) fluid and histology. Delivery of BMP-IOH-NPs to the lungs of AAI mice was monitored by in vivo optical imaging and by fluorescence microscopy. Results: Uptake of BMP-IOH-NPs by MH-S cells was observed during the first 10 min of incubation, with the NP load increasing over time. The anti-inflammatory effect of BMP-IOH-NPs in vitro was dose dependent and higher than that of Dexa or free BMP, confirming efficient release of the drug. In vivo, Zymosan-A-induced paw inflammation was significantly reduced in mice treated with BMP-IOH-NPs. AAI mice that received BMP-IOH-NPs or Dexa but not BMP revealed significantly decreased eosinophil numbers in BALs and reduced immune cell infiltration in lungs. Correspondingly, lung function parameters, which were strongly affected in non-treated AAI mice, were unaffected in AAI mice treated with BMP-IOH-NPs and resembled those of healthy animals. Accumulation of BMP-IOH-NPs within the lungs of AAI mice was detectable by optical imaging for at least 4 h in vivo, where they were preferentially taken up by peribronchial and alveolar M2 macrophages. Conclusion: Our results show that BMP-IOH-NPs can effectively be applied in therapy of inflammatory diseases with at least equal efficacy as the gold standard Dexa, while their delivery can be simultaneously tracked in vivo by fluorescence imaging. BMP-IOH-NPs thus have the potential to reach clinical applications."],["dc.identifier.doi","10.7150/thno.28324"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59620"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1838-7640"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.subject.ddc","610"],["dc.title","Therapeutic Fluorescent Hybrid Nanoparticles for Traceable Delivery of Glucocorticoids to Inflammatory Sites"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","24"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","ChemNanoMat"],["dc.bibliographiccitation.lastpage","45"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Neumeier, B. Lilli"],["dc.contributor.author","Khorenko, Mikhail"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Goldmann, Oliver"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Schepers, Ute"],["dc.contributor.author","Reichardt, Holger M."],["dc.contributor.author","Feldmann, Claus"],["dc.date.accessioned","2022-03-01T11:45:18Z"],["dc.date.available","2022-03-01T11:45:18Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1002/cnma.201800310"],["dc.identifier.issn","2199-692X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103282"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","2199-692X"],["dc.title","Fluorescent Inorganic-Organic Hybrid Nanoparticles"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1958"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","International Journal of Cancer"],["dc.bibliographiccitation.lastpage","1974"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Mueller, Friedemann"],["dc.contributor.author","Uhland, Kerstin"],["dc.contributor.author","Petri, Jean Bernhard"],["dc.contributor.author","van de Locht, Andreas"],["dc.contributor.author","Steinmetzer, Torsten"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2018-11-07T08:38:00Z"],["dc.date.available","2018-11-07T08:38:00Z"],["dc.date.issued","2010"],["dc.description.abstract","Proteolytic enzymes expressed on the surface of tumor cells, and thus easily accessible to external interventions, represent useful targets for anticancer and antimetastatic therapies. In our study, we thoroughly evaluated matriptase, a trypsin-like transmembrane serine protease, as potential target for novel inhibitor-based tumor therapies. We applied time-domain near infrared fluorescence (NIRF) imaging to characterize expression and activity of matriptase in vivo in an orthotopic AsPC-1 pancreatic tumor model in nude mice. We show strong and tumor-specific binding of intravenously injected Cy5.5 labeled antimatriptase antibody (MT-Ab Cy5.5) only to primary AsPC-1 tumors and their metastases over time within living mice, taking into account fluorescence intensities and fluorescence lifetimes of the applied probes. Specific binding of MT-Ab Cy5.5 to tumor sites was confirmed by ex vivo NIRF imaging of tumor tissue, NIRF microscopy and by coregistration of the in vivo acquired NIRF intensity maps to anatomical structures visualized by flat-panel volume computed tomography (fpVCT) in