Relevant bibliographies by topics / Immunotoxine

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Immunotoxine'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Immunotoxine"

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Zovickian, John, Virginia Gray Johnson, and Richard J. Youle. "Potent and specific killing of human malignant brain tumor cells by an anti-transferrin receptor antibody-ricin immunotoxin." Journal of Neurosurgery 66, no. 6 (June 1987): 850–61. http://dx.doi.org/10.3171/jns.1987.66.6.0850.

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✓ Immunotoxins are hybrid molecules which combine the exquisite selectivity of monoclonal antibodies with the potent toxicity of protein toxins. An immunotoxin was constructed by linking a murine monoclonal antibody against the human transferrin receptor (TR) to the plant toxin, ricin. The cytotoxic activity of the anti-TR-ricin immunotoxin was tested in vitro and demonstrated highly potent and cell type-specific killing of cells derived from human glioblastoma, medulloblastoma, and leukemia. The anti-TR-ricin immunotoxin killed more than 50% of “target” cells at a concentration of 5.6 × 10−13 M after an 18-hour incubation with the ionophore, monensin. This potency exceeds that of any other anti-TR immunotoxin reported in the literature. When the activity of the anti-TR-ricin immunotoxin against “target” tumor-derived cells was compared with the immunotoxin's activity against “non-target” cells, it could be predicted that a selective toxicity of anti-TR-ricin immunotoxin between tumor cells and normal brain was more than 150- to 1380-fold. Solid-phase indirect radioimmunoassay techniques were used to demonstrate significantly higher levels of TR in the glioblastoma- and medulloblastoma-derived cell lines, as well as in surgical tissue samples of medulloblastoma and glioblastoma, as compared to normal brain. Immunotoxins targeted to the TR may possess sufficient specificity to be of therapeutic importance, particularly to treat neoplastic disease of the central nervous system involving compartments (such as intrathecal, intraventricular, or cystic) where delivery of immunotoxins to tumor would not require transvascular transport.
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Allahyari, Hossein, Sahar Heidari, Mehdi Ghamgosha, Parvaneh Saffarian, and Jafar Amani. "Immunotoxin: A new tool for cancer therapy." Tumor Biology 39, no. 2 (February 2017): 101042831769222. http://dx.doi.org/10.1177/1010428317692226.

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Cancer is one of the main reasons of death in the most countries and in Iran. Immunotherapy quickly became one of the best methods of cancer treatment, along with chemotherapy and radiation. “Immunotoxin Therapy” is a promising way of cancer therapy that is mentioned in this field. Immunotoxins are made from a toxin attaching to an antibody target proteins present on cancer cells. The first-generation immunotoxins were made of a full-length toxin attached to whole monoclonal antibodies. But, these immunotoxins could bind to normal cells. DAB389IL2 was the first immunotoxin approved by the Food and Drug Administration. Current trends and researches are ongoing on finding proteins that in combination with immunotoxins have minimal immunogenicity and the most potency for target cell killing.
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Wu, Y. N., M. Gadina, J. H. Tao-Cheng, and R. J. Youle. "Retinoic acid disrupts the Golgi apparatus and increases the cytosolic routing of specific protein toxins." Journal of Cell Biology 125, no. 4 (May 15, 1994): 743–53. http://dx.doi.org/10.1083/jcb.125.4.743.

