Dephosphorylation of p53 during cell death by N-alpha-tosyl-L-phenylalanyl chloromethyl ketone
The apoptotic function of N-alpha-tosyl-L-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. (C) 2003 Elsevier Science (USA). All rights reserved.
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Issue Date
- 2003-07
- Language
- English
- Article Type
- Article
- Keywords
DAMAGE-INDUCED PHOSPHORYLATION; TUMOR-SUPPRESSOR PROTEIN; DNA-BINDING FUNCTION; MURINE B-CELLS; TERMINAL SITES; APOPTOSIS; INHIBITION; 14-3-3-PROTEINS; ASSOCIATION; ACTIVATION
- Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.306, no.4, pp.954 - 958
- ISSN
- 0006-291X
- Appears in Collection
- BS-Journal Papers(저널논문)
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