Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway
Although the participation of the ubiquitin-dependent pathway and of the proteasome in apoptosis has been proposed, its role in this process is not yet clearly defined. In previous studies, we have shown that in the central nervous system of the rat, programmed cell death and the ubiquitin-dependent...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03643190_v27_n11_p1401_Pasquini http://hdl.handle.net/20.500.12110/paper_03643190_v27_n11_p1401_Pasquini |
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paper:paper_03643190_v27_n11_p1401_Pasquini2023-06-08T15:35:35Z Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway Apoptosis Lactocystin Proteasome Schwann cells Ubiquitin caspase 3 I kappa B immunoglobulin enhancer binding protein lactacystin lipocortin 5 proteasome protein bcl 2 protein p53 ubiquitin ubiquitin protein ligase animal cell apoptosis article cell cycle cell structure central nervous system controlled study correlation analysis enzyme activity flow cytometry glia cell measurement nerve cell culture nonhuman priority journal protein degradation protein expression rat Schwann cell signal transduction Animals Apoptosis Cells, Cultured Cysteine Endopeptidases Flow Cytometry Hydrolysis Immunohistochemistry Multienzyme Complexes Proteasome Endopeptidase Complex Rats Rats, Wistar Schwann Cells Ubiquitin Animalia Although the participation of the ubiquitin-dependent pathway and of the proteasome in apoptosis has been proposed, its role in this process is not yet clearly defined. In previous studies, we have shown that in the central nervous system of the rat, programmed cell death and the ubiquitin-dependent proteolytic pathway are closely related to each other and that different types of neurons and of glial cells, shown different types of correlation between the two phenomena. In this work, we have used lactacystin, a highly specific inhibitor of the proteasome, to explore in Schwann cell cultures the relationship between the activity of the Ub-dependent pathway and apoptosis. Apoptosis was explored analyzing changes in nuclear morphology, using the Annexin V assay and by flow cytometry. Activity of caspase-3 was also measured. Changes in the levels of ubiquitin-protein conjugates and of the ubiquitin activating enzymes, E1, as well as expression of proteins that instruct the cells to apoptosis (p53, NFκB-IκB, Bc12), or that participate in the control and regulation of the cell cycle, were also examined. Our results indicate that the decrease in the activity of the proteasome induced by lactacystin in Schwann cells, induces apoptotic cell death through changes in the concentration of certain key proteins that are involved in the apoptosis-signaling pathways. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03643190_v27_n11_p1401_Pasquini http://hdl.handle.net/20.500.12110/paper_03643190_v27_n11_p1401_Pasquini |
| 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 Lactocystin Proteasome Schwann cells Ubiquitin caspase 3 I kappa B immunoglobulin enhancer binding protein lactacystin lipocortin 5 proteasome protein bcl 2 protein p53 ubiquitin ubiquitin protein ligase animal cell apoptosis article cell cycle cell structure central nervous system controlled study correlation analysis enzyme activity flow cytometry glia cell measurement nerve cell culture nonhuman priority journal protein degradation protein expression rat Schwann cell signal transduction Animals Apoptosis Cells, Cultured Cysteine Endopeptidases Flow Cytometry Hydrolysis Immunohistochemistry Multienzyme Complexes Proteasome Endopeptidase Complex Rats Rats, Wistar Schwann Cells Ubiquitin Animalia |
| spellingShingle |
Apoptosis Lactocystin Proteasome Schwann cells Ubiquitin caspase 3 I kappa B immunoglobulin enhancer binding protein lactacystin lipocortin 5 proteasome protein bcl 2 protein p53 ubiquitin ubiquitin protein ligase animal cell apoptosis article cell cycle cell structure central nervous system controlled study correlation analysis enzyme activity flow cytometry glia cell measurement nerve cell culture nonhuman priority journal protein degradation protein expression rat Schwann cell signal transduction Animals Apoptosis Cells, Cultured Cysteine Endopeptidases Flow Cytometry Hydrolysis Immunohistochemistry Multienzyme Complexes Proteasome Endopeptidase Complex Rats Rats, Wistar Schwann Cells Ubiquitin Animalia Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| topic_facet |
Apoptosis Lactocystin Proteasome Schwann cells Ubiquitin caspase 3 I kappa B immunoglobulin enhancer binding protein lactacystin lipocortin 5 proteasome protein bcl 2 protein p53 ubiquitin ubiquitin protein ligase animal cell apoptosis article cell cycle cell structure central nervous system controlled study correlation analysis enzyme activity flow cytometry glia cell measurement nerve cell culture nonhuman priority journal protein degradation protein expression rat Schwann cell signal transduction Animals Apoptosis Cells, Cultured Cysteine Endopeptidases Flow Cytometry Hydrolysis Immunohistochemistry Multienzyme Complexes Proteasome Endopeptidase Complex Rats Rats, Wistar Schwann Cells Ubiquitin Animalia |
| description |
Although the participation of the ubiquitin-dependent pathway and of the proteasome in apoptosis has been proposed, its role in this process is not yet clearly defined. In previous studies, we have shown that in the central nervous system of the rat, programmed cell death and the ubiquitin-dependent proteolytic pathway are closely related to each other and that different types of neurons and of glial cells, shown different types of correlation between the two phenomena. In this work, we have used lactacystin, a highly specific inhibitor of the proteasome, to explore in Schwann cell cultures the relationship between the activity of the Ub-dependent pathway and apoptosis. Apoptosis was explored analyzing changes in nuclear morphology, using the Annexin V assay and by flow cytometry. Activity of caspase-3 was also measured. Changes in the levels of ubiquitin-protein conjugates and of the ubiquitin activating enzymes, E1, as well as expression of proteins that instruct the cells to apoptosis (p53, NFκB-IκB, Bc12), or that participate in the control and regulation of the cell cycle, were also examined. Our results indicate that the decrease in the activity of the proteasome induced by lactacystin in Schwann cells, induces apoptotic cell death through changes in the concentration of certain key proteins that are involved in the apoptosis-signaling pathways. |
| title |
Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| title_short |
Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| title_full |
Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| title_fullStr |
Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| title_full_unstemmed |
Apoptosis in Schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| title_sort |
apoptosis in schwann cell cultures is closely interrelated with the activity of the ubiquitin-proteasome proteolytic pathway |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03643190_v27_n11_p1401_Pasquini http://hdl.handle.net/20.500.12110/paper_03643190_v27_n11_p1401_Pasquini |
| _version_ |
1768544320446529536 |