Cellular death linked to irreversible stress in the sarcoplasmic reticulum: The effect of inhibiting Ca2+–ATPase or protein glycosylation in the myocardiac cell model H9c2
| Autor: | Antonio Lax, Francisco Fernandez-Belda, Fernando Soler |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Glycosylation
Thapsigargin Biophysics Apoptosis Caspase 3 Calcium-Transporting ATPases Caspase 8 Biochemistry Mitochondria Heart Cell Line chemistry.chemical_compound Animals Myocytes Cardiac Molecular Biology Caspase Caspase-9 biology Tunicamycin Endoplasmic reticulum Cytochrome c Cytochromes c Molecular biology Rats Cell biology Enzyme Activation Sarcoplasmic Reticulum chemistry Caspases biology.protein Caspase 12 |
| Zdroj: | Archives of Biochemistry and Biophysics. 466:194-202 |
| ISSN: | 0003-9861 |
| Popis: | Experimental sarcoplasmic reticulum damage induced by 3 microM thapsigargin or 1 microg/ml tunicamycin provoked viability loss of the cell population in approximately 72 h. Release of cytochrome c from mitochondria was an early event and Bax translocation to the mitochondria preceded or was simultaneous with cytochrome c release. The release of cytochrome c was not related with mitochondria depolarization or caspase activation. Irreversible stress in the sarcoplasmic reticulum, detected by the early activation of caspase 12, was functionally linked to the mitochondrial apoptotic pathway. Caspase 3 processing was blocked by cells preincubation with a selective inhibitor of either caspase 9 or caspase 8 whereas caspase 8 activation was inhibited by a selective caspase 9 inhibitor. This was consistent with the involvement of caspase 8 in a positive feedback loop leading to amplify the caspase cascade. Caspase inhibition did not protect against cell death indicating the existence of alternative caspase-independent mechanisms. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect