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43 results on '"Cubedo, Elena"'

15. Abdominal Wall Reconstruction Utilizing the Combination of Absorbable and Permanent Mesh in a Retromuscular Position: A Multicenter Prospective Study

Author

García-Ureña, Miguel Ángel, primary, López-Monclús, Javier, additional, Cuccurullo, Diego, additional, Blázquez Hernando, Luis Alberto, additional, García-Pastor, Providencia, additional, Reggio, Stefano, additional, Jiménez Cubedo, Elena, additional, San Miguel Méndez, Carlos, additional, Cruz Cidoncha, Arturo, additional, and Robin Valle de Lersundi, Alvaro, additional

Published
2018
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22. Blocking the PAH2 domain of Sin3A inhibits tumorigenesis and confers retinoid sensitivity in triple negative breast cancer

Author

Bansal, Nidhi, primary, Bosch, Almudena, additional, Leibovitch, Boris, additional, Pereira, Lutecia, additional, Cubedo, Elena, additional, Yu, Jianshi, additional, Pierzchalski, Keely, additional, Jones, Jace W., additional, Fishel, Melissa, additional, Kane, Maureen, additional, Zelent, Arthur, additional, Waxman, Samuel, additional, and Farias, Eduardo, additional

Published
2016
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23. Colecistitis hemorrágica perforada

Author

Calvo Espino, Pablo, primary, Chaparro Cabezas, María Dolores, additional, Jiménez Cubedo, Elena, additional, Lucena de la Poza, José Luis, additional, and Sánchez Turrión, Víctor, additional

Published
2016
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24. Perforated Hemorrhagic Cholecystitis

Author

Calvo Espino, Pablo, primary, Chaparro Cabezas, María Dolores, additional, Jiménez Cubedo, Elena, additional, Lucena de la Poza, José Luis, additional, and Sánchez Turrión, Víctor, additional

Published
2016
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25. PRDM1/Blimp1 Down-regulates Expression of Germinal Center Genes LMO2 and HGAL

Author

Cubedo, Elena, Maurin, Michelle, Jiang, Xiaoyu, Lossos, Izidore S, and Wright, Kenneth L.

Subjects
B-Lymphocytes, Chromatin Immunoprecipitation, Lymphoma, B-Cell, Transcription, Genetic, Reverse Transcriptase Polymerase Chain Reaction, Microfilament Proteins, Intracellular Signaling Peptides and Proteins, Down-Regulation, LIM Domain Proteins, Article, Recombinant Proteins, Neoplasm Proteins, DNA-Binding Proteins, Repressor Proteins, Genes, Reporter, hemic and lymphatic diseases, Cell Line, Tumor, Proto-Oncogene Proteins, Metalloproteins, Humans, Positive Regulatory Domain I-Binding Factor 1, RNA, Messenger, Promoter Regions, Genetic, Adaptor Proteins, Signal Transducing
Abstract

Human germinal center-associated lymphoma (HGAL) and LIM domain only-2 (LMO2) are proteins highly expressed in germinal center (GC) B lymphocytes. HGAL and LMO2 are also expressed in GC-derived lymphomas and distinguish biologically distinct subgroups of diffuse large B-cell lymphomas (DLBCL) associated with improved survival. However, little is known about their regulation. PRDM1/Blimp1 is a master regulator of terminal B cell differentiation and may also function as a tumor suppressor in the pathogenesis of DLBCL, where it is frequently inactivated by mutations and deletions. We now demonstrate that both HGAL and LMO2 are directly regulated by the transcription repressor PRDM1. In vivo studies demonstrate that PRDM1 directly binds to the recognition sites within the upstream promoters of both HGAL and LMO2. PRDM1 binding suppresses endogenous protein and mRNA levels of HGAL and LMO2. In addition, promoter analysis reveals that site-specific binding of PRDM1 to the promoters is capable of repressing transcriptional activity. This inhibitory effect of PRDM1 suggests that it has a key role in the loss of HGAL and LMO2 expression upon differentiation of GC B cells to plasma cells and may also contribute to absence of HGAL and LMO2 expression in post-GC lymphoid tumors.

