DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Karam | - |
dc.contributor.author | Choi, Kyung Hee | - |
dc.contributor.author | Fu, Ya-Min | - |
dc.contributor.author | Meadows, Gary G. | - |
dc.contributor.author | Joe, Cheol O. | - |
dc.date.accessioned | 2009-12-08T03:08:42Z | - |
dc.date.available | 2009-12-08T03:08:42Z | - |
dc.date.issued | 2003-07-11 | - |
dc.identifier.citation | Biochemical and Biophysical Research Communications, Vol.306, No.4, pp.954-958 | en |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10203/14374 | - |
dc.description.abstract | The apoptotic function of N-α-tosyl- -phenylalanyl chloromethyl ketone (TPCK) was investigated in cultured human colorectal carcinoma cells (HCT116). TPCK-induced apoptosis was shown to be p53-dependent in HCT116 cells during the early stage of incubation. The function of p53 was required for TPCK-induced activation of caspase-3 and caspase-7. TPCK promoted dephosphorylation of p53 on serine residues at 6, 9, 46, 376, and 378 in parallel with the activation of p53 transcriptional activity. HCT116 p53−/− cells expressing p53 mutant, in which serine residues at 6, 9, 46, 376, and 378 were replaced by aspartic acids, were resistant to TPCK-induced apoptosis suggesting the requirement of dephosphorylation of p53 on serine residues during TPCK-induced apoptosis. | en |
dc.description.sponsorship | We thank Dr. John Blenis and Dr. Bryan Ballif for important communications and critical reading of the manuscript. This work was supported by the Grant 2002-CP0432 from Korea Research Foundation, South Korea. | en |
dc.language.iso | en_US | en |
dc.publisher | Elsevier | en |
dc.subject | TPCK | en |
dc.subject | p53 | en |
dc.subject | Dephosphorylation | en |
dc.subject | Apoptosis | en |
dc.subject | Caspase | en |
dc.title | Dephosphorylation of p53 during cell death by N-α-tosyl- -phenylalanyl chloromethyl ketone | en |
dc.type | Article | en |
dc.identifier.doi | 10.1016/S0006-291X(03)01088-X | - |
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