living mice. Moreover, using an activatable synthetic substrate S DY-681 we could clearly demonstrate that matriptase is proteolytically active in vitro as well as in vivo in tumor-bearing mice, and that application of synthetic active-site inhibitors having high affinity and selectivity toward matriptase can efficiently inhibit its proteolytic activity for at least 24 hr. We thus successfully applied NIRF imaging in combination with fpVCT to characterize matriptase as a promising molecular target for inhibitor-based cancer therapies."],["dc.identifier.doi","10.1002/ijc.25405"],["dc.identifier.isi","000282404900023"],["dc.identifier.pmid","20473895"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18675"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1097-0215"],["dc.relation.issn","0020-7136"],["dc.title","Time-domain in vivo near infrared fluorescence imaging for evaluation of matriptase as a potential target for the development of novel, inhibitor-based tumor therapies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","721"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","733"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Pardo, Luis A."],["dc.contributor.author","Hartung, Franziska"],["dc.contributor.author","Tietze, Lutz Friedjan"],["dc.contributor.author","Stühmer, Walter"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2018-11-07T10:07:59Z"],["dc.date.available","2018-11-07T10:07:59Z"],["dc.date.issued","2016"],["dc.description.abstract","The K(v)10.1 (Eag1) voltage-gated potassium channel represents a promising molecular target for novel cancer therapies or diagnostic purposes. Physiologically, it is only expressed in the brain, but it was found overexpressed in more than 70 % of tumours of diverse origin. Furthermore, as a plasma membrane protein, it is easily accessible to extracellular interventions. In this study we analysed the feasibility of the anti-K(v)10.1 monoclonal antibody mAb62 to target tumour cells in vitro and in vivo and to deliver therapeutics to the tumour. Using time-domain near infrared fluorescence (NIRF) imaging in a subcutaneous MDA-MB-435S tumour model in nude mice, we showed that mAb62-Cy5.5 specifically accumulates at the tumour for at least 1 week in vivo with a maximum intensity at 48 h. Blocking experiments with an excess of unlabelled mAb62 and application of the free Cy5.5 fluorophore demonstrate specific binding to the tumour. Ex vivo NIRF imaging of whole tumours as well as NIRF imaging and microscopy of tumour slices confirmed the accumulation of the mAb62-Cy5.5 in tumours but not in brain tissue. Moreover, mAb62 was conjugated to the prodrug-activating enzyme beta-D-galactosidase (beta-gal; mAb62-beta-gal). The beta-gal activity of the mAb62-beta-gal conjugate was analysed in vitro on K(v)10.1-expressing MDAMB-435S cells in comparison to control AsPC-1 cells. We show that the mAb62-beta-gal conjugate possesses high beta-gal activity when bound to K(v)10.1-expressing MDA-MB-435S cells. Moreover, using the beta-gal activatable NIRF probe DDAOG, we detected mAb62-beta-gal activity in vivo over the tumour area. In summary, we could show that the anti-K(v)10.1 antibody is a promising tool for the development of novel concepts of targeted cancer therapy."],["dc.identifier.doi","10.1007/s00249-016-1152-z"],["dc.identifier.isi","000384822200012"],["dc.identifier.pmid","27444284"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13779"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39387"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","In vivo imaging of tumour xenografts with an antibody targeting the potassium channel K(v)10.1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","143"],["dc.bibliographiccitation.journal","Journal of Synchrotron Radiation"],["dc.bibliographiccitation.lastpage","155"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","dal Monego, Simeone"],["dc.contributor.author","Larsson, Emanuel"],["dc.contributor.author","Mohammadi, Sara"],["dc.contributor.author","Krenkel, Martin"],["dc.contributor.author","Garrovo, Chiara"],["dc.contributor.author","Biffi, Stefania"],["dc.contributor.author","Lorenzon, Andrea"],["dc.contributor.author","Markus, Andrea"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Accardo, Agostino"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Tromba, Giuliana"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","Functionalized