Caspase‐2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase‐7
Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase‐2 was the first pro‐apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase‐2 using r...
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| Published in | The FEBS journal Vol. 272; no. 6; pp. 1401 - 1414 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Science Ltd
01.03.2005
Blackwell Publishing Ltd |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1742-464X 1742-4658 |
| DOI | 10.1111/j.1742-4658.2005.04573.x |
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| Abstract | Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase‐2 was the first pro‐apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase‐2 using recombinant proteins and a yeast‐based system. Our data suggest that for human caspase‐2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase‐2 could provoke the activation of caspase‐7. Caspase‐2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors. |
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| AbstractList | Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase-2 using recombinant proteins and a yeast-based system. Our data suggest that for human caspase-2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase-2 could provoke the activation of caspase-7. Caspase-2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors. [PUBLICATION ABSTRACT] Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase‐2 was the first pro‐apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase‐2 using recombinant proteins and a yeast‐based system. Our data suggest that for human caspase‐2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase‐2 could provoke the activation of caspase‐7. Caspase‐2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors. Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase-2 using recombinant proteins and a yeast-based system. Our data suggest that for human caspase-2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase-2 could provoke the activation of caspase-7. Caspase-2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors.Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase-2 using recombinant proteins and a yeast-based system. Our data suggest that for human caspase-2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase-2 could provoke the activation of caspase-7. Caspase-2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors. |
| Author | Ekert, Paul G. Jabbour, Anissa M. Hawkins, Christine J. Ho, Po‐ki |
| Author_xml | – sequence: 1 givenname: Po‐ki surname: Ho fullname: Ho, Po‐ki – sequence: 2 givenname: Anissa M. surname: Jabbour fullname: Jabbour, Anissa M. – sequence: 3 givenname: Paul G. surname: Ekert fullname: Ekert, Paul G. – sequence: 4 givenname: Christine J. surname: Hawkins fullname: Hawkins, Christine J. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15752357$$D View this record in MEDLINE/PubMed |
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| Snippet | Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase‐2 was the first pro‐apoptotic caspase identified, but its... Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its... |
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| SubjectTerms | Animals Apoptosis - physiology Caspase 2 Caspase 7 Caspase Inhibitors Caspases - metabolism Cytokines Enzyme Activation enzyme activity Inhibitor of Apoptosis Proteins Mammals protease Proteins Proteins - metabolism Recombinant Proteins - metabolism S. cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Signal Transduction Yeast |
| Title | Caspase‐2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase‐7 |
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