| pubmed-article:16352606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C0537969 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C1657248 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C0332232 | lld:lifeskim |
| pubmed-article:16352606 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:16352606 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:16352606 | pubmed:dateCreated | 2006-2-13 | lld:pubmed |
| pubmed-article:16352606 | pubmed:abstractText | MCF-7 cells lack caspase-3 but undergo mitochondrial-dependent apoptosis via caspase-7 activation. It is assumed that the Apaf-1-caspase-9 apoptosome processes caspase-7 in an analogous manner to that described for caspase-3. However, this has not been validated experimentally, and we have now characterized the caspase-7 activating apoptosome complex in MCF-7 cell lysates activated with dATP/cytochrome c. Apaf-1 oligomerizes to produce approximately 1.4-MDa and approximately 700-kDa apoptosome complexes, and the latter complex directly cleaves/activates procaspase-7. This approximately 700-kDa apoptosome complex, which is also formed in apoptotic MCF-7 cells, is assembled by rapid oligomerization of Apaf-1 and followed by a slower process of procaspase-9 recruitment and cleavage to form the p35/34 forms. However, procaspase-9 recruitment and processing are accelerated in lysates supplemented with caspase-3. In lysates containing very low levels of Smac and Omi/HtrA2, XIAP (X-linked inhibitor of apoptosis) binds tightly to caspase-9 in the apoptosome complex, and as a result caspase-7 processing is abrogated. In contrast, in MCF-7 lysates containing Smac and Omi/HtrA2, active caspase-7 is released from the apoptosome and forms a stable approximately 200-kDa XIAP-caspase-7 complex, which apparently does not contain cIAP1 or cIAP2. Thus, in comparison to caspase-3-containing cells, XIAP appears to have a more significant antiapoptotic role in MCF-7 cells because it directly inhibits caspase-7 activation by the apoptosome and also forms a stable approximately 200-kDa complex with active caspase-7. | lld:pubmed |
| pubmed-article:16352606 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16352606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16352606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16352606 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16352606 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16352606 | pubmed:author | pubmed-author:CohenGerald... | lld:pubmed |
| pubmed-article:16352606 | pubmed:author | pubmed-author:CainKelvinK | lld:pubmed |
| pubmed-article:16352606 | pubmed:author | pubmed-author:TwiddyDavinaD | lld:pubmed |
| pubmed-article:16352606 | pubmed:author | pubmed-author:MacfarlaneMar... | lld:pubmed |
| pubmed-article:16352606 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16352606 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:16352606 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16352606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16352606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16352606 | pubmed:pagination | 3876-88 | lld:pubmed |
| pubmed-article:16352606 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:meshHeading | pubmed-meshheading:16352606... | lld:pubmed |
| pubmed-article:16352606 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16352606 | pubmed:articleTitle | Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex. | lld:pubmed |
| pubmed-article:16352606 | pubmed:affiliation | Medical Research Council Toxicology Unit, Hodgkin Building, University of Leicester, UK. | lld:pubmed |
| pubmed-article:16352606 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16352606 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16352606 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16352606 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16352606 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16352606 | lld:pubmed |
