The Experts below are selected from a list of 321 Experts worldwide ranked by ideXlab platform
Yuji Moriyasu - One of the best experts on this subject based on the ideXlab platform.
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detecting autophagy in arabidopsis roots by membrane permeable cysteine Protease Inhibitor e 64d and endocytosis tracer fm4 64
Plant Signaling & Behavior, 2011Co-Authors: Yuumi Ohye, Yuko Inoue, Yuji MoriyasuAbstract:Autophagy is the process by which cells degrade their own components in lysosomes or vacuoles. Autophagy in tobacco BY-2 cells cultured in sucrose-free medium takes place in formed, autolysosomes in the presence of a cysteine Protease Inhibitor. The autolysosomes in BY-2 cells are located in the endocytotic pathway and thus can be stained with fluorescent endocytosis marker FM4-64. In the present study, in order to detect autophagy in the root cells of Arabidopsis, we incubated root tips from Arabidopsis seedlings in culture medium containing the membrane-permeable cysteine Protease Inhibitor E-64d and FM4-64, and examined whether autolysosomes stained with FM4-64 are accumulated. The results suggest that autophagy accompanying the formation of autolysosomes also occurs in Arabidopsis root cells. Such autophagy appeared to occur constitutively in the root cells in nutrient-sufficient culture medium. Even in atg5 mutants in which an autophagy-related gene is disrupted, accumulation of the structures stained with FM4-64, which likely correspond to autolysosomes, was seen although at lower level than in wild type roots.
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Detecting autophagy in Arabidopsis roots by membrane-permeable cysteine Protease Inhibitor E-64d and endocytosis tracer FM4–64
Plant Signaling & Behavior, 2011Co-Authors: Yuko Inoue, Yuji MoriyasuAbstract:Autophagy is the process by which cells degrade their own components in lysosomes or vacuoles. Autophagy in tobacco BY-2 cells cultured in sucrose-free medium takes place in formed, autolysosomes in the presence of a cysteine Protease Inhibitor. The autolysosomes in BY-2 cells are located in the endocytotic pathway and thus can be stained with fluorescent endocytosis marker FM4-64. In the present study, in order to detect autophagy in the root cells of Arabidopsis, we incubated root tips from Arabidopsis seedlings in culture medium containing the membrane-permeable cysteine Protease Inhibitor E-64d and FM4-64, and examined whether autolysosomes stained with FM4-64 are accumulated. The results suggest that autophagy accompanying the formation of autolysosomes also occurs in Arabidopsis root cells. Such autophagy appeared to occur constitutively in the root cells in nutrient-sufficient culture medium. Even in atg5 mutants in which an autophagy-related gene is disrupted, accumulation of the structures stained with FM4-64, which likely correspond to autolysosomes, was seen although at lower level than in wild type roots.
Juerg Tschopp - One of the best experts on this subject based on the ideXlab platform.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Cell Death & Differentiation, 2007Co-Authors: J A Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, Merel C. M. Strik, C E Hack, Juerg TschoppAbstract:Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
C E Hack - One of the best experts on this subject based on the ideXlab platform.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis.
Cell Death and Differentiation, 2007Co-Authors: Jean Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, C E Hack, Merel Strik, Jürg TschoppAbstract:Apoptosis is a highly controlled process, whose triggering is associated with the activation of caspases. Apoptosis can be induced via a subgroup of the tumor necrosis factor (TNF) receptor superfamily, which recruit and activate pro-caspase-8 and -10. Regulation of apoptosis is achieved by several Inhibitors, including c-FLICE-Inhibitory protein, which prevents apoptosis by inhibiting the pro-apoptotic activation of upstream caspases. Here we show that the human intracellular serine Protease Inhibitor (serpin), Protease Inhibitor 9 (PI9), inhibits TNF-, TNF-related apoptosis-inducing ligand- and Fas ligand-mediated apoptosis in certain TNF-sensitive cell lines. The reactive center P1 residue of PI9 was required for this inhibition since PI9 harboring a Glu --> Ala mutation in its reactive center failed to impair death receptor-induced cell death. This suggests a classical serpin-Protease interaction. Indeed, PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. This indicates that PI9 can regulate pro-apoptotic apical caspases.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Cell Death & Differentiation, 2007Co-Authors: J A Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, Merel C. M. Strik, C E Hack, Juerg TschoppAbstract:Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Pascal Schneider - One of the best experts on this subject based on the ideXlab platform.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis.
Cell Death and Differentiation, 2007Co-Authors: Jean Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, C E Hack, Merel Strik, Jürg TschoppAbstract:Apoptosis is a highly controlled process, whose triggering is associated with the activation of caspases. Apoptosis can be induced via a subgroup of the tumor necrosis factor (TNF) receptor superfamily, which recruit and activate pro-caspase-8 and -10. Regulation of apoptosis is achieved by several Inhibitors, including c-FLICE-Inhibitory protein, which prevents apoptosis by inhibiting the pro-apoptotic activation of upstream caspases. Here we show that the human intracellular serine Protease Inhibitor (serpin), Protease Inhibitor 9 (PI9), inhibits TNF-, TNF-related apoptosis-inducing ligand- and Fas ligand-mediated apoptosis in certain TNF-sensitive cell lines. The reactive center P1 residue of PI9 was required for this inhibition since PI9 harboring a Glu --> Ala mutation in its reactive center failed to impair death receptor-induced cell death. This suggests a classical serpin-Protease interaction. Indeed, PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. This indicates that PI9 can regulate pro-apoptotic apical caspases.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Cell Death & Differentiation, 2007Co-Authors: J A Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, Merel C. M. Strik, C E Hack, Juerg TschoppAbstract:Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Razi Quadir - One of the best experts on this subject based on the ideXlab platform.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis.
Cell Death and Differentiation, 2007Co-Authors: Jean Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, C E Hack, Merel Strik, Jürg TschoppAbstract:Apoptosis is a highly controlled process, whose triggering is associated with the activation of caspases. Apoptosis can be induced via a subgroup of the tumor necrosis factor (TNF) receptor superfamily, which recruit and activate pro-caspase-8 and -10. Regulation of apoptosis is achieved by several Inhibitors, including c-FLICE-Inhibitory protein, which prevents apoptosis by inhibiting the pro-apoptotic activation of upstream caspases. Here we show that the human intracellular serine Protease Inhibitor (serpin), Protease Inhibitor 9 (PI9), inhibits TNF-, TNF-related apoptosis-inducing ligand- and Fas ligand-mediated apoptosis in certain TNF-sensitive cell lines. The reactive center P1 residue of PI9 was required for this inhibition since PI9 harboring a Glu --> Ala mutation in its reactive center failed to impair death receptor-induced cell death. This suggests a classical serpin-Protease interaction. Indeed, PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. This indicates that PI9 can regulate pro-apoptotic apical caspases.
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Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
Cell Death & Differentiation, 2007Co-Authors: J A Kummer, Olivier Micheau, Pascal Schneider, Niels Bovenschen, Roel Broekhuizen, Razi Quadir, Merel C. M. Strik, C E Hack, Juerg TschoppAbstract:Ectopic expression of the serine Protease Inhibitor PI9 modulates death receptor-mediated apoptosis