Published
2011

29. Identification of LMO2 transcriptome and interactome in diffuse large B-cell lymphoma

Author

Ministerio de Economía y Competitividad (España), Fundación Alfonso Martín Escudero, National Institutes of Health (US), Dwoskin Family Foundation, Ministerio de Ciencia e Innovación (España), European Commission, Cubedo, Elena, Jiang, Xiaoyu, Romero-Camarero, Isabel, Sánchez García, Isidro, Lossos, Izidore S., Ministerio de Economía y Competitividad (España), Fundación Alfonso Martín Escudero, National Institutes of Health (US), Dwoskin Family Foundation, Ministerio de Ciencia e Innovación (España), European Commission, Cubedo, Elena, Jiang, Xiaoyu, Romero-Camarero, Isabel, Sánchez García, Isidro, and Lossos, Izidore S.

Abstract

LMO2 regulates gene expression by facilitating the formation of multipartite DNA-binding complexes. In B cells, LMO2 is specifically up-regulated in the germinal center (GC) and is expressed in GC-derived non-Hodgkin lymphomas. LMO2 is one of the most powerful prognostic indicators in diffuse large B-cell (DLBCL) patients. However, its function in GC B cells and DLBCL is currently unknown. In this study, we characterized the LMO2 transcriptome and transcriptional complex in DLBCL cells. LMO2 regulates genes implicated in kinetochore function, chromosome assembly, and mitosis. Overexpression of LMO2 in DLBCL cell lines results in centrosome amplification. In DLBCL, the LMO2 complex contains some of the traditional partners, such as LDB1, E2A, HEB, Lyl1, ETO2, and SP1, but not TAL1 or GATA proteins. Furthermore, we identified novel LMO2 interacting partners: ELK1, nuclear factor of activated T-cells (NFATc1), and lymphoid enhancer-binding factor1 (LEF1) proteins. Reporter assays revealed that LMO2 increases transcriptional activity of NFATc1 and decreases transcriptional activity of LEF1 proteins. Overall, our studies identified a novel LMO2 transcriptome and interactome in DLBCL and provides a platform for future elucidation of LMO2 function in GC B cells and DLBCL pathogenesis. © 2012 by The American Society of Hematology.

Published
2012

30. Identification of LMO2 Transcriptome and Interactome in Diffuse Large B-Cell Lymphoma by Integrated Experimental and Computational Approach

Author

Cubedo, Elena, primary, Gentles, Andrew J., additional, Huang, Chuanxin, additional, Natkunam, Yasodha, additional, Bhatt, Shruti, additional, Jiang, Xiaoyu, additional, Lu, Xiaoqing, additional, Romero-Camarero, Isabel, additional, Plevritis, Sylvia K., additional, Martinez-Climent, Jose A, additional, Sanchez-Garcia, Isidro, additional, Melnick, Ari, additional, and Lossos, Izidore S, additional

Published
2011
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40. Dysregulation of apoptosis is a major mechanism in the lymph node involvement in colorectal carcinoma

Author

Bandres, Eva, primary, Catalan, Victoria, additional, Sola, Iosu, additional, Honorato, Beatriz, additional, Cubedo, Elena, additional, Cordeu, Lucia, additional, Andion, Esther, additional, Escalada, Alvaro, additional, Zarate, Ruth, additional, Salgado, Esteban, additional, Zabalegui, Natalia, additional, García, Fermin, additional, and Garcia-Foncillas, Jesus, additional

Published
2004
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41. Gene Expression Profile of Ewing Sarcoma Cell Lines Differing in Their EWS-FLI1Fusion Type

Author

Bandrés, Eva, Malumbres, Raquel, Escalada, Alvaro, Cubedo, Elena, González, Iranzu, Honorato, Beatriz, Zarate, Ruth, García-Foncillas, Jesus, and de Alava, Enrique

Abstract

The t(11;22)(q24;q12) translocation is present in up to 95% of Ewing tumor patients and results in the formation of an EWS-FLI-1fusion gene that encodes a chimeric transcription factor. Many alternative forms of EWS-FLI-1exist because of variations in the location of the EWSand FLI-1genomic breakpoints. Previous reports have shown that the type 1 fusion is associated with a significantly better prognosis than the other fusion types. It has been suggested that the observed clinical discrepancies result from different transactivation potentials of the various EWS-FLI-1fusion proteins. In an attempt to identify genes whose expression levels are differentially modulated by structurally different EWS-FLI-1transcription factors, we have used microarray technology to interrogate 19,000 sequence genes to compare gene expression profile of type 1 or non-type 1 Ewing sarcoma cell lines. Data analysis showed few qualitative differences on gene expression; expression of only 41 genes (0.215% of possible sequences analyzed) differed significantly between Ewing tumor cell lines carrying EWS-FLI-1fusion type 1 with respect to those with non-type 1 fusion.

