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pubmed-article:8597041pubmed:abstractTextData from a number of model systems support a role for proteolysis in apoptotic cell death. Using immature rat thymocytes, we demonstrate that the protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and benzyloxycarbonyl-valinyl-alaninyl-aspartyl fluoromethylketone (Z-VAD.FMK) inhibit apoptosis. N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) has a very different effect, inducing the early morphological and biochemical changes associated with apoptosis. TLCK inhibits trypsin-like proteases whilst Z-VAD.FMK inhibits interleukin-1 beta-converting enzyme (ICE)-like proteases; this and the contrasting effects of TPCK support the hypothesis that thymocyte apoptosis involves a hierarchy of proteases which act at different stages of the process.lld:pubmed
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pubmed-article:8597041pubmed:pagination135-41lld:pubmed
pubmed-article:8597041pubmed:dateRevised2003-11-14lld:pubmed
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pubmed-article:8597041pubmed:year1995lld:pubmed
pubmed-article:8597041pubmed:articleTitleDNA degradation and proteolysis in thymocyte apoptosis.lld:pubmed
pubmed-article:8597041pubmed:affiliationMRC Toxicology Unit, University of Leicester, UK.lld:pubmed
pubmed-article:8597041pubmed:publicationTypeJournal Articlelld:pubmed
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