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  • 1
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    German Medical Science; Düsseldorf, Köln
    In:  57. Jahrestagung der Deutschen Gesellschaft für Neurochirurgie e.V. (DGNC), Joint Meeting mit der Japanischen Gesellschaft für Neurochirurgie; 20060511-20060514; Essen; DOCP 12.201 /20060508/
    Publication Date: 2006-07-31
    Keywords: spinal implants ; titanium ; corrosion ; Wirbelsäulenimplantate ; Titan ; Korrosion ; ddc: 610
    Language: English
    Type: conferenceObject
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  • 2
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  Deutscher Kongress für Orthopädie und Unfallchirurgie (DKOU 2015); 20151020-20151023; Berlin; DOCPO17-879 /20151005/
    Publication Date: 2015-10-06
    Keywords: Querschnittlähmung ; Neuroregeneration ; Therapie ; Mikrosystemtechnik ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 3
    Keywords: APOPTOSIS ; PATHWAYS ; DEATH ; MESSENGER-RNA ; IDENTIFICATION ; chemotherapy ; PROGRESS ; Anti-cancer ; ENDOPLASMIC-RETICULUM-STRESS ; ACTIVATING TRANSCRIPTION FACTOR-3 ; Bio-weapon ; Depurination ; RICIN ; RIP ; Riproximin ; UPR ; Volkensin ; XIMENIA-AMERICANA
    Abstract: Cytotoxic ribosome-inactivating proteins (RIPs) of type II such as ricin were investigated as anti-cancer agents, but also pose a threat as biological weapons. The molecular mechanism leading to their toxic effects is, however, not yet clear. The current paradigm, which states that the irreversible depurination of 28S rRNA results in a general translational arrest eventually leading to cell death, has been questioned. Using micro-array, qRT-PCR and Western blot, we identified the unfolded protein response (UPR), a cellular mechanism activated in response to endoplasmic reticulum stress, that is induced in HCT116 and MDA-MB-231 cells exposed to the plant type II RIPs ricin, riproximin and volkensin. Apoptosis was induced by concentrations at which translation of UPR-related genes still occurred, despite concomitant ribosomal depurination. We conclude that UPR induction represents a model that better describes the cellular effects of RIP exposure at concentrations at which selected proteins are translated despite ribosomal depurination.
    Type of Publication: Journal article published
    PubMed ID: 20844919
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  • 4
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  Deutscher Kongress für Orthopädie und Unfallchirurgie (DKOU 2012); 20121023-20121026; Berlin; DOCPO17-734 /20121002/
    Publication Date: 2012-10-03
    Keywords: Mikrosystem ; Regeneration ; Rückenmarksläsion ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 5
    Keywords: tumor ; Germany ; TOXICITY ; EXPOSURE ; liver ; RISK ; RISKS ; TUMORS ; MICE ; TIME ; RAT ; RATS ; chemotherapy ; DIET ; rat liver ; STANDARD ; DEHP ; DI(2-ETHYLHEXYL) PHTHALATE ; di-(2-ethylhexyl)-phthalate ; epigenetic carcinogenicity ; leydig cell tumors of the testes ; lifelong exposure ; PPAR-ALPHA ; TESTICULAR TOXICITY
    Abstract: The plasticizer di-(2-ethylhexyl)-phthalate (DEHP) is the most important phthalate with respect to its production, use and occurrence in the environment. In standard carcinogenicity experiments with F344 rats and B6C3F1 mice, DEHP has been shown to induce hepatocellular tumors. Moreover, DEHP is strongly suspected to be a developmental and reproductive toxicant. The present study aimed at determining the long-term toxic effects of lifetime exposure to low concentrations of DEHP in Sprague-Dawley rat strain. Seven hundred and thirty male rats, stratified into four groups, received DEHP with the diet, resulting in dosages of 300, 95, 30 and 0 mg/kg per day for up to 159 weeks and were only sacrificed when moribund. All organs of the dead and sacrificed animals were histopathologically examined. Significantly increased tumor incidences after exposure to 300 mg/kg per day DEHP (P = 0.04 for testes and 0.05 for liver) and a significant dose-related trend (P-Trend = 0.02 for testes and 0.03 for liver) were detected in both organs liver and testes. Time to tumor analysis revealed that DEHP-induced testicular tumors developed earlier in lifetime than hepatocellular neoplasias, and their multiplicity increased with time. In addition, animals exposed to the highest DEHP dose showed a significantly increased rate of testicular tubular atrophy (P 〈 0.01). In conclusion, this study shows for the first time that the rat testes are a target organ of DEHP carcinogenicity in Sprague-Dawley rats upon lifetime exposure. This new finding indicates the importance of evaluating the effects of lifetime exposure in assessing the potential human health risks of DEHR In addition, the carcinogenicity should be evaluated in rat strains with low spontaneous tumor incidence in the organs known as target of DEHP toxicity. (C) 2004 Elsevier Ireland Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 15588926
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  • 6
    Keywords: CLONING ; PROTEIN ; SEQUENCE ; ISOFORMS ; IDENTIFICATION ; CHROMATOGRAPHY ; LECTINS ; RIBOSOME-INACTIVATING PROTEINS ; PLANTS ; Riproximin ; A-CHAIN ; Plant lectin ; RICINUS-COMMUNIS AGGLUTININ ; SAMBUCUS ; Type II RIP ; VISCUM-ALBUM L ; Ximenia americana
    Abstract: Highly pure riproximin was isolated from the fruit kernels of Ximenia americana, a defined, seasonally available and potentially unlimited herbal source. The newly established purification procedure included an initial aqueous extraction, removal of lipids with chloroform and subsequent chromatographic purification steps on a strong anion exchange resin and lactosyl-Sepharose. Consistent purity and stable biological properties were shown over several purification batches. The purified, kernel-derived riproximin was characterized in comparison to the African plant material riproximin and revealed highly similar biochemical and biological properties but differences in the electrophoresis pattern and mass spectrometry peptide profile. Our results suggest that although the purified fruit kernel riproximin consists of a mixture of closely related isoforms, it provides a reliable basis for further research and development of this type II ribosome inactivating protein (RIP).
