3 results on '"Florence Durieux"'
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2. Methylglyoxal, a glycolysis side-product, induces Hsp90 glycation and YAP-mediated tumor growth and metastasis
- Author
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Marie-Julie Nokin, Florence Durieux, Paul Peixoto, Barbara Chiavarina, Olivier Peulen, Arnaud Blomme, Andrei Turtoi, Brunella Costanza, Nicolas Smargiasso, Dominique Baiwir, Jean L Scheijen, Casper G Schalkwijk, Justine Leenders, Pascal De Tullio, Elettra Bianchi, Marc Thiry, Koji Uchida, David A Spiegel, James R Cochrane, Craig A Hutton, Edwin De Pauw, Philippe Delvenne, Dominique Belpomme, Vincent Castronovo, and Akeila Bellahcène
- Subjects
carbonyl stress ,glyoxalase 1 ,LATS1 ,breast cancer ,methylglyoxal ,YAP ,Medicine ,Science ,Biology (General) ,QH301-705.5 - Abstract
Metabolic reprogramming toward aerobic glycolysis unavoidably induces methylglyoxal (MG) formation in cancer cells. MG mediates the glycation of proteins to form advanced glycation end products (AGEs). We have recently demonstrated that MG-induced AGEs are a common feature of breast cancer. Little is known regarding the impact of MG-mediated carbonyl stress on tumor progression. Breast tumors with MG stress presented with high nuclear YAP, a key transcriptional co-activator regulating tumor growth and invasion. Elevated MG levels resulted in sustained YAP nuclear localization/activity that could be reverted using Carnosine, a scavenger for MG. MG treatment affected Hsp90 chaperone activity and decreased its binding to LATS1, a key kinase of the Hippo pathway. Cancer cells with high MG stress showed enhanced growth and metastatic potential in vivo. These findings reinforce the cumulative evidence pointing to hyperglycemia as a risk factor for cancer incidence and bring renewed interest in MG scavengers for cancer treatment.
- Published
- 2016
- Full Text
- View/download PDF
3. Methylglyoxal, a glycolysis side-product, induces Hsp90 glycation and YAP-mediated tumor growth and metastasis
- Author
-
Barbara Chiavarina, Brunella Costanza, Justine Leenders, Philippe Delvenne, Elettra Bianchi, James R. Cochrane, Koji Uchida, Pascal de Tullio, Paul Peixoto, Akeila Bellahcene, Craig A. Hutton, Olivier Peulen, Dominique Baiwir, Marc Thiry, Casper G. Schalkwijk, Vincent Castronovo, Andrei Turtoi, Dominique Belpomme, Arnaud Blomme, Florence Durieux, Jean L.J.M. Scheijen, Nicolas Smargiasso, Marie-Julie Nokin, Edwin De Pauw, David Spiegel, Promovendi CD, Interne Geneeskunde, MUMC+: MA Alg Interne Geneeskunde (9), RS: CARIM - R3.01 - Vascular complications of diabetes and the metabolic syndrome, Université de Liège, Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Maastricht University [Maastricht], Cardiovascular Research Institute Maastricht (CARIM), Centre Hospitalier Universitaire de Liège (CHU-Liège), Nagoya University, Yale University [New Haven], University of Melbourne, and Association for Research and Treatments Against Cancer (ARTAC)
- Subjects
Glycation End Products, Advanced ,0301 basic medicine ,Glycosylation ,Metastasis ,chemistry.chemical_compound ,Lactoylglutathione lyase ,Glycation ,cell biology ,methylglyoxal ,Neoplasm Metastasis ,Biology (General) ,cancer biology ,General Neuroscience ,MESH: Glycation End Products, Advanced ,Methylglyoxal ,General Medicine ,Pyruvaldehyde ,MESH: Glycosylation ,Aerobiosis ,LATS1 ,3. Good health ,carbonyl stress ,MESH: Glycolysis ,Medicine ,YAP ,Glycolysis ,Research Article ,medicine.medical_specialty ,MESH: Pyruvaldehyde ,MESH: Cell Line, Tumor ,QH301-705.5 ,Science ,chicken ,Breast Neoplasms ,[SDV.CAN]Life Sciences [q-bio]/Cancer ,Biology ,MESH: Phosphoproteins ,glyoxalase 1 ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,breast cancer ,Cell Line, Tumor ,MESH: Aerobiosis ,MESH: Cell Proliferation ,Internal medicine ,MESH: HSP90 Heat-Shock Proteins ,medicine ,Humans ,HSP90 Heat-Shock Proteins ,human ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,mouse ,Adaptor Proteins, Signal Transducing ,Cell Proliferation ,MESH: Adaptor Proteins, Signal Transducing ,Hippo signaling pathway ,MESH: Humans ,General Immunology and Microbiology ,YAP-Signaling Proteins ,Phosphoproteins ,medicine.disease ,MESH: Neoplasm Metastasis ,030104 developmental biology ,Endocrinology ,chemistry ,Tumor progression ,Anaerobic glycolysis ,MESH: Protein Processing, Post-Translational ,Cancer cell ,biology.protein ,Cancer research ,Protein Processing, Post-Translational ,MESH: Breast Neoplasms ,Transcription Factors - Abstract
Metabolic reprogramming toward aerobic glycolysis unavoidably induces methylglyoxal (MG) formation in cancer cells. MG mediates the glycation of proteins to form advanced glycation end products (AGEs). We have recently demonstrated that MG-induced AGEs are a common feature of breast cancer. Little is known regarding the impact of MG-mediated carbonyl stress on tumor progression. Breast tumors with MG stress presented with high nuclear YAP, a key transcriptional co-activator regulating tumor growth and invasion. Elevated MG levels resulted in sustained YAP nuclear localization/activity that could be reverted using Carnosine, a scavenger for MG. MG treatment affected Hsp90 chaperone activity and decreased its binding to LATS1, a key kinase of the Hippo pathway. Cancer cells with high MG stress showed enhanced growth and metastatic potential in vivo. These findings reinforce the cumulative evidence pointing to hyperglycemia as a risk factor for cancer incidence and bring renewed interest in MG scavengers for cancer treatment. DOI: http://dx.doi.org/10.7554/eLife.19375.001
- Published
- 2016
- Full Text
- View/download PDF
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