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All-trans retinoic acid can specifically increase receptor mediated intoxication of ricin A chain immunotoxins more than 10,000 times, whereas fluid phase endocytosis of ricin A chain alone or ricin A chain immunotoxins was not influenced by retinoic acid. The immunotoxin activation by retinoic acid does not require RNA or protein synthesis and is not a consequence of increased receptor binding of the immunotoxin. Vitamin D3 and thyroid hormone T3, that activate retinoic acid receptor (RAR) cognates, forming heterodimers with retinoid X receptor (RXR), do not affect the potency of immunotoxins. Among other retinoids tested, 13-cis retinoic acid, which binds neither RAR nor RXR, also increases the potency of the ricin A chain immunotoxin. Therefore, retinoic acid receptor activation does not appear to be necessary for immunotoxin activity. Retinoic acid potentiation of immunotoxins is prevented by brefeldin A (BFA) indicating that in the presence of retinoic acid, the immunotoxin is efficiently routed through the Golgi apparatus en route to the cytoplasm. Directly examining cells with a monoclonal antibody (Mab) against mannosidase II, a Golgi apparatus marker enzyme, demonstrates that the Golgi apparatus changes upon treatment with retinoic acid from a perinuclear network to a diffuse aggregate. Within 60 min after removal of retinoic acid the cell reassembles the perinuclear Golgi network indistinguishable with that of normal control cells. C6-NBD-ceramide, a vital stain for the Golgi apparatus, shows that retinoic acid prevents the fluorescent staining of the Golgi apparatus and eliminates fluorescence of C6-NBD-ceramide prestained Golgi apparatus. Electron microscopy of retinoic acid-treated cells demonstrates the specific absence of any normal looking Golgi apparatus and a perinuclear vacuolar structure very similar to that seen in monensin-treated cells. This vacuolization disappears after removal of the retinoic acid and a perinuclear Golgi stacking reappears. These results indicate that retinoic acid alters intracellular routing, probably through the Golgi apparatus, potentiating immunotoxin activity indepedently of new gene expression. Retinoic acid appears to be a new reagent to manipulate the Golgi apparatus and intracellular traffic. As retinoic acid and immunotoxins are both in clinical trials for cancer therapy, their combined activity in vivo would be interesting to examine.
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Fleming, Bryan D., and Mitchell Ho. "Development of Glypican-3 Targeting Immunotoxins for the Treatment of Liver Cancer: An Update." Biomolecules 10, no. 6 (June 20, 2020): 934. http://dx.doi.org/10.3390/biom10060934.

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Hepatocellular carcinoma (HCC) accounts for most liver cancers and represents one of the deadliest cancers in the world. Despite the global demand for liver cancer treatments, there remain few options available. The U.S. Food and Drug Administration (FDA) recently approved Lumoxiti, a CD22-targeting immunotoxin, as a treatment for patients with hairy cell leukemia. This approval helps to demonstrate the potential role that immunotoxins can play in the cancer therapeutics pipeline. However, concerns have been raised about the use of immunotoxins, including their high immunogenicity and short half-life, in particular for treating solid tumors such as liver cancer. This review provides an overview of recent efforts to develop a glypican-3 (GPC3) targeting immunotoxin for treating HCC, including strategies to deimmunize immunotoxins by removing B- or T-cell epitopes on the bacterial toxin and to improve the serum half-life of immunotoxins by incorporating an albumin binding domain.
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Dieffenbach, Michael, and Ira Pastan. "Mechanisms of Resistance to Immunotoxins Containing Pseudomonas Exotoxin A in Cancer Therapy." Biomolecules 10, no. 7 (June 30, 2020): 979. http://dx.doi.org/10.3390/biom10070979.

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Immunotoxins are a class of targeted cancer therapeutics in which a toxin such as Pseudomonas exotoxin A (PE) is linked to an antibody or cytokine to direct the toxin to a target on cancer cells. While a variety of PE-based immunotoxins have been developed and a few have demonstrated promising clinical and preclinical results, cancer cells frequently have or develop resistance to these immunotoxins. This review presents our current understanding of the mechanism of action of PE-based immunotoxins and discusses cellular mechanisms of resistance that interfere with various steps of the pathway. These steps include binding of the immunotoxin to the target antigen, internalization, intracellular processing and trafficking to reach the cytosol, inhibition of protein synthesis through ADP-ribosylation of elongation factor 2 (EF2), and induction of apoptosis. Combination therapies that increase immunotoxin action and overcome specific mechanisms of resistance are also reviewed.
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Weldon, John E., Laiman Xiang, Oleg Chertov, Inger Margulies, Robert J. Kreitman, David J. FitzGerald, and Ira Pastan. "A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity." Blood 113, no. 16 (April 16, 2009): 3792–800. http://dx.doi.org/10.1182/blood-2008-08-173195.

