A nuclear protein tyrosine phosphatase activates p53 and induces caspase-1-dependent apoptosis

PTP-S2/TC45 is a nuclear protein tyrosine phosphatase, which induces p53-dependent apoptosis. Here we show that the p53 protein level increased in MCF-7 cells in response to PTP-S2 overexpression. PTP-S2-induced p53 protein was transcriptionally active and it could activate caspase-1 gene expression...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2002-12, Vol.532 (1), p.61-66
Main Authors: Gupta, Sanjeev, Radha, Vegesna, Sudhakar, Ch, Swarup, Ghanshyam
Format: Article
Language:English
Subjects:
Apoptosis
Caspase 1 - genetics
Caspase 1 - physiology
Caspase-1
CAT, chloramphenicol acetyltransferase
cmk, chloromethylketone
GAPDH, glyceraldehyde-3-phosphate dehydrogenase
Humans
Nuclear Proteins - physiology
p53
Protein tyrosine phosphatase
Protein Tyrosine Phosphatase, Non-Receptor Type 2
Protein Tyrosine Phosphatases - genetics
Protein Tyrosine Phosphatases - physiology
RNA, Messenger - biosynthesis
RT-PCR, reverse transcription polymerase chain reaction
Transcriptional Activation
Transfection
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:PTP-S2/TC45 is a nuclear protein tyrosine phosphatase, which induces p53-dependent apoptosis. Here we show that the p53 protein level increased in MCF-7 cells in response to PTP-S2 overexpression. PTP-S2-induced p53 protein was transcriptionally active and it could activate caspase-1 gene expression from endogenous as well as ectopic promoter. Coexpression of an active site mutant of procaspase-1 strongly inhibited PTP-S2-induced apoptosis. Mutant procaspase-1 also inhibited apoptosis induced by p53 overexpression or doxorubicin treatment, which induce caspase-1 gene expression. In contrast, apoptosis induced by staurosporine or cycloheximide, which do not increase caspase-1 gene expression, was not affected by mutant procaspase-1. These results suggest that caspase-1 may be one of the mediators of p53-dependent apoptosis in human cells.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)03628-1