Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis
Most cells are naturally resistant to TNF-α-induced cell death and become sensitized when NF-κB transactivation is blocked or in the presence of protein synthesis inhibitors that prevent the expression of anti-apoptotic genes. In this report we analyzed the role of osmotic stress on TNIF-α-induced c...
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todo:paper_13509047_v9_n10_p1090_Franco2023-10-03T16:10:04Z Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis Franco, D.L. Nojek, I.M. Molinero, L. Coso, O.A. Costas, M.A. Apoptosis MAP kinases NF-κB TNF-α immunoglobulin enhancer binding protein phosphotransferase protein bcl 2 protein synthesis inhibitor synaptophysin tumor necrosis factor alpha apoptosis article cell death controlled study enzyme activity enzyme inhibition gene activity gene expression HeLa cell human human cell osmotic stress priority journal protein synthesis inhibition sensitization transactivation Apoptosis Dose-Response Relationship, Drug Enzyme Inhibitors Eukaryotic Cells Hela Cells Humans MAP Kinase Signaling System Mitogen-Activated Protein Kinase 12 Mitogen-Activated Protein Kinase 8 Mitogen-Activated Protein Kinases NF-kappa B Osmotic Pressure p38 Mitogen-Activated Protein Kinases Proto-Oncogene Proteins c-bcl-2 Saline Solution, Hypertonic Stress Sulfasalazine Transcription Factor RelA Tumor Necrosis Factor-alpha Most cells are naturally resistant to TNF-α-induced cell death and become sensitized when NF-κB transactivation is blocked or in the presence of protein synthesis inhibitors that prevent the expression of anti-apoptotic genes. In this report we analyzed the role of osmotic stress on TNIF-α-induced cell death. We found that it sensitizes the naturally resistant HeLa cells to TNF-α-induced apoptosis, with the involvement of an increase in the activity of several kinases, the inhibition of Bcl-2 expression, and a late increase on NF-κB activation. Cell death occurs regardless of the enhanced NF-κB activity, whose inhibition produces an increase in apoptosis. The inhibition of p38 kinase, also involved in NF-κB activation, significantly increases the effect of osmotic stress on TNF-α-induced cell death. Fil:Franco, D.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nojek, I.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Molinero, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Coso, O.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Costas, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13509047_v9_n10_p1090_Franco |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Apoptosis MAP kinases NF-κB TNF-α immunoglobulin enhancer binding protein phosphotransferase protein bcl 2 protein synthesis inhibitor synaptophysin tumor necrosis factor alpha apoptosis article cell death controlled study enzyme activity enzyme inhibition gene activity gene expression HeLa cell human human cell osmotic stress priority journal protein synthesis inhibition sensitization transactivation Apoptosis Dose-Response Relationship, Drug Enzyme Inhibitors Eukaryotic Cells Hela Cells Humans MAP Kinase Signaling System Mitogen-Activated Protein Kinase 12 Mitogen-Activated Protein Kinase 8 Mitogen-Activated Protein Kinases NF-kappa B Osmotic Pressure p38 Mitogen-Activated Protein Kinases Proto-Oncogene Proteins c-bcl-2 Saline Solution, Hypertonic Stress Sulfasalazine Transcription Factor RelA Tumor Necrosis Factor-alpha |
spellingShingle |
Apoptosis MAP kinases NF-κB TNF-α immunoglobulin enhancer binding protein phosphotransferase protein bcl 2 protein synthesis inhibitor synaptophysin tumor necrosis factor alpha apoptosis article cell death controlled study enzyme activity enzyme inhibition gene activity gene expression HeLa cell human human cell osmotic stress priority journal protein synthesis inhibition sensitization transactivation Apoptosis Dose-Response Relationship, Drug Enzyme Inhibitors Eukaryotic Cells Hela Cells Humans MAP Kinase Signaling System Mitogen-Activated Protein Kinase 12 Mitogen-Activated Protein Kinase 8 Mitogen-Activated Protein Kinases NF-kappa B Osmotic Pressure p38 Mitogen-Activated Protein Kinases Proto-Oncogene Proteins c-bcl-2 Saline Solution, Hypertonic Stress Sulfasalazine Transcription Factor RelA Tumor Necrosis Factor-alpha Franco, D.L. Nojek, I.M. Molinero, L. Coso, O.A. Costas, M.A. Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
topic_facet |
Apoptosis MAP kinases NF-κB TNF-α immunoglobulin enhancer binding protein phosphotransferase protein bcl 2 protein synthesis inhibitor synaptophysin tumor necrosis factor alpha apoptosis article cell death controlled study enzyme activity enzyme inhibition gene activity gene expression HeLa cell human human cell osmotic stress priority journal protein synthesis inhibition sensitization transactivation Apoptosis Dose-Response Relationship, Drug Enzyme Inhibitors Eukaryotic Cells Hela Cells Humans MAP Kinase Signaling System Mitogen-Activated Protein Kinase 12 Mitogen-Activated Protein Kinase 8 Mitogen-Activated Protein Kinases NF-kappa B Osmotic Pressure p38 Mitogen-Activated Protein Kinases Proto-Oncogene Proteins c-bcl-2 Saline Solution, Hypertonic Stress Sulfasalazine Transcription Factor RelA Tumor Necrosis Factor-alpha |
description |
Most cells are naturally resistant to TNF-α-induced cell death and become sensitized when NF-κB transactivation is blocked or in the presence of protein synthesis inhibitors that prevent the expression of anti-apoptotic genes. In this report we analyzed the role of osmotic stress on TNIF-α-induced cell death. We found that it sensitizes the naturally resistant HeLa cells to TNF-α-induced apoptosis, with the involvement of an increase in the activity of several kinases, the inhibition of Bcl-2 expression, and a late increase on NF-κB activation. Cell death occurs regardless of the enhanced NF-κB activity, whose inhibition produces an increase in apoptosis. The inhibition of p38 kinase, also involved in NF-κB activation, significantly increases the effect of osmotic stress on TNF-α-induced cell death. |
format |
JOUR |
author |
Franco, D.L. Nojek, I.M. Molinero, L. Coso, O.A. Costas, M.A. |
author_facet |
Franco, D.L. Nojek, I.M. Molinero, L. Coso, O.A. Costas, M.A. |
author_sort |
Franco, D.L. |
title |
Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
title_short |
Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
title_full |
Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
title_fullStr |
Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
title_full_unstemmed |
Osmotic stress sensitizes naturally resistant cells to TNF-α-induced apoptosis |
title_sort |
osmotic stress sensitizes naturally resistant cells to tnf-α-induced apoptosis |
url |
http://hdl.handle.net/20.500.12110/paper_13509047_v9_n10_p1090_Franco |
work_keys_str_mv |
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1807318063311224832 |