Napp, Joanna

[["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.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","101"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","ChemBioChem"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Pauli, Jutta"],["dc.contributor.author","Pochstein, Marieke"],["dc.contributor.author","Haase, Andrea"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Luch, Andreas"],["dc.contributor.author","Resch-Genger, Ute"],["dc.date.accessioned","2018-11-07T10:28:29Z"],["dc.date.available","2018-11-07T10:28:29Z"],["dc.date.issued","2017"],["dc.description.abstract","The design of bright and functional dye-protein conjugates requires hydrophilic and stable fluorophores with high molar absorption coefficients and high fluorescence quantum yields, which must not be prone to dimerization, as well as conservation of protein function and suppression of protein association. Although many synthetic dyes meet these needs, the influence of dye charge on bioconjugate performance is commonly neglected. This encouraged us to assess the spectroscopic properties, antibody functionality, binding behavior, folding, and association of conjugates of the therapeutic antibodies trastuzumab and cetuximab with the red cyanine dyes S0586, S2381, and 6SIDCC (bearing two, three, and six sulfonate groups, respectively). Our results demonstrate a negligible effect of dye labeling on antibody folding, yet a strong influence of label charge and density on antibody isoelectric points and association. Especially 6SIDCC decreased strongly the isoelectric points of both antibodies and their heavy or light chains even at low labeling degrees, thus favoring protein association. Although an increasingly negative dye charge reduces antigen affinity as shown in a competitive immunoassay, all conjugates still bound to cells overexpressing the target of the respective antibody. Obviously, dyes that cause minimum dimerization with a small number of charged groups are best for conjugate brightness, minimum protein association, and strong target binding. This underlines the need to consider dye charge for the rational design of conjugates with optimum performance."],["dc.identifier.doi","10.1002/cbic.201600299"],["dc.identifier.isi","000392936000011"],["dc.identifier.pmid","27790811"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43432"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1439-7633"],["dc.relation.issn","1439-4227"],["dc.title","Influence of Label and Charge Density on the Association of the Therapeutic Monoclonal Antibodies Trastuzumab and Cetuximab Conjugated to Anionic Fluorophores"],["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"]]

[["dc.bibliographiccitation.firstpage","96"],["dc.bibliographiccitation.lastpage","97"],["dc.bibliographiccitation.volume","Life Sciences and Cultural Heritage, Elettra - SYRMEP"],["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, G."],["dc.date.accessioned","2020-03-11T09:34:33Z"],["dc.date.available","2020-03-11T09:34:33Z"],["dc.date.issued","2015"],["dc.description.abstract","We successfully applied synchrotron in-line phase contrast CT in combination with single distance phase retrieval to image lungs of asthmatic and healthy mice in high resolution in situ. The increased image quality in phase contrast CT added functional contrast to CT which enabled simultaneous i\\) anatomical imaging for the discrimination of asthmatic from healthy mice based on alterations of their lung structure as well as ii\\) functional imaging to track the location of barium sulfate loaded intratracheally instilled alveolar macrophages. Link to fulltext: http://www.elettra.eu/images/Documents/SCIENCE/Elettra%20HL%202015.pdf"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63295"],["dc.language.iso","en"],["dc.publisher","Elettra - Sincrotrone Trieste"],["dc.publisher.place","Trieste"],["dc.relation.ispartof","ELETTRA HIGHLIGHTS 2014-2015"],["dc.title","Simultaneous localization of labelled macrophages and structural analysis of asthmatic mice by phase contrast CT"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","469"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Imaging"],["dc.bibliographiccitation.lastpage","480"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Mathejczyk, Julia Eva"],["dc.contributor.author","Pauli, Jutta"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Napp, Joanna"],["dc.contributor.author","Tietze, Lutz F."],["dc.contributor.author","Kessler, Horst"],["dc.contributor.author","Resch-Genger, Ute"],["dc.contributor.author","Alves, Frauke"],["dc.date.accessioned","2018-11-07T08:50:00Z"],["dc.date.available","2018-11-07T08:50:00Z"],["dc.date.issued","2011"],["dc.description.abstract","Labeling