| pubmed-article:11583996 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0667830 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0758959 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C1720947 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
| pubmed-article:11583996 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:11583996 | pubmed:issue | 49 | lld:pubmed |
| pubmed-article:11583996 | pubmed:dateCreated | 2001-12-3 | lld:pubmed |
| pubmed-article:11583996 | pubmed:abstractText | Caspase-8 is believed to play an obligatory role in apoptosis initiation by death receptors, but the role of its structural relative, caspase-10, remains controversial. Although earlier evidence implicated caspase-10 in apoptosis signaling by CD95L and Apo2L/TRAIL, recent studies indicated that these death receptor ligands recruit caspase-8 but not caspase-10 to their death-inducing signaling complex (DISC) even in presence of abundant caspase-10. We characterized a series of caspase-10-specific antibodies and found that certain commercially available antibodies cross-react with HSP60, shedding new light on previous results. The majority of 55 lung and breast carcinoma cell lines expressed mRNA for both caspase-8 and -10; however, immunoblot analysis revealed that caspase-10 protein expression was more frequently absent than that of caspase-8, suggesting a possible selective pressure against caspase-10 production in cancer cells. In nontransfected cells expressing both caspases, CD95L and Apo2L/TRAIL recruited endogenous caspase-10 as well as caspase-8 to their DISC, where both enzymes were proteolytically processed with similar kinetics. Caspase-10 recruitment required the adaptor FADD/Mort1, and caspase-10 cleavage in vitro required DISC assembly, consistent with the processing of an apoptosis initiator. Cells expressing only one of the caspases underwent ligand-induced apoptosis, indicating that each caspase can initiate apoptosis independently of the other. Thus, apoptosis signaling by death receptors involves not only caspase-8 but also caspase-10, and both caspases may have equally important roles in apoptosis initiation. | lld:pubmed |
| pubmed-article:11583996 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11583996 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11583996 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11583996 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11583996 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11583996 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:AshkenaziAA | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:LawrenceD ADA | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:GazdarAA | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:BlenisJJ | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:VirmaniAA | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:SchowPP | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:LeBlancHH | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:ArnottDD | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:KischkelF CFC | lld:pubmed |
| pubmed-article:11583996 | pubmed:author | pubmed-author:TinelAA | lld:pubmed |
| pubmed-article:11583996 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11583996 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:11583996 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11583996 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11583996 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11583996 | pubmed:pagination | 46639-46 | lld:pubmed |
| pubmed-article:11583996 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11583996 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11583996 | pubmed:articleTitle | Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. | lld:pubmed |
| pubmed-article:11583996 | pubmed:affiliation | Department of Molecular Oncology, Genentech, Inc., South San Francisco, California 94080, USA. | lld:pubmed |
| pubmed-article:11583996 | pubmed:publicationType | Journal Article | lld:pubmed |
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