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- Publisher Website: 10.1038/ncb1340
- Scopus: eid_2-s2.0-30344459150
- PMID: 16362053
- WOS: WOS:000234651500014
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Article: In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
Title | In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis |
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Authors | |
Issue Date | 2006 |
Citation | Nature Cell Biology, 2006, v. 8, n. 1, p. 72-77 How to Cite? |
Abstract | Activation of 'initiator' (or 'apical') caspases-2, -8 or -9 (refs 1-3) is crucial for induction of apoptosis. These caspases function to activate executioner caspapses that, in turn, orchestrate apoptotic cell death. Here, we show that a cell-permeable, biotinylated pan-caspase inhibitor (bVAD-fmk) both inhibited and 'trapped' the apical caspase activated when apoptosis was triggered. As expected, only caspase-8 was trapped in response to ligation of death receptors, whereas only caspase-9 was trapped in response to a variety of other apoptosis-inducing agents. Caspase-2 was exclusively activated in heat shock-induced apoptosis. This activation of caspase-2 was also observed in cells protected from heat-shock-induced apoptosis by Bcl-2 or Bcl-xL. Reduced sensitivity to heat-shock-induced death was observed in caspase-2-/- cells. Furthermore, cells lacking the adapter molecule RAIDD failed to activate caspase-2 after heat shock treatment and showed resistance to apoptosis in this setting. This approach unambiguously identifies the apical caspase activated in response to apoptotic stimuli, and establishes caspase-2 as a proximal mediator of heat shock-induced apoptosis. © 2006 Nature Publishing Group. |
Persistent Identifier | http://hdl.handle.net/10722/292553 |
ISSN | 2021 Impact Factor: 28.213 2020 SCImago Journal Rankings: 11.380 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Tu, Shine | - |
dc.contributor.author | McStay, Gavin P. | - |
dc.contributor.author | Boucher, Louis Martin | - |
dc.contributor.author | Mak, Tak | - |
dc.contributor.author | Beere, Helen M. | - |
dc.contributor.author | Green, Douglas R. | - |
dc.date.accessioned | 2020-11-17T14:56:43Z | - |
dc.date.available | 2020-11-17T14:56:43Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Nature Cell Biology, 2006, v. 8, n. 1, p. 72-77 | - |
dc.identifier.issn | 1465-7392 | - |
dc.identifier.uri | http://hdl.handle.net/10722/292553 | - |
dc.description.abstract | Activation of 'initiator' (or 'apical') caspases-2, -8 or -9 (refs 1-3) is crucial for induction of apoptosis. These caspases function to activate executioner caspapses that, in turn, orchestrate apoptotic cell death. Here, we show that a cell-permeable, biotinylated pan-caspase inhibitor (bVAD-fmk) both inhibited and 'trapped' the apical caspase activated when apoptosis was triggered. As expected, only caspase-8 was trapped in response to ligation of death receptors, whereas only caspase-9 was trapped in response to a variety of other apoptosis-inducing agents. Caspase-2 was exclusively activated in heat shock-induced apoptosis. This activation of caspase-2 was also observed in cells protected from heat-shock-induced apoptosis by Bcl-2 or Bcl-xL. Reduced sensitivity to heat-shock-induced death was observed in caspase-2-/- cells. Furthermore, cells lacking the adapter molecule RAIDD failed to activate caspase-2 after heat shock treatment and showed resistance to apoptosis in this setting. This approach unambiguously identifies the apical caspase activated in response to apoptotic stimuli, and establishes caspase-2 as a proximal mediator of heat shock-induced apoptosis. © 2006 Nature Publishing Group. | - |
dc.language | eng | - |
dc.relation.ispartof | Nature Cell Biology | - |
dc.title | In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1038/ncb1340 | - |
dc.identifier.pmid | 16362053 | - |
dc.identifier.scopus | eid_2-s2.0-30344459150 | - |
dc.identifier.volume | 8 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 72 | - |
dc.identifier.epage | 77 | - |
dc.identifier.isi | WOS:000234651500014 | - |
dc.identifier.f1000 | 1029921 | - |
dc.identifier.issnl | 1465-7392 | - |