computed tomography (CT) in combination with labelled cells is virtually non-existent due to the limited sensitivity of X-ray-absorption-based imaging, but would be highly desirable to realise cell tracking studies in entire organisms. In this study we applied in-line free propagation X-ray phase-contrast CT (XPCT) in an allergic asthma mouse model to assess structural changes as well as the biodistribution of barium-labelled macrophages in lung tissue. Alveolar macrophages that were barium-sulfate-loaded and fluorescent-labelled were instilled intratracheally into asthmatic and control mice. Mice were sacrificed after 24 h, lungs were kept in situ, inflated with air and scanned utilizing XPCT at the SYRMEP beamline (Elettra Synchrotron Light Source, Italy). Single-distance phase retrieval was used to generate data sets with ten times greater contrast-to-noise ratio than absorption-based CT (in our setup), thus allowing to depict and quantify structural hallmarks of asthmatic lungs such as reduced air volume, obstruction of airways and increased soft-tissue content. Furthermore, we found a higher concentration as well as a specific accumulation of the barium-labelled macrophages in asthmatic lung tissue. It is believe that XPCT will be beneficial in preclinical asthma research for both the assessment of therapeutic response as well as the analysis of the role of the recruitment of macrophages to inflammatory sites."],["dc.identifier.doi","10.1107/S1600577514021730"],["dc.identifier.fs","608140"],["dc.identifier.gro","3141991"],["dc.identifier.isi","000346850200022"],["dc.identifier.pmid","25537601"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11558"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3334"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/230739/EU//P3AGI"],["dc.relation.eissn","1600-5775"],["dc.relation.issn","0909-0495"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","biomedical tomography"],["dc.title","Functionalized synchrotron in-line phase-contrast computed tomography: a novel approach for simultaneous quantification of structural alterations and localization of barium-labelled alveolar macrophages within mouse lung samples"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","089801"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Journal of Biomedical Optics"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Mathejczyk, Julia Eva"],["dc.contributor.author","Pauli, Jutta"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Resch-Genger, Ute"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Napp, Joanna"],["dc.date.accessioned","2018-11-07T09:21:43Z"],["dc.date.available","2018-11-07T09:21:43Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1117/1.JBO.18.8.089801"],["dc.identifier.isi","000324287700025"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29174"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Spie-soc Photo-optical Instrumentation Engineers"],["dc.relation.issn","1083-3668"],["dc.title","High-sensitivity detection of breast tumors in vivo by use of a pH-sensitive near-infrared fluorescence probe (vol 17, 076028, 2012)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2787"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","International Journal of Cancer"],["dc.bibliographiccitation.lastpage","2798"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Leisering, Pia"],["dc.contributor.author","von Ahlen, Melanie"],["dc.contributor.author","Schnelle, Moritz"],["dc.contributor.author","Vogel, Sabine"],["dc.contributor.author","Malz, Cordula R."],["dc.contributor.author","Bordoli, Mattia Renato"],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Hesse, Amke"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Kristiansen, Glen"],["dc.contributor.author","Farhat, Katja"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T09:23:40Z"],["dc.date.available","2018-11-07T09:23:40Z"],["dc.date.issued","2013"],["dc.description.abstract","The prolyl-4-hydroxylase domain 13 (PHD13) enzymes are regulating the protein stability of the -subunit of the hypoxia-inducible factor-1 (HIF-1), which mediates oxygen-dependent gene expression. PHD2 is the main isoform regulating HIF-1 hydroxylation and thus stability in normoxia. In human cancers, HIF-1 is overexpressed as a result of intratumoral hypoxia which in turn promotes tumor