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Abstract Immunotoxins based on Pseudomonas exotoxin A (PE) are promising anticancer agents that combine a variable fragment (Fv) from an antibody to a tumor-associated antigen with a 38-kDa fragment of PE (PE38). The intoxication pathway of PE immunotoxins involves receptor-mediated internalization and trafficking through endosomes/lysosomes, during which the immunotoxin undergoes important proteolytic processing steps but must otherwise remain intact for eventual transport to the cytosol. We have investigated the proteolytic susceptibility of PE38 immunotoxins to lysosomal proteases and found that cleavage clusters within a limited segment of PE38. We subsequently generated mutants containing deletions in this region using HA22, an anti-CD22 Fv-PE38 immunotoxin currently undergoing clinical trials for B-cell malignancies. One mutant, HA22-LR, lacks all identified cleavage sites, is resistant to lysosomal degradation, and retains excellent biologic activity. HA22-LR killed chronic lymphocytic leukemia cells more potently and uniformly than HA22, suggesting that lysosomal protease digestion may limit immunotoxin efficacy unless the susceptible domain is eliminated. Remarkably, mice tolerated doses of HA22-LR at least 10-fold higher than lethal doses of HA22, and these higher doses exhibited markedly enhanced antitumor activity. We conclude that HA22-LR advances the therapeutic efficacy of HA22 by using an approach that may be applicable to other PE-based immunotoxins.
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Zovickian, John, and Richard J. Youle. "Efficacy of intrathecal immunotoxin therapy in an animal model of leptomeningeal neoplasia." Journal of Neurosurgery 68, no. 5 (May 1988): 767–74. http://dx.doi.org/10.3171/jns.1988.68.5.0767.

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✓ Immunotoxins comprise a new class of cell-type specific cytotoxic reagents which consist of a monoclonal antibody linked to a protein toxin. This report examines the efficacy of intrathecal immunotoxin therapy for the treatment of tumors of the cerebrospinal fluid compartment. A syngeneic animal model of leptomeningeal neoplasia was developed in which percutaneous inoculation of L2C tumor cells into the cisterna magna of Strain 2 guinea pigs produced disseminated leptomeningeal and intraventricular leukemia and death. Percutaneous intracisternal injecton of 2 µg of an anti-idiotype monoclonal antibody (M6)-intact ricin immunotoxin 24 hours following intracisternal inoculation of 105 L2C cells (10,000 times the lethal dose) produced prolonged survival (p < 0.005) of tumor-bearing animals. The immunotoxin therapy caused no detectable toxicity. Intracisternal injection of either M6 monoclonal antibody alone or a nonspecific control immunotoxin had no therapeutic effect. The observed extension of survival times in immunotoxin-treated animals corresponds to a median 2- to 3-log (99% to 99.9%) and, in some animals, possibly a 5-log (99.999%) or greater kill of tumor cells. These results support a possible role for immunotoxins in the clinical treatment of central nervous system neoplastic disease involving compartments (intrathecal, intraventricular, or cystic tumor).
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Guerrero-Ochoa, Patricia, Diederich Aguilar-Machado, Raquel Ibáñez-Pérez, Javier Macías-León, Ramón Hurtado-Guerrero, Javier Raso, and Alberto Anel. "Production of a Granulysin-Based, Tn-Targeted Cytolytic Immunotoxin Using Pulsed Electric Field Technology." International Journal of Molecular Sciences 21, no. 17 (August 26, 2020): 6165. http://dx.doi.org/10.3390/ijms21176165.

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Granulysin is a protein present in the granules of human cytotoxic T lymphocytes (CTL) and natural killer (NK) cells, with cytolytic activity against microbes and tumors. Previous work demonstrated the therapeutic effect of the intratumoral injection of recombinant granulysin and of the systemic injection of an immunotoxin between granulysin and the anti-carcinoembryonic antigen single-chain Fv antibody fragment MFE23, which were produced in the yeast Pichia pastoris. In the present work, we developed a second immunotoxin combining granulysin and the anti-Tn antigen single-chain Fv antibody fragment SM3, that could have a broader application in tumor treatment than our previous immunotoxin. In addition, we optimized a method based on electroporation by pulsed electric field (PEF) to extract the remaining intracellular protein from yeast, augmenting the production and purificiation yield. The immunotoxin specifically recognized the Tn antigen on the cell surface. We also compared the thermal stability and the cytotoxic potential of the extracellular and intracellular immunotoxins on Tn-expressing human cell lines, showing that they were similar. Moreover, the bioactivity of both immunotoxins against several Tn+ cell lines was higher than that of granulysin alone.
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Bregni, M., S. Siena, A. Formosa, DA Lappi, D. Martineau, F. Malavasi, B. Dorken, G. Bonadonna, and AM Gianni. "B-cell restricted saporin immunotoxins: activity against B-cell lines and chronic lymphocytic leukemia cells." Blood 73, no. 3 (February 15, 1989): 753–62. http://dx.doi.org/10.1182/blood.v73.3.753.753.

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Abstract B cell-restricted immunotoxins were constructed by conjugating anti-B monoclonal antibodies to saporin, the major ribosome inactivating protein from the seeds of the plant Saponaria officinalis. HD37-SAP is directed against CD19, the broadest B cell-specific determinant. HD39- SAP and HD6-SAP recognize two different epitopes on the CD22 molecule, an antigen present on the cell surface of B cells at late stages of differentiation. All three immunotoxins inhibited DNA synthesis and protein synthesis in target B lymphoma cells with a dose-related effect, in short incubation times and in the absence of potentiators. A clonogenic assay demonstrated that all immunotoxins could eliminate more than two logs of clonogenic malignant B cells with a two-hour incubation at concentrations not toxic to cells not bearing target antigens. The immunotoxin activity was evaluated by DNA synthesis inhibition in fresh B-chronic lymphocytic leukemia cells (B-CLL) stimulated to proliferate by incubation with an antibody specific for the receptor of C3b complement component (CR1) plus B cell growth factor. B-CLL cell DNA synthesis was actively inhibited by treatment at low immunotoxin concentration without need of potentiators. Immunotoxins exerted their effect also in whole blood of CLL patients under conditions achievable in vivo. We conclude that B cell-restricted immunotoxins HD37-SAP, HD39-SAP, and HD6-SAP are good candidates for in vivo therapy of B-cell malignancies.
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Bregni, M., S. Siena, A. Formosa, DA Lappi, D. Martineau, F. Malavasi, B. Dorken, G. Bonadonna, and AM Gianni. "B-cell restricted saporin immunotoxins: activity against B-cell lines and chronic lymphocytic leukemia cells." Blood 73, no. 3 (February 15, 1989): 753–62. http://dx.doi.org/10.1182/blood.v73.3.753.bloodjournal733753.

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B cell-restricted immunotoxins were constructed by conjugating anti-B monoclonal antibodies to saporin, the major ribosome inactivating protein from the seeds of the plant Saponaria officinalis. HD37-SAP is directed against CD19, the broadest B cell-specific determinant. HD39- SAP and HD6-SAP recognize two different epitopes on the CD22 molecule, an antigen present on the cell surface of B cells at late stages of differentiation. All three immunotoxins inhibited DNA synthesis and protein synthesis in target B lymphoma cells with a dose-related effect, in short incubation times and in the absence of potentiators. A clonogenic assay demonstrated that all immunotoxins could eliminate more than two logs of clonogenic malignant B cells with a two-hour incubation at concentrations not toxic to cells not bearing target antigens. The immunotoxin activity was evaluated by DNA synthesis inhibition in fresh B-chronic lymphocytic leukemia cells (B-CLL) stimulated to proliferate by incubation with an antibody specific for the receptor of C3b complement component (CR1) plus B cell growth factor. B-CLL cell DNA synthesis was actively inhibited by treatment at low immunotoxin concentration without need of potentiators. Immunotoxins exerted their effect also in whole blood of CLL patients under conditions achievable in vivo. We conclude that B cell-restricted immunotoxins HD37-SAP, HD39-SAP, and HD6-SAP are good candidates for in vivo therapy of B-cell malignancies.
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Dissertations / Theses on the topic "Immunotoxine"

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Kleinschmidt, Martin. "Design modularer Immunotoxine unter Verwendung polyionischer Fusionspeptide." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973422343.

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Buret, Sylvie. "Les immunotoxines." Paris 5, 1989. http://www.theses.fr/1989PA05P170.

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Heisler, Iring. "Bedeutung spaltbarer Peptidlinker für die Funktion rekombinanter Saporin-EGF-Immunotoxine." [S.l.] : [s.n.], 2003. http://www.diss.fu-berlin.de/2003/210/index.html.

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Posch, Maximilian. "Neue Ansätze zur zielgerichteten Behandlung solider Tumoren." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2002. http://dx.doi.org/10.18452/14828.

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Eingeschränkte Apoptose trägt zur Tumorentstehung und zur Entwicklung von Chemoresistenz bei, da die Apoptose normalerweise Zellen mit genetischen Schäden oder malignem Potential eliminiert. Dieser Prozess, der bereits für viele unterschiedlichen Tumorzellen nachgewiesen wurde, limitiert häufig die Behandelbarkeit maligner Erkrankungen und ist somit ein grosses Problem in der heutigen Krebsbehandlung. Es existieren unterschiedliche Ansätze die Auslöseschwelle für die Apoptose zu vermindern, um so Chemotherapie-resistente Tumorzellen zu eliminieren. Im ersten Teil dieser Arbeit wurde das anti-tumorale Potential des bispezifischen 4625 Antisense-Oligonukleotid in Kombination mit chemotherapeutischen Wirkstoffen in vitro und in vivo untersucht. Der zweite Teil beschreibt die Ergebnisse mit dem rekombinanten Ep-CAM spezifischen scFv Immunotoxin 4D5MOC-B-ETA in vitro und im Modell der Nacktmaus. Bcl-2 und Bcl-xL sind Inhibitoren der Apoptose, die von vielen malignen Tumorzellen überexprimiert werden. Das Herunterregulieren von Bcl-2 oder Bcl-xL erniedrigt die apoptotische Auslöseschwelle und Tumorzellen sterben durch programmierten Zelltod. Das 4625 Antisense Oligonukleotid richtet sich gegen eine Region hoher Homologie in der bcl-2/bcl-xL mRNA und hemmt simultan die Expression von Bcl-2 und Bcl-xL. Die durch das bispezifische 4625 Antisense gehemmte Expression von Bcl-2 und Bcl-xL in Tumorzellen unterschiedlicher Histologie zeigen die Ergebnisse der Immuno-Blots. Weiterhin führt 4625 zur dosisabhängigen Wachstumshemmung von Krebszellen bei Konzentrationen von 75-600 nM im MTT Assay. Für die Kombinationsbehandlung wurden Paclitaxel und 5-FU jeweils als Standardtherapie zur Behandlung von Brust- und kolorektalem Karzinom gewählt. Die ip. Applikation von 20mg/kg KG 4625 mit oder ohne Paclitaxel/5-FU führte zu einem verlangsamten Wachstum humaner Tumor Xenotransplantaten in Nacktmäusen, im Vergleich mit denen die mit dem Kontrolloligonukleotid 4626 mit oder ohne Chemotherapie behandelt wurden. Bcl-2 und Bcl-xL spielen unterschiedliche Rollen in der Tumorentwicklung und sind häufig heterogen in soliden Tumorgeweben exprimiert. Diese Daten zeigen, daß die moderne Antisense Technologie eine wirksame Methode zur Herunterregulierung zweier Hauptinhibitoren der Apoptose mit einem einzigen Oligonukleotid darstellt, wovon möglicherweise mehr Patienten mit malignen Erkrankungen in Zukunft profitieren könnten. Die Expression bestimmter Zelloberflächenmoleküle ist ein häufiger Prozess in vielen soliden Tumoren, was sie für eine zielgerichtete Antikörpertherapie angreifbar macht. Das epitheliale Glykoprotein-2 (Ep-CAM) wird reichlich von epithelialen Tumoren und Tumorzellinien exprimiert. Die antineoplastische Aktivität des Ep-CAM spezifischen 4D5MOC-B-ETA Immunotoxin wird im zweiten Teil dieser Arbeit beschrieben. In vitro hemmt 4D5MOC-B-ETA spezifisch die Proteinsynthese in Ep-CAM positiven Krebszellen unterschiedlichen histologischen Ursprungs ermittelt durch [H3]leucin Aufnahme und reduzierte die Überlebensrate dieser Zellen in Konzentrationen von 0.01 bis 1 pM. Ep-CAM negative Zellen wurden als negative Kontrolle genutzt und blieben durch das Immunotoxin in Konzentration bis zu 10.000 pM unversehrt, was dessen hochgradige Ep-CAM Spezifität beweist. Die tägliche Applikation von 0.01 mg 4D5MOC-B-ETA im Nacktmausmodell führte zu einem Schrumpfen der Tumor Xenotransplantate während der Behandlungszeit. Diese hohe Wirksamkeit des scFv Immunotoxin bedarf weiterer Beachtung in der zukünftigen Krebstherapie.
Impaired apoptosis contributes to cancer development and resistance towards chemotherapy, since apoptosis normally eliminates cells with damaged DNA or increased malignant potential. The increased resistance towards cell death often limits therapeutic options in the clinic and is one major problemin current tumor therapy. Different approaches, which have been described so far intend to lower the apoptotic threshold in order to eliminate chemoresistant cancer cells. In the first part of this thesis the anti-tumor potential of the bispecific 4625 oligonucleotide was investigated in combination with chemotherapeutic drugs in vitro and in vivo. The second part describes the anti tumor activity of the recombinant Ep-CAM specific scFv immunotoxin 4D5MOC-B-ETA in vitro and in nude mice. Bcl-2 and Bcl-xL are inhibitors of apoptosis frequently overexpressed in malignant tumor cells. Downregulation of either Bcl-2 or Bcl-xL lowers the apoptotic threshold and tumor cells undergo apoptosis. The 4625 antisense oligonucleotide targets a region of high homology shared by the bcl-2/bcl-xL mRNAs and simultaneously downregulates Bcl-2 and Bcl-xL. The 4625 bispecific Antisense Oligonucleotide downregulates Bcl-2 and Bcl-xL expression in cancer cell lines of diverse histological origins assessed by immuno blotting. It further leads to proliferation inhibition of cancer cells at concentrations ranging from 75-600 nM in MTT assay in a dose-dependent manner. For combination experiments Paclitaxel and 5-FU were chosen as standard therapy for the treatment of breast and colorectal cancer, respectively. The ip. application of 20 mg/kg 4625 with or without Paclitaxel/5-FU led to a growth inhibition of established human carcinomas xenografts in nude mice, relative to those treated with the 4626 control oligonucleotide with or without chemotherapy. Bcl-2 and Bcl-xL play nonredundant roles in tumor growth and are often heterogeneously expressed in solid tumor tissues. This data suggests that state-of-the-art antisense technology offers a potent approach to inhibit the expression of the two major anti-apoptotic proteins Bcl-2 and Bcl-xL with one single oligonucleotide, which could make additional patients benefit from a treatment with this antisense compound. Expression of certain cell surface antigens is a common process in many solid tumors making them suitable for targeted antibody therapy. The epithelial glycoprotein-2 (Ep-CAM) is abundantly expressed on carcinomas and cancer cell lines. The anti tumor activity of the Ep-CAM specific 4D5MOC-B-ETA immunotoxin is described in the second part. In vitro 4D5MOC-B-ETA specifically inhibited protein synthesis in Ep-CAM positive cancer cells of diverse histological origin assessed by [H3]leucin incorporation and reduced cell viability with IC50 ranging from 0.01 to 1 pM. Ep-CAM negative cells were taken as control and were not harmed by the immunotoxin at concentrations up to 10.000 pM, which proves the 4D5MOC-B-ETA Ep-CAM specific potential. In athymic mice, the systemic application of 4D5MOC-B-ETA at a dose of 0.01 mg per day resulted in the regression of established tumor xenografts during the time of treatment. This highly potent anti-tumor activity of a recombinant scFv immunotxin deserves further attention for use in cancer therapy.
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Jaffrézou, Jean-Pierre. "Reversion de la resistance pleiotropique et activation des immunotoxines : participation du metabolisme sphingolipidique." Toulouse 3, 1991. http://www.theses.fr/1991TOU30115.