    Type of Publication: Journal article published
    PubMed ID: 22178181
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  • 7
    Abstract: PURPOSE: We have previously identified the gene MACC1 as a strong prognostic biomarker for colorectal cancer metastasis and patient survival. Here, we report for the first time the generation of transgenic mouse models for MACC1. EXPERIMENTAL DESIGN: We generated mice with transgenic overexpression of MACC1 in the intestine driven by the villin promoter (vil-MACC1) and crossed them with Apc(Min) mice (vil-MACC1/Apc(Min)). RESULTS: vil-MACC1/Apc(Min) mice significantly increased the total number of tumors (P = 0.0056). This was particularly apparent in large tumors (〉/=3-mm diameter; P = 0.0024). A detailed histopathologic analysis of these lesions demonstrated that the tumors from the vil-MACC1/Apc(Min) mice had a more invasive phenotype and, consequently, showed a significantly reduced survival time than Apc(Min) mice (P = 0.03). Molecular analysis revealed an increased Wnt and pluripotency signaling in the tumors of vil-MACC1/Apc(Min) mice. Specifically, we observed a prominent upregulation of the pluripotency markers Oct4 and Nanog in these tumors compared with Apc(Min) controls. Finally, we could also validate that Oct4 and Nanog are regulated by MACC1 in vitro and strongly correlate with MACC1 levels in a cohort of 60 tumors of colorectal cancer patients (r = 0.7005 and r = 0.6808, respectively; P 〉 0.0001 and P 〉 0.0002, respectively). CONCLUSIONS: We provide proof of principle that MACC1-induced tumor progression in colorectal cancer acts, at least in part, via the newly discovered MACC1/Nanog/Oct4 axis. These findings might have important implications for the design of novel therapeutic intervention strategies to restrict tumor progression. Clin Cancer Res; 22(11); 2812-24. (c)2016 AACR.
    Type of Publication: Journal article published
    PubMed ID: 26758557
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  • 8
    Abstract: MACC1 (Metastasis Associated in Colon Cancer 1) is a key driver and prognostic biomarker for cancer progression and metastasis in a large variety of solid tumor types, particularly colorectal cancer (CRC). However, no MACC1 inhibitors have been identified yet. Therefore, we aimed to target MACC1 expression using a luciferase reporter-based high-throughput screening with the ChemBioNet library of more than 30,000 compounds. The small molecules lovastatin and rottlerin emerged as the most potent MACC1 transcriptional inhibitors. They remarkably inhibited MACC1 promoter activity and expression, resulting in reduced cell motility. Lovastatin impaired the binding of the transcription factors c-Jun and Sp1 to the MACC1 promoter, thereby inhibiting MACC1 transcription. Most importantly, in CRC-xenografted mice, lovastatin and rottlerin restricted MACC1 expression and liver metastasis. This is-to the best of our knowledge-the first identification of inhibitors restricting cancer progression and metastasis via the novel target MACC1. This drug repositioning might be of therapeutic value for CRC patients.
