pubmed-article:8885990 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C0376448 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C0032405 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C0061878 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
pubmed-article:8885990 | lifeskim:mentions | umls-concept:C2346714 | lld:lifeskim |
pubmed-article:8885990 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8885990 | pubmed:dateCreated | 1996-12-9 | lld:pubmed |
pubmed-article:8885990 | pubmed:abstractText | Cytotoxic lymphocytes utilize granule associated serine proteases (granzymes) and perforin to induce apoptosis. Although the importance of granzyme B has been established by gene ablation experiments, biochemical events initiated by the granzyme remain enigmatic. We show here that exposure of Jurkat cells to granzyme B and perforin results in cleavage of poly(ADP-ribose) polymerase to an apoptotic 89 kDa fragment and to lesser amounts of a 64 kDa fragment. The 64 kDa fragment is produced directly by granzyme B while the 89 kDa fragment is presumably generated by activated ICE/Ced-3 proteases. Establishing the intracellular function of GrB in the apoptotic response, these results indicate that granzyme B enters perforin treated targets activating the ICE/Ced-3 family proteases which then cleave poly(ADP-ribose) polymerase to its apoptotic fragment. Intracellular granzyme B appears to be translocated to the nucleus where the protease directly cleaves poly(ADP-ribose) polymerase. | lld:pubmed |
pubmed-article:8885990 | pubmed:language | eng | lld:pubmed |
pubmed-article:8885990 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8885990 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8885990 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8885990 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:PoirierG GGG | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:EarnshawW CWC | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:FroelichC JCJ | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:ShahG MGM | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:AlnemriE SES | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:SalvesenG SGS | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:HannaW LWL | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:D'AmoursDD | lld:pubmed |
pubmed-article:8885990 | pubmed:author | pubmed-author:DuriezP JPJ | lld:pubmed |
pubmed-article:8885990 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8885990 | pubmed:day | 23 | lld:pubmed |
pubmed-article:8885990 | pubmed:volume | 227 | lld:pubmed |
pubmed-article:8885990 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8885990 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8885990 | pubmed:pagination | 658-65 | lld:pubmed |
pubmed-article:8885990 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:8885990 | pubmed:meshHeading | pubmed-meshheading:8885990-... | lld:pubmed |
pubmed-article:8885990 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8885990 | pubmed:articleTitle | Granzyme B/perforin-mediated apoptosis of Jurkat cells results in cleavage of poly(ADP-ribose) polymerase to the 89-kDa apoptotic fragment and less abundant 64-kDa fragment. | lld:pubmed |
pubmed-article:8885990 | pubmed:affiliation | Department of Medicine, Evanston Hospital, Northwestern University, Illinois 60201, USA. granzyme@merle.acns.nwu.edu | lld:pubmed |
pubmed-article:8885990 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8885990 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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