progression. The role of PHD2 for tumor progression is in contrast far from being thoroughly understood. Therefore, we established PHD2 knockdown clones of MDA-MB-231 breast cancer cells and analyzed their tumor-forming potential in a SCID mouse model. Tumor progression was significantly impaired in the PHD2 knockdown MDA-MB-231 cells, which could be partially rescued by re-establishing PHD2 expression. In a RNA profile screen, we identified the secreted phosphoprotein 1 (SPP1) as one target, which is differentially regulated as a consequence of the PHD2 knockdown. Knockdown of PHD2 drastically reduced the SPP1 expression in MDA-MB-231 cells. A correlation of SPP1 and PHD2 expression was additionally verified in 294 invasive breast cancer biopsies. In subsequent analyses, we identified that PHD2 alters the processing of transforming growth factor (TGF)-1, which is highly involved in SPP1 expression. The altered processing capacity was associated with a dislocation of the pro-protein convertase furin. Thus, our data demonstrate that in MDA-MB-231 cells PHD2 might affect tumor-relevant TGF-1 target gene expression by altering the TGF-1 processing capacity."],["dc.description.sponsorship","Wilhelm Sander Stiftung [1348530]"],["dc.identifier.doi","10.1002/ijc.27982"],["dc.identifier.isi","000317593100008"],["dc.identifier.pmid","23225569"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29634"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0020-7136"],["dc.title","Knockdown of prolyl-4-hydroxylase domain 2 inhibits tumor growth of human breast cancer MDA-MB-231 cells by affecting TGF-1 processing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2118"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","International Journal of Cancer"],["dc.bibliographiccitation.lastpage","2129"],["dc.bibliographiccitation.volume","142"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Stammes, Marieke A"],["dc.contributor.author","Claussen, Jing"],["dc.contributor.author","Prevoo, Hendrica A J M"],["dc.contributor.author","Sier, Cornelis"],["dc.contributor.author","Hoeben, Freek J M"],["dc.contributor.author","Robillard, Marc"],["dc.contributor.author","Vahrmeijer, Alexander"],["dc.contributor.author","Devling, Tim"],["dc.contributor.author","Chan, Alan B."],["dc.contributor.author","de Geus-Oei, Lioe-Fee"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2018-10-10T11:55:08Z"],["dc.date.available","2018-10-10T11:55:08Z"],["dc.date.issued","2018-05-15"],["dc.description.abstract","A crucial point for the management of pancreatic ductal adenocarcinoma (PDAC) is the decrease of R1 resections. Our aim was to evaluate the combination of multispectral optoacoustic tomography (MSOT) with fluorescence guided surgery (FGS) for diagnosis and perioperative detection of tumor nodules and resection margins in a xenotransplant mouse model of human pancreatic cancer. The peptide cRGD, conjugated with the near infrared fluorescent (NIRF) dye IRDye800CW and with a trans-cyclooctene (TCO) tag for future click chemistry (cRGD-800CW-TCO), was applied to PDAC bearing immunodeficient nude mice; 27 days after orthotopic transplantation of human AsPC-1 cells into the head of the pancreas, mice were injected with cRGD-800CW-TCO and imaged with fluorescence- and optoacoustic devices before and 2, 6 and 24 hr after injection, before they were sacrificed and dissected with a guidance of FGS imaging system. Fluorescence imaging of cRGD-800CW-TCO allowed detection of the tumor area but without information about the depth, whereas MSOT allowed high resolution 3 D identification of the tumor area, in particular of small tumor nodules. Highly sensitive delineation of tumor burden was achieved during FGS in all mice. Imaging of whole-mouse cryosections, histopathological analysis and NIRF microscopy confirmed the localization of cRGD-800CW-TCO within the tumor tissue. In principle, all imaging modalities applied here were able to detect PDAC in vivo. However, the combination of MSOT and FGS provided detailed spatial information of the signal and achieved a complete overview of the distribution and localization of cRGD-800CW-TCO within the tumor before and during surgical intervention."],["dc.identifier.doi","10.1002/ijc.31236"],["dc.identifier.gro","631975"],["dc.identifier.pmid","29277891"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15961"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1097-0215"],["dc.title","Fluorescence- and