    Type of Publication: Journal article published
    PubMed ID: 28570591
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  • 9
    Keywords: PEPTIDE ; CANCER ; CELLS ; Germany ; IN-VIVO ; MODEL ; PHASE-I ; VIVO ; SYSTEM ; DISTINCT ; PROTEIN ; PROTEINS ; DNA ; FAMILY ; RAT ; MR ; BINDING ; CELL-LINES ; SEQUENCE ; treatment ; IDENTIFICATION ; METASTASIS ; colorectal cancer ; COLORECTAL-CANCER ; chemotherapy ; CRYSTAL-STRUCTURE ; EXCHANGE ; PEPTIDES ; Jun ; LECTIN ; DE-NOVO ; SEQUENCE-ANALYSIS ; AFFINITY ; ENDOPLASMIC-RETICULUM ; CYTOTOXICITY ; FAMILIES ; SOLID TUMORS ; EXTRACTION ; CANCER-TREATMENT ; in vivo ; FRAGMENT ; AGREEMENT ; PRIMERS ; anticancer agent ; RAT-LIVER METASTASIS ; AVISCUMINE RVISCUMIN ; liver metastasis model ; peroral activity ; plant protein ; RICIN-A-CHAIN
    Abstract: The aim of this study was to identify and characterize the active component(s) of Ximenia americana plant material used to treat cancer in African traditional medicine. By a combination of preextraction, extraction, ion exchange and affinity chromatography, a mixture of two cytotoxic proteins was isolated. Using degenerated primers designed on the de novo sequence of two tryptic peptides from one of these proteins, a DNA fragment was amplified and the sequence obtained was used to determine the complete cDNA sequence by the RACE method. Sequence analysis and molecular modeling showed that the new protein, riproximin, belongs to the family of type II ribosome inactivating proteins. These results are in good agreement with the ability of riproximin to inhibit protein synthesis in a cell-free system, as well as with the cytotoxicity of riproximin, as demonstrated by its IC50 value of 0.5 pM in MCF7, 1.1 pM in HELA and 0.6 pM in CC531-lacZ cells. To assess the antineoplastic efficacy of the purified riproximin in vivo, the CC531-lacZ colorectal cancer rat metastasis model was used. Significant anticancer activity was found after administration of total dosages of 100 (perorally) and 10 (intraperitoneally) pmol riproximin/kg. These results suggest that riproximin has distinct potential for cancer treatment
    Type of Publication: Journal article published
    PubMed ID: 16641197
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  • 10
    Keywords: CANCER ; CANCER CELLS ; CELLS ; IN-VITRO ; tumor ; AGENTS ; Germany ; IN-VIVO ; VITRO ; GENE ; PROTEIN ; PROTEINS ; LINES ; DNA ; MECHANISM ; RAT ; MR ; BREAST ; breast cancer ; BREAST-CANCER ; ACIDS ; IDENTIFICATION ; COLORECTAL-CANCER ; mass spectrometry ; CELL-LINE ; chemotherapy ; leukemia ; LINE ; CANCER-CELLS ; MASS-SPECTROMETRY ; AMINO-ACIDS ; sensitivity ; AFFINITY ; CYTOTOXICITY ; antitumor agents ; Chinese herbal medicines ; LEUKEMIA-CELLS ; GEMCITABINE ; in vivo ; ANTITUMOR ; Miltefosine ; CC531 isogenic rat model ; MOLECULAR COMPOUNDS ; new antineoplastic agent ; plant origin ; RAT-LIVER METASTASIS ; RIBOSOME-INACTIVATING PROTEINS ; selective cytotoxicity
    Abstract: The antineoplastic activity of a plant powder used in African traditional medicine for treating cancer was investigated by analyzing the activity of various extracts in vitro. The most active, aqueous extract was subsequently subjected to a detailed investigation in a panel of 17 tumor cell lines, showing an average IC50 of 49 mg raw powder/ml medium. The sensitivity of the cell lines varied by two orders of magnitude, from 1.7 mg/ml in MCF7 breast cancer cells to 170 mg/ml in AR230 chronic-myeloid leukemia cells. Immortalized, non-tumorigenic cell lines showed a marginal sensitivity. In addition, kinetic and recovery experiments performed in MCF7 and U87-MG cells and a comparison with the antineoplastic activity of miltefosine, gemcitabine, and cisplatinum in MCF7, U87-MG, HEp2, and SAOS2 cells revealed no obvious similarity between the sensitivity profiles of the extract and the three standard agents, suggesting a different mechanism of cytotoxicity. The in vivo antitumor activity was determined in the CC531 colorectal cancer rat model. Significant anticancer activity was found following administration of equitoxic doses of 100 (perorally) and 5 (intraperitoneally) mg raw powder/kg, indicating a 95% reduced activity following intestinal absorption. By sequencing the mitochondrial gene for the large Subunit of the ribulose bis-phosphate carboxylase (rbcL) in DNA from the plant material, the source plant was identified as Ximenia americana. A physicochemical characterization showed that the active antineoplastic component(s) of the plant material are proteins with galactose affinity. Moreover, by mass spectrometry, one of these proteins was shown to contain a stretch of 11 amino acids identical to a tryptic peptide from the ribosome-inactivating protein ricin. (c) 2005 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16005923
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