| pubmed-article:8760815 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0212694 | lld:lifeskim |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0039195 | lld:lifeskim |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0599733 | lld:lifeskim |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0021755 | lld:lifeskim |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:8760815 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:8760815 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8760815 | pubmed:dateCreated | 1996-9-23 | lld:pubmed |
| pubmed-article:8760815 | pubmed:abstractText | Cytotoxic T cells (CTL) represent the major defense mechanism against the spread of virus infection. It is believed that the pore-forming protein, perforin, facilitates the entry of a series of serine proteases (particularly granzyme B) into the target cell which ultimately leads to DNA fragmentation and apoptosis. We demonstrate here that during CTL-mediated cytolysis the catalytic subunit of DNA-dependent protein kinase (DNA-PKcs), an enzyme implicated in the repair of double strand breaks in DNA, is specifically cleaved by an interleukin (IL)-1 beta-converting enzyme (ICE)-like protease. A serine protease inhibitor, 3,4-dichloroisocoumarin (DCl), which is known to block granzyme B activity, inhibited CTL-induced apoptosis and prevented the degradation of DNA-PKcs in cells but failed to prevent the degradation of purified DNA-PKcs by CTL extracts. However, Tyr-Val-Ala-Asp-CH2Cl (YVAD-CMK) and other cysteine protease inhibitors prevented the degradation of purified DNA-PKcs by CTL extracts. Furthermore, incubation of DNA-PKcs with granzyme B did not produce the same cleavage pattern observed in cells undergoing apoptosis and when this substrate was incubated with either CTL extracts or the ICE-like protease, CPP32. Sequence analysis revealed that the cleavage site in DNA-PKcs during CTL killing was the same as that when this substrate was exposed to CPP32. This study demonstrates for the first time that the cleavage of DNA-PKcs in this intact cell system is exclusively due to an ICE-like protease. | lld:pubmed |
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| pubmed-article:8760815 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8760815 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8760815 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8760815 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8760815 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8760815 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:KumarSS | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:SmithGG | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:LitwackGG | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:FOLL | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:JacksonSS | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:MossD JDJ | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:LavinM FMF | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:LuHH | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:SoniSS | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:BurrowsS RSR | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:Lees-MillerS... | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:TrapaniJ AJA | lld:pubmed |
| pubmed-article:8760815 | pubmed:author | pubmed-author:AlnemriEE | lld:pubmed |
| pubmed-article:8760815 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8760815 | pubmed:day | 1 | lld:pubmed |