of RGD peptides with near-infrared fluorophores yields optical probes for noninvasive imaging of tumors overexpressing alpha(v)beta(3) integrins. An important prerequisite for optimum detection sensitivity in vivo is strongly absorbing and highly emissive probes with a known fluorescence lifetime. The RGD-Cy5.5 optical probe was derived by coupling Cy5.5 to a cyclic arginine-glycine-aspartic acid-D-phenylalanine lysine (RGDfK) peptide via an aminohexanoic acid spacer. Spectroscopic properties of the probe were studied in different matrices in comparison to Cy5.5. For in vivo imaging, human glioblastoma cells were subcutaneously implanted into nude mice, and in vivo fluorescence intensity and lifetime were measured. The fluorescence quantum yield and lifetime of Cy5.5 were found to be barely affected on RGD conjugation but dramatically changed in the presence of proteins. By time domain fluorescence imaging, we demonstrated specific binding of RGD-Cy5.5 to glioblastoma xenografts in nude mice. Discrimination of unspecific fluorescence by lifetime-gated analysis further enhanced the detection sensitivity of RGD-Cy5.5-derived signals. We characterized RGD-Cy5.5 as a strongly emissive and stable probe adequate for selective targeting of alpha(v)beta(3) integrins. The specificity and thus the overall detection sensitivity in vivo were optimized with lifetime gating, based on the previous determination of the probes fluorescence lifetime under application-relevant conditions."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [Sonderforschungsbereich 416]"],["dc.identifier.doi","10.2310/7290.2011.00018"],["dc.identifier.isi","000299129200007"],["dc.identifier.pmid","22201538"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21589"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation.issn","1535-3508"],["dc.title","Spectroscopically Well-Characterized RGD Optical Probe as a Prerequisite for Lifetime-Gated Tumor Imaging"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2277"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","International Journal of Cancer"],["dc.bibliographiccitation.lastpage","2289"],["dc.bibliographiccitation.volume","139"],["dc.contributor.author","Saccomano, Mara"],["dc.contributor.author","Dullin, Christian"],["dc.contributor.author","Alves, Frauke"],["dc.contributor.author","Napp, Joanna"],["dc.date.accessioned","2018-11-07T10:05:47Z"],["dc.date.available","2018-11-07T10:05:47Z"],["dc.date.issued","2016"],["dc.description.abstract","The high rate of recurrence in patients with pancreatic ductal adenocarcinoma (PDAC) could be reduced by supporting the surgeons in discriminating healthy from diseased tissues with intraoperative fluorescence-guidance. Here, we studied the suitability of Cetuximab, a therapeutic monoclonal antibody targeting the human epidermal growth factor receptor (EGFR), near-infrared (NIR) fluorescently labeled as a new tool for fluorescence-guided surgery. Distribution and binding of systemically injected Cetuximab Alexa Fluor 647 conjugate (Cetux-Alexa-647) and the co-injected control human IgG Alexa Fluor 750 conjugate (hIgG-Alexa-750) was studied over 48 h by NIR fluorescence imaging in mice bearing human orthotopic AsPC-1 and MIA PaCa-2 PDAC tumors. Cetux-Alexa-647, but not the control hIgG-Alexa-750 fluorescence, was specifically detected in vivo in both primary pancreatic tumors with maximum fluorescence intensities at 24 h, and in metastases of AsPC-1 tumors as small as 1 mm. Lifetime analysis and NIR fluorescence microscopy of tumor sections confirmed the binding specificity of Cetux-Alexa-647 to PDAC cells. Comparable results were obtained with Cetuximab conjugated to Alexa Fluor 750 dye (Cetux-Alexa-750). Fluorescence-guided dissection, performed 24 h after injection of Cetuximab conjugated to IRDye 800CW (Cetux-800CW), enabled a real-time delineation of AsPC-1 tumor margins, and small metastases. Odyssey scans revealed that only the vital part of the tumor, but not the necrotic part was stained with Cetux-800CW. NIR fluorescently labeled Cetuximab may be a promising tool that can be applied for fluorescence-guided surgery to visualize tumor margins and metastatic sites in order to allow a precise surgical resection."],["dc.identifier.doi","10.1002/ijc.30277"],["dc.identifier.isi","000384646100013"],["dc.identifier.pmid","27428782"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38967"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1097-0215"],["dc.relation.issn","0020-7136"],["dc.title","Preclinical evaluation of near-infrared (NIR) fluorescently labeled cetuximab as a potential tool for fluorescence-guided surgery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]