The Experts below are selected from a list of 3090 Experts worldwide ranked by ideXlab platform
Christoph Borner - One of the best experts on this subject based on the ideXlab platform.
-
Phylogenetically Distant Viruses Use the Same BH3-Only Protein PUMA to Trigger Bax/Bak-Dependent Apoptosis of Infected Mouse and Human Cells.
PloS one, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Francesca Marino-merlo, Antonio Mastino, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
-
phylogenetically distant viruses use the same bh3 only Protein PUMA to trigger bax bak dependent apoptosis of infected mouse and human cells
PLOS ONE, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Antonio Mastino, Francesca Marinomerlo, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
Sung H. Lee - One of the best experts on this subject based on the ideXlab platform.
-
Expressional and mutational analysis of pro-apoptotic Bcl-2 member PUMA in hepatocellular carcinomas.
Digestive diseases and sciences, 2007Co-Authors: Chang H. Ahn, N.j. Yoo, Eun Goo Jeong, Sung Soo Kim, Jong W. Lee, Sung H. Lee, Sung H. Kim, Min S. KimAbstract:Deregulation of apoptosis is involved in mechanisms of cancer development. PUMA is a pro-apoptotic member of the Bcl-2 family and mediates p53-dependent and -independent apoptosis. The aim of this study was to investigate whether alterations of PUMA Protein expression and somatic mutations of PUMA gene are characteristics of human hepatocellular carcinoma (HCC). We analyzed expression of PUMA Protein in 20 HCCs using immunohistochemistry. Also, we analyzed mutation of the Bcl-2 homology 3 (BH3) domain of PUMA gene, which is an important domain in apoptosis function of PUMA by single-strand conformation polymorphism (SSCP) in 69 HCCs. PUMA Protein expression was detected in both HCC cells and non-tumor hepatocytes in all of the 20 HCCs. In 10 of these HCCs, cancer cells showed higher PUMA expression than non-tumor (cirrhotic) hepatocytes of the same patients; whereas in the remaining 10, cancer cells and non-tumor hepatocytes showed similar levels. Mutational analysis revealed no PUMA BH3 domain mutation in the 69 HCCs, suggesting that PUMA BH3 domain mutation is not a direct target of inactivation in hepatocellular cancer development. The increased expression of PUMA in malignant hepatocellular cells relative to that in non-tumor hepatocytes suggests that PUMA expression may play a role in HCC development.
-
Pro-Apoptotic PUMA and Anti-Apoptotic Phospho-BAD Are Highly Expressed in Colorectal Carcinomas
Digestive diseases and sciences, 2007Co-Authors: Mi R Kim, N.j. Yoo, Eun Goo Jeong, Jong W. Lee, Boa Chae, Young Hwa Soung, Suk W Nam, Jung Y Lee, Sung H. LeeAbstract:Several lines of evidence indicate that, together with deregulated growth, alteration of apoptosis plays a pivotal role in tumorigenesis. PUMA, a pro-apoptotic member of Bcl-2 family, mediates p53-dependent and -independent apoptosis. BAD is also a pro-apoptotic Bcl-2 family member and phosphorylation of BAD Protein inhibits the pro-apoptosis function of BAD. To see whether the alteration of Protein expressions of PUMA and phospho-BAD (p-BAD) are characteristics of human colorectal cancers, we analyzed the expression of these Proteins in 103 colorectal carcinomas by immunohistochemistry. Also, we analyzed the mutation of the Bcl-2 homology 3 (BH3) domain of PUMA gene, an important domain in the apoptosis function of PUMA, by single-strand conformation polymorphism (SSCP) in 98 colorectal carcinomas. p-BAD immunostaining was detected in 62 cases (60.1%) of the 103 carcinomas, whereas it was not detected in the normal colonic mucosal epithelial cells. PUMA Protein expression was detected in both cancer cells and normal mucosal cells in all of the 103 cases. However, the cancer cells showed higher intensities of PUMA immunostaining than the normal cells of the same patients in 50.4% of the cases. There was no association of the p-BAD expression with the PUMA expression. The mutational analysis revealed no PUMA BH3 domain mutation in the cancers. Our data indicated that expressions of both PUMA and p-BAD were increased in the colorectal cancer cells, and suggested that the increased expression of these Proteins in malignant colorectal epithelial cells compared to the normal mucosal epithelial cells may possibly alter the cell death regulation during colorectal tumorigenesis.
Emanuela Papaianni - One of the best experts on this subject based on the ideXlab platform.
-
Phylogenetically Distant Viruses Use the Same BH3-Only Protein PUMA to Trigger Bax/Bak-Dependent Apoptosis of Infected Mouse and Human Cells.
PloS one, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Francesca Marino-merlo, Antonio Mastino, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
-
phylogenetically distant viruses use the same bh3 only Protein PUMA to trigger bax bak dependent apoptosis of infected mouse and human cells
PLOS ONE, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Antonio Mastino, Francesca Marinomerlo, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
Simon Neumann - One of the best experts on this subject based on the ideXlab platform.
-
Phylogenetically Distant Viruses Use the Same BH3-Only Protein PUMA to Trigger Bax/Bak-Dependent Apoptosis of Infected Mouse and Human Cells.
PloS one, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Francesca Marino-merlo, Antonio Mastino, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
-
phylogenetically distant viruses use the same bh3 only Protein PUMA to trigger bax bak dependent apoptosis of infected mouse and human cells
PLOS ONE, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Antonio Mastino, Francesca Marinomerlo, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
Souhayla El Maadidi - One of the best experts on this subject based on the ideXlab platform.
-
Phylogenetically Distant Viruses Use the Same BH3-Only Protein PUMA to Trigger Bax/Bak-Dependent Apoptosis of Infected Mouse and Human Cells.
PloS one, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Francesca Marino-merlo, Antonio Mastino, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
-
phylogenetically distant viruses use the same bh3 only Protein PUMA to trigger bax bak dependent apoptosis of infected mouse and human cells
PLOS ONE, 2015Co-Authors: Emanuela Papaianni, Souhayla El Maadidi, Andrea Schejtman, Simon Neumann, Ulrich Maurer, Antonio Mastino, Francesca Marinomerlo, Christoph BornerAbstract:Viruses can trigger apoptosis of infected host cells if not counteracted by cellular or viral anti-apoptotic Proteins. These protective Proteins either inhibit the activation of caspases or they act as Bcl-2 homologs to prevent Bax/Bak-mediated outer mitochondrial membrane permeabilization (MOMP). The exact mechanism by which viruses trigger MOMP has however remained enigmatic. Here we use two distinct types of viruses, a double stranded DNA virus, herpes simplex virus-1 (HSV-1) and a positive sense, single stranded RNA virus, Semliki Forest virus (SFV) to show that the BH3-only Protein PUMA is the major mediator of virus-induced Bax/Bak activation and MOMP induction. Indeed, when PUMA was genetically deleted or downregulated by shRNA, mouse embryonic fibroblasts and IL-3-dependent monocytes as well as human colon carcinoma cells were as resistant to virus-induced apoptosis as their Bax/Bak double deficient counterparts (Bax/Bak-/-). PUMA Protein expression started to augment after 2 h postinfection with both viruses. PUMA mRNA levels increased as well, but this occurred after apoptosis initiation (MOMP) because it was blocked in cells lacking Bax/Bak or overexpressing Bcl-xL. Moreover, none of the classical PUMA transcription factors such as p53, p73 or p65 NFκB were involved in HSV-1-induced apoptosis. Our data suggest that viruses use a PUMA Protein-dependent mechanism to trigger MOMP and apoptosis in host cells.
