| pubmed-article:11953316 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C1705064 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0008546 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0125258 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0598405 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:11953316 | lifeskim:mentions | umls-concept:C0233656 | lld:lifeskim |
| pubmed-article:11953316 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11953316 | pubmed:dateCreated | 2002-4-15 | lld:pubmed |
| pubmed-article:11953316 | pubmed:abstractText | To study the role of caspase-6 during nuclear disassembly, we generated a chicken DT40 cell line in which both alleles of the caspase-6 gene were disrupted. No obvious morphological differences were observed in the apoptotic process in caspase-6- deficient cells compared with the wild type. However, examination of apoptosis in a cell-free system revealed a block in chromatin condensation and apoptotic body formation when nuclei from HeLa cells expressing lamin A or lamin A-transfected Jurkat cells were incubated in caspase-6-deficient apoptotic extracts. Transfection of exogenous caspase-6 into the clone reversed this phenotype. Lamins A and C, which are caspase-6-only substrates, were cleaved by the wild-type and heterozygous apoptotic extracts but not by the extracts lacking caspase-6. Furthermore, the caspase-6 inhibitor z-VEID-fmk mimicked the effects of caspase-6 deficiency and prevented the cleavage of lamin A. Taken together, these observations indicate that caspase-6 activity is essential for lamin A cleavage and that when lamin A is present it must be cleaved in order for the chromosomal DNA to undergo complete condensation during apoptotic execution. | lld:pubmed |
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| pubmed-article:11953316 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11953316 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11953316 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11953316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11953316 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11953316 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11953316 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11953316 | pubmed:author | pubmed-author:DingwallColin... | lld:pubmed |
| pubmed-article:11953316 | pubmed:author | pubmed-author:KottkeTimothy... | lld:pubmed |
| pubmed-article:11953316 | pubmed:author | pubmed-author:RuchaudSandri... | lld:pubmed |
| pubmed-article:11953316 | pubmed:author | pubmed-author:EarnshawWilli... | lld:pubmed |
