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

FEBS Letters

Radha, Vegesna¹  Sudhakar, Ch¹  Swarup, Ghanshyam¹  Gupta, Sanjeev¹ 

[1] Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India

关键词: Caspase-1;    p53;    Protein tyrosine phosphatase;    Apoptosis;    RT-PCR;    reverse transcription polymerase chain reaction;    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;    CAT;    chloramphenicol acetyltransferase;    cmk;    chloromethylketone;   

DOI  :  10.1016/S0014-5793(02)03628-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown