Search

Your search keyword '"Bal-Mahieu, Christine"' showing total 13 results
Start Over Author "Bal-Mahieu, Christine"
13 results on '"Bal-Mahieu, Christine"'

4. Low level of baseline circulating VEGF-A is associated with better outcome in patients with vascular sarcomas receiving sorafenib: an ancillary study from a phase II trial

Author

Penel, Nicolas, Ray-Coquard, Isabelle, Bal-Mahieu, Christine, Chevreau, Christine, Le Cesne, Axel, Italiano, Antoine, Bompas, Emmanuelle, Clisant, Stéphanie, Baldeyrou, Brigitte, Lansiaux, Amélie, Robin, Yves-Marie, Bay, Jacques-Olivier, Piperno-Neumann, Sophie, Blay, Jean-Yves, and Fournier, Charles

Published
2014
Full Text
View/download PDF

5. Evofosfamide Is Effective against Pediatric Aggressive Glioma Cell Lines in Hypoxic Conditions and Potentiates the Effect of Cytotoxic Chemotherapy and Ionizing Radiations

Author

Bailleul, Quentin, primary, Navarin, Pauline, additional, Arcicasa, Mélanie, additional, Bal-Mahieu, Christine, additional, Carcaboso, Angel Montero, additional, Le Bourhis, Xuefen, additional, Furlan, Alessandro, additional, Meignan, Samuel, additional, and Leblond, Pierre, additional

Published
2021
Full Text
View/download PDF

6. Synthesis, Structure, and Antiproliferative Activity of Ruthenium(II) Arene Complexes of Indenoisoquinoline Derivatives

Author

Wambang, Nathalie, primary, Schifano-Faux, Nadège, additional, Martoriati, Alain, additional, Henry, Natacha, additional, Baldeyrou, Brigitte, additional, Bal-Mahieu, Christine, additional, Bousquet, Till, additional, Pellegrini, Sylvain, additional, Meignan, Samuel, additional, Cailliau, Katia, additional, Goossens, Jean-François, additional, Bodart, Jean-François, additional, T. Ndifon, Peter, additional, and Pélinski, Lydie, additional

Published
2016
Full Text
View/download PDF

7. PCM-13THE HYPOXIA-ACTIVATED PRODRUG EVOFOSFAMIDE (TH-302) IS EFFICACIOUS IN PEDIATRIC HIGH GRADE GLIOMA CELL LINES AS A MONOTHERAPY AND IN COMBINATION WITH CHEMOTHERAPIES

Author

Leblond, Pierre, primary, Navarin, Pauline, additional, Arcicasa, Mélanie, additional, Bal-Mahieu, Christine, additional, Lemahieu, Nicole, additional, Völkel, Pamela, additional, Lartigau, Eric, additional, Angrand, Pierre-Olivier, additional, and Meignan, Samuel, additional

Published
2016
Full Text
View/download PDF

8. New selective carbonic anhydrase IX inhibitors: Synthesis and pharmacological evaluation of diarylpyrazole-benzenesulfonamides

Author

UCL - SSS/LDRI - Louvain Drug Research Institute, Rogez-Florent, Tiphaine, Meignan, Samuel, Foulon, Catherine, Six, Perrine, Gros, Abigaëlle, Bal-Mahieu, Christine, Supuran, Claudiu T., Scozzafava, Andrea, Frédérick, Raphaël, Masereel, Bernard, Depreux, Patrick, Lansiaux, Amélie, Goossens, Jean-François, Gluszok, Sébastien, Goossens, Laurence, UCL - SSS/LDRI - Louvain Drug Research Institute, Rogez-Florent, Tiphaine, Meignan, Samuel, Foulon, Catherine, Six, Perrine, Gros, Abigaëlle, Bal-Mahieu, Christine, Supuran, Claudiu T., Scozzafava, Andrea, Frédérick, Raphaël, Masereel, Bernard, Depreux, Patrick, Lansiaux, Amélie, Goossens, Jean-François, Gluszok, Sébastien, and Goossens, Laurence

Abstract

Carbonic anhydrase (CA) IX expression is increased upon hypoxia and has been proposed as a therapeutic target since it has been associated with poor prognosis, tumor progression and pH regulation. We report the synthesis and the pharmacological evaluation of a new class of human carbonic anhydrase (hCA) inhibitors, 4-(5-aryl-2-hydroxymethyl-pyrazol-1-yl)-benzenesulfonamides. A molecular modeling study was conducted in order to simulate the binding mode of this new family of enzyme inhibitors within the active site of hCA IX. Pharmacological studies revealed high hCA IX inhibitory potency in the parameters nanomolar range. This study showed that the position of sulfonamide group in meta of the 1-phenylpyrazole increase a selectivity hCA IX versus hCA II of our compounds. An in vitro antiproliferative screening has been performed on the breast cancer MDA-MB-231 cell using doxorubicin as cytotoxic agent and in presence of selected CA IX inhibitor. The results shown that the cytotoxic efficiency of doxorubicin in an hypoxic environment, expressed in IC 50 value, is restored at 20% level with 1 μM CA IX inhibitor. © 2012 Elsevier Ltd. All rights reserved.