multispectral optoacoustic imaging for an optimized detection of deeply located tumors in an orthotopic mouse model of pancreatic carcinoma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3860"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of Materials Chemistry C"],["dc.bibliographiccitation.lastpage","3868"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Poß, Marieke"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Niehaus, Oliver"],["dc.contributor.author","Pöttgen, Rainer"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Feldmann, Claus"],["dc.date.accessioned","2022-03-01T11:46:08Z"],["dc.date.available","2022-03-01T11:46:08Z"],["dc.date.issued","2015"],["dc.description.abstract","[M 3+ ][AMA] 3− hybrid nanoparticles consist of M 3+ (M = La, Gd) and the fluorescent dye anion [AMA] 3− (AMA: amaranth red) and show multimodal functionality (fluorescence, magnetism) at excellent photostability."],["dc.description.abstract","Lanthanum and gadolinium amaranth-red hybrid nanoparticles consist of an inorganic cation M 3+ (M = La, Gd) and the fluorescent organic dye anion [AMA] 3− (AMA: amaranth red, C 20 H 11 N 2 O 10 S 3 ) that is systematically named (4 E )-3-oxo-4-[(4-sulfonatonaphth-1-yl)hydrazinyliden]naphthalin-2,7-disulfonate (as well named E123, C.I. 16185, Acid Red 27, C-Red 46, Echtrot D, or Food Red 9). M 3+ [AMA] 3− (M = La, Gd) nanoparticles are prepared via aqueous synthesis as highly stable colloidal suspensions with a mean particle diameter of 47 nm. The chemical composition is validated by infrared spectroscopy (FT-IR), energy-dispersive X-ray analysis (EDX), thermogravimetry (TG) and elemental analysis (EA). M 3+ [AMA] 3− (M = La, Gd) shows intense red emission ( λ max = 700 nm) upon excitation at 400–650 nm. Even after 15 hours of UV irradiation (310 nm), the nanoparticles do not show any significant photobleaching. Based on its red fluorescence and its Gd 3+ -based magnetism, especially, Gd 3+ [AMA] 3− nanoparticles can be interesting as a multimodal contrast agent for biomedical applications or as a magneto-optical marker in polymers. This holds even more in view of biocompatibility, high dye load (79 wt%), excellent photostability, and water-based synthesis of the M 3+ [AMA] 3− (M = La, Gd) inorganic–organic hybrid nanoparticles."],["dc.description.abstract","[M 3+ ][AMA] 3− hybrid nanoparticles consist of M 3+ (M = La, Gd) and the fluorescent dye anion [AMA] 3− (AMA: amaranth red) and show multimodal functionality (fluorescence, magnetism) at excellent photostability."],["dc.description.abstract","Lanthanum and gadolinium amaranth-red hybrid nanoparticles consist of an inorganic cation M 3+ (M = La, Gd) and the fluorescent organic dye anion [AMA] 3− (AMA: amaranth red, C 20 H 11 N 2 O 10 S 3 ) that is systematically named (4 E )-3-oxo-4-[(4-sulfonatonaphth-1-yl)hydrazinyliden]naphthalin-2,7-disulfonate (as well named E123, C.I. 16185, Acid Red 27, C-Red 46, Echtrot D, or Food Red 9). M 3+ [AMA] 3− (M = La, Gd) nanoparticles are prepared via aqueous synthesis as highly stable colloidal suspensions with a mean particle diameter of 47 nm. The chemical composition is validated by infrared spectroscopy (FT-IR), energy-dispersive X-ray analysis (EDX), thermogravimetry (TG) and elemental analysis (EA). M 3+ [AMA] 3− (M = La, Gd) shows intense red emission ( λ max = 700 nm) upon excitation at 400–650 nm. Even after 15 hours of UV irradiation (310 nm), the nanoparticles do not show any significant photobleaching. Based on its red fluorescence and its Gd 3+ -based magnetism, especially, Gd 3+ [AMA] 3− nanoparticles can be interesting as a multimodal contrast agent for biomedical applications or as a magneto-optical marker in polymers. This holds even more in view of biocompatibility, high dye load (79 wt%), excellent photostability, and water-based synthesis of the M 3+ [AMA] 3− (M = La, Gd) inorganic–organic hybrid nanoparticles."],["dc.identifier.doi","10.1039/C5TC00413F"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103574"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2050-7534"],["dc.relation.issn","2050-7526"],["dc.title","M 3+ [amaranth red] 3− (M = La, Gd): a novel sulfonate-based inorganic–organic hybrid nanomaterial for multimodal imaging"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]