Published
2005
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42. Synthesis and biological evaluation of 2,4,6-functionalized derivatives of pyrido[2,3-d]pyrimidines as cytotoxic agents and apoptosis inducers.

Author

Sanmartín C, Domínguez MV, Cordeu L, Cubedo E, García-Foncillas J, Font M, and Palop JA

Subjects
Antineoplastic Agents chemistry, Antineoplastic Agents pharmacology, Caspase 3 metabolism, Cell Line, Tumor, Drug Screening Assays, Antitumor, Enzyme Activation, Humans, Models, Molecular, Pyridines chemistry, Pyridines pharmacology, Pyrimidines chemical synthesis, Pyrimidines chemistry, Structure-Activity Relationship, Antineoplastic Agents chemical synthesis, Apoptosis, Pyridines chemical synthesis, Pyrimidines pharmacology
Abstract

In the search for new derivatives with anticancer activity that are able to induce a selective pro-apoptotic mechanism in cancer cells, we have designed, synthesized, and evaluated a series of new 2-(alkylsulfanyl)-N-alkylpyrido[2,3-d]pyrimidine-4-amine derivatives as cytotoxic and apoptosis inducers. The potential antitumor activity of the compounds was evaluated in vitro by examining their cytotoxic effects against human breast, colon, and bladder cancer-cell lines. The IC(50)values of the compounds that showed cytotoxic activity were calculated. The cytotoxic compounds were then tested for their ability to induce caspase-3 activation and nuclear-chromatin degradation. Some compounds, such as 6c, 6d, 6e, 6j, 6o, and 6p, show significant in-vitro cytotoxicity in at least two of the three tested cell lines, induced apoptosis, and also produced a rapid dose-dependent increase in the caspase-3 level in some of the cell lines tested. In order to test the selectivity of the compounds, two non-tumoral human cell lines were used. Several compounds of the did not show cytotoxicity in these cell lines.

Published
2008
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43. Synthesis and biological evaluation of heteroaryldiamides and heteroaryldiamines as cytotoxic agents, apoptosis inducers and caspase-3 activators.

Author

Echeverría M, Mendívil B, Cordeu L, Cubedo E, García-Foncillas J, Font M, Sanmartín C, and Palop JA

Subjects
Amides chemical synthesis, Antineoplastic Agents chemical synthesis, Caspase 3, Cell Line, Tumor, Cell Survival drug effects, Diamines chemical synthesis, Dose-Response Relationship, Drug, Enzyme Activation, HT29 Cells, Humans, Models, Molecular, Molecular Structure, Structure-Activity Relationship, Amides pharmacology, Antineoplastic Agents pharmacology, Apoptosis, Caspases metabolism, Diamines pharmacology
Abstract

The work described here involved the synthesis and biological evaluation of new heteroaryldiamides and heteroaryldiamines. A new general model in which the structures can be adjusted has been applied in this study. Three different structural units can be distinguished: a central nucleus and two symmetric terminal units. The central element is either an aliphatic chain of varying length and flexibility, piperazine, or a polyamine nucleus. However, the terminal units are pyridine, quinoline, indole, benzene or pyrido[2,3-d]pyrimidine with different substituents. The antitumoural activities of the compounds were evaluated in vitro by examining their cytotoxic effects against human breast, colon, and bladder cancer cell lines. Compounds that showed cytotoxic activity were subjected to both apoptosis and caspase-3 assays. With regard to selectivity, the cytotoxicity was also determined in cell cultures of two nontumoural lines. The most promising compounds are 4c, 5c and 7, which are amino-pyridinium, quinolyl-N-oxide, and pyridyl derivatives, respectively, and these reveal a significant in vitro cytotoxicity in at least two of the three cell lines tested. These compounds induced apoptosis and also produced a rapid dose-dependent increase in the caspase-3 level in HT-29 cells. Other encouraging profiles were found, such as those presented by 1k and 8d, which are cytotoxic and apoptotic but do not provoke an increase in the level of caspase-3, or those presented by 2f, 3c and 4a, which are slightly cytotoxic but do not show any other significant activity. The different types of behaviour of each compound are not necessarily parallel in the three cell lines tested.

Published
2006
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