Published
2013

9. Low level of baseline circulating VEGF-A is associated with better outcome in patients with vascular sarcomas receiving sorafenib: an ancillary study from a phase II trial

Author

Penel, Nicolas, primary, Ray-Coquard, Isabelle, additional, Bal-Mahieu, Christine, additional, Chevreau, Christine, additional, Le Cesne, Axel, additional, Italiano, Antoine, additional, Bompas, Emmanuelle, additional, Clisant, Stéphanie, additional, Baldeyrou, Brigitte, additional, Lansiaux, Amélie, additional, Robin, Yves-Marie, additional, Bay, Jacques-Olivier, additional, Piperno-Neumann, Sophie, additional, Blay, Jean-Yves, additional, and Fournier, Charles, additional

Published
2013
Full Text
View/download PDF

11. Novel Stable Camptothecin Derivatives Replacing the E-Ring Lactone by a Ketone Function Are Potent Inhibitors of Topoisomerase I and Promising Antitumor Drugs

Author

Lansiaux, Amélie, primary, Léonce, Stéphane, additional, Kraus-Berthier, Laurence, additional, Bal-Mahieu, Christine, additional, Mazinghien, Romain, additional, Didier, Sébastien, additional, David-Cordonnier, Marie-Hélène, additional, Hautefaye, Patrick, additional, Lavielle, Gilbert, additional, Bailly, Christian, additional, Hickman, John A., additional, and Pierré, Alain, additional

Published
2007
Full Text
View/download PDF

13. Lamellarin D: a novel potent inhibitor of topoisomerase I.

Author

Facompré M, Tardy C, Bal-Mahieu C, Colson P, Perez C, Manzanares I, Cuevas C, and Bailly C

Subjects
Animals, Antineoplastic Agents chemistry, Cattle, Coumarins chemistry, DNA drug effects, DNA metabolism, DNA Topoisomerases, Type I chemistry, DNA Topoisomerases, Type I metabolism, Enzyme Inhibitors chemistry, Heterocyclic Compounds, 4 or More Rings chemistry, Isoquinolines chemistry, Leukemia P388 drug therapy, Leukemia P388 enzymology, Mice, Models, Molecular, Antineoplastic Agents pharmacology, Coumarins pharmacology, Enzyme Inhibitors pharmacology, Heterocyclic Compounds, 4 or More Rings pharmacology, Isoquinolines pharmacology, Topoisomerase I Inhibitors
Abstract

We report the identification and characterization of a novel potent inhibitor of DNA topoisomerase I: lamellarin D (LAM-D), initially isolated from a marine mollusk, Lamellaria sp., and subsequently identified from various ascidians. This alkaloid, which displays potent cytotoxic activities against multidrug-resistant tumor cell lines and is highly cytotoxic to prostate cancer cells, bears a 6H-[1]benzopyrano[4',3':4,5]pyrrolo[2,1-a]isoquinolin-one pentacyclic planar chromophore, whereas its synthetic 5,6-dehydro analogue, LAM-501, has a significantly tilted structure. DNA binding measurements by absorbance, fluorescence, and electric linear dichroism spectroscopy show that LAM-D is a weak DNA binder that intercalates between bp of the double helix. In contrast, the nonplanar analogue LAM-501 did not bind to DNA and failed to inhibit topoisomerase I. DNA intercalation may be required for the stabilization of topoisomerase I-DNA complexes by LAM-D. In the DNA relaxation assay, LAM-D strongly promoted the conversion of supercoiled DNA into nicked DNA in the presence of topoisomerase I. The marine product was approximately 5 times less efficient than camptothecin (CPT) at stabilizing topoisomerase I-DNA complexes, but interestingly, the two drugs exhibited slightly distinct sequence specificity profiles. Topoisomerase I-mediated DNA cleavage in the presence of LAM-D occurred at some sites common to CPT, but a few specific sites identified with CPT but not with LAM-D or conversely unique sites cleaved by LAM-D but not by CPT were detected. The distinct specificity profiles suggest that LAM-D and CPT interact differently with the topoisomerase I-DNA interface. A molecular modeling analysis provided structural information on the orientation of LAM-D within the topoisomerase I-DNA covalent complex. The marine alkaloid did not induce DNA cleavage by topoisomerase II. Immunoblotting experiments revealed that endogenous topoisomerase I was efficiently trapped on DNA by LAM-D in P388 and CEM leukemia cells. P388/CPT5 and CEM/C2 cell lines, both resistant to CPT and expressing a mutated top1 gene, were cross-resistant to LAM-D. Collectively, the results identify LAM-D as a novel lead candidate for the development of topoisomerase I-targeted antitumor agents.

Published
2003

Catalog

Books, media, physical & digital resources
See catalog results