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L'existence de molecules susceptibles a la fois de reverser in vitro la resistance mdr et d'activer les immunotoxines souleve un double interet d'un point de vue a la fois mecanistique et pharmacologique. Ceci suggere donc que ces agents interviennent au niveau du transport et/ou de la degradation intracellulaire. Il est en effet possible que les perturbations du metabolisme lipidiques induite par ces agents, et plus specifiquement celle de la sphingomyeline, sont a l'origine de leur activite
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The, Dean Timothy Neal. "Immunotoxic effects of aldicarb /." This resource online, 1990. http://scholar.lib.vt.edu/theses/available/etd-03142009-040641/.

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Keller, Jutta. "Entwicklung molekularer Adapter zur Optimierung von Immunotoxinen." [S.l.] : [s.n.], 2002. http://www.diss.fu-berlin.de/2002/243/index.html.

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Casellas, Pierre. "Immunotoxines molécules informatiques programmées à vocation cytotoxique /." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37603672m.

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Dean, Timothy Neal. "The immunotoxic effects of aldicarb." Thesis, Virginia Tech, 1990. http://hdl.handle.net/10919/41612.

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Rostaing-Capaillon, Odile. "Optimisation de l'efficacité antitumorale des immunotoxines "in vivo"." Montpellier 2, 1990. http://www.theses.fr/1990MON20188.

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L'utilisation des immunotoxines in vivo rencontre de nombreuses difficultes dont les principales sont une faible localisation tumorale apres injection intraveineuses et une activite cytotoxique insuffisante. L'amelioration de la capacite de ciblage des immunotoxines a chaine a de ricine eeeeea ete realisee grace a l'utilisation de fragments d'anticorps f(ab)2 et fab qui reduisent la taillee de l'immunotoxine et facilitent son extravasation et grace a la deglycosylation de la chaine a qui ralentit considerablement la clairance plasmatique de l'immunotoxine. Toutefois, seule l'injection intratumorale permet d'obtenir une saturation des antigenes cibles. Des facteurs specifique et non-specifique sont responsables de l'inactivation du site de fixation de l'anticorps, ce qui limite la capacite de ciblage de l'immunotoxine circulante mais l'activite cytotoxique des immunotoxines associees aux cellules tumorales est preservee. L'efficacite cytotoxique des immunotoxines in vivo est liee au nombre de molecules fixees par cellule. Cependant, meme apres saturation des antigenes cibles, l'effet antitumoral reste limite. L'injection intratumorale du conjugue albumine-monensine permet alors d'eradiquer une large masse tumorale constituee d'au moins huit cent millions de cellules par souris, meme si la localisation tumorale de l'immunotoxine est reduite
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Books on the topic "Immunotoxine"

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Frankel, Arthur E., ed. Immunotoxins. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9.

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Frankel, Arthur E., ed. Clinical Applications of Immunotoxins. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-72153-3.

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Hall, Walter A. Immunotoxin Methods and Protocols. New Jersey: Humana Press, 2000. http://dx.doi.org/10.1385/1592591140.

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Phillips, Gail Lewis, ed. Antibody-Drug Conjugates and Immunotoxins. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-5456-4.

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Verma, Rama Shanker, and Benjamin Bonavida, eds. Resistance to Immunotoxins in Cancer Therapy. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-17275-0.

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Phan, Văn Chi. Trichobakin và Immunotoxin tái tổ hợp. Hà Nội: Nhà xuất bản Khoa học tự nhiên và công nghệ, 2008.

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Grawunder, Ulf, and Stefan Barth, eds. Next Generation Antibody Drug Conjugates (ADCs) and Immunotoxins. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46877-8.

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Magerstadt, Michael. Antibody conjugates and malignant disease. Boca Raton: CRC Press, 1991.

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A, Lappi Douglas, ed. Suicide transport and immunolesioning. Austin: R.G. Landes, 1994.

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10

Ramakrishnan, S. Cytotoxic conjugates. Austin: R.G. Landes Co., 1993.

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Book chapters on the topic "Immunotoxine"

1

Houston, L. L. "Introduction." In Immunotoxins, 1–7. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_1.

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Vallera, Daniel A., and Dorothea E. Myers. "Immunotoxins containing ricin." In Immunotoxins, 141–59. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_10.

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FitzGerald, David J., Mark C. Willingham, and Ira Pastan. "Pseudomonas exotoxin — Immunotoxins." In Immunotoxins, 161–73. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_11.

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Lambert, John M., Walter A. Blättler, Gordon D. McIntyre, Victor S. Goldmacher, and Charles F. Scott. "Immunotoxins containing single chain ribosome-inactivating proteins." In Immunotoxins, 175–209. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_12.

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Marsh, Jon W., Kasturi Srinivasachar, and David M. Neville. "Antibody-toxin conjugation." In Immunotoxins, 213–37. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_13.

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Wawrzynczak, Edward J., and Philip E. Thorpe. "Effect of chemical linkage upon the stability and cytotoxic activity of A chain immunotoxins." In Immunotoxins, 239–51. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_14.

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Bjorn, Michael J., and C. L. Villemez. "Immunotoxins: Selection of cell-surface antigens and their corresponding monoclonal antibodies." In Immunotoxins, 255–77. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_15.

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Oeltmann, Thomas N., and Ronald G. Wiley. "Hormone, lectin and toxin-toxin conjugates." In Immunotoxins, 281–95. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_16.

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Raso, Vic. "Growth factors and other ligands." In Immunotoxins, 297–320. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_17.

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Lambert, John M., and Walter A. Blättler. "Purification and biochemical characterization of immunotoxins." In Immunotoxins, 323–48. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_18.

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Conference papers on the topic "Immunotoxine"

1

Wiiger, Merete T., Øystein Fodstad, and Yvonne Andersson. "Abstract 772: Targeted cancer therapy with immunotoxins." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-772.

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Kreitman, Robert, Daniel Gorelik, Maryalice Stetler-Stevenson, Constance M. Yuan, Hao-Wei Wang, Hong Zhou, Katherine Potocka, Erin Fykes, Evgeny Arons, and Ira Pastan. "Abstract CN07-03: Recombinant immunotoxins for hematologic malignancies." In Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-cn07-03.

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Ho, Mitchell, Bryan D. Fleming, Tim F. Greten, and Ira Pastan. "Abstract CN07-02: Immunotoxins targeting GPC3 for liver cancer." In Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-cn07-02.

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Simon, Nathan, Antonella Antignani, Stephen Hewitt, Massimo Gadina, Masanori Onda, Christine Alewine, and David Joseph Fitzgerald. "Abstract 3023: The antitumor activity of immunotoxins is enhanced by tofacitinib." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3023.

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Manning, Michael L., Emily Mason-Osann, Masanori Onda, and Ira Pastan. "Abstract 2586: Bortezomib reduces preexisting antibodies to recombinant immunotoxins in mice." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2586.

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Hamakubo, Takao. "Enhancement of immunotoxin effect on tumor with photodynamic therapy (Conference Presentation)." In 17th International Photodynamic Association World Congress, edited by Tayyaba Hasan. SPIE, 2019. http://dx.doi.org/10.1117/12.2527654.

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Liu, Xiu Fen, Laiman Xiang, Marco Prunotto, Gerhard Niederfellner, and Ira Pastan. "Abstract 1290: Actinomycin D enhanced immunotoxin RG7787 killing of cancer cells." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1290.

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Shen, Luqun, Kelsey Weigel, Clayton Thomas, Lauren Drapalik, Zachary T. Schafer, and Shaun Lee. "Abstract 347: Developing a novel immunotoxin that targets cells overexpressing ErbB2." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-347.

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Bostad, Monica, Kristian Berg, Anders Høgset, and Pål Kristian Selbo. "Abstract 3381: Photochemical internalization (PCI) of immunotoxins targeting cancer stem cell markers." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3381.

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Berstad, Maria Eb, Kristian Berg, Michael Rosenblum, Yu Cao, James D. Marks, and Anette Weyergang. "Abstract 3635: Improved efficacy of HER2 targeted-immunotoxins using photochemical internalization (PCI)." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3635.

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Reports on the topic "Immunotoxine"

1

Yotnda, Patricia. Enhanced Eradication of Lymphoma by Tumor-Specific Cytotoxic T-Cells Secreting an Engineered Tumor-Specific Immunotoxin. Fort Belvoir, VA: Defense Technical Information Center, June 2010. http://dx.doi.org/10.21236/ada541224.

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Frazier, Donald E., and Melinda J. Tarr. Investigation of the Hepatotoxic and Immunotoxic Effects of the Peroxisome Proliferator Perfluorodecanoic Acid. Fort Belvoir, VA: Defense Technical Information Center, April 1991. http://dx.doi.org/10.21236/ada237787.

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Tarr, Melinda J., and Larry E. Mathes. Investigation of the Hepatotoxic and Immunotoxic Effects of the Peroxisome Proliferator Perfluorodecanoic Acid. Fort Belvoir, VA: Defense Technical Information Center, April 1992. http://dx.doi.org/10.21236/ada250176.

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