Bax is upregulated by p53 signal pathway in the SPE B-induced apoptosis

Wei-Ting Lee, Chia Wen Chang

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

We identify integrin αvβ3 and Fas as receptors for the streptococcal pyrogenic exotoxin B (SPE B), and G308S (SPE B mutant, glycine at residue 308 is changed to serine), which interacts with Fas only, in our previous study. Here, we explore the signal pathways that regulate proapoptotic protein expression after SPE B stimulation. We find that both SPE B and G308S can stimulate the serine phosphorylation of p53, and p53 phosphorylation is inhibited by the anti-Fas antibody but not by anti-αVβ3 antibody. p38 inhibitor and siRNA decrease the activation and translocation of p53 into the nucleus, which executes its transcription activity. These results indicate that after SPE B treatment, p53 is activated and p38 is the upstream of p53. p38 siRNA also decreases the binding of p53 to the bax promoter and interferes with the association of p53 and STAT1. p53, p38, and STAT1 siRNAs downregulate SPE B-induced Bax expression. This shows that SPE B activates the bax promoter via p38/p53 signal pathways through the Fas receptor, and that STAT1 acts as a coactivator of p53. In addition, p38 and p53 siRNAs inhibit SPE B-induced apoptosis. This is consistent with the findings that SPE B upregulates Bax expression through p38/p53 signal pathways that enhance cell apoptosis.

Original languageEnglish
Pages (from-to)271-279
Number of pages9
JournalMolecular and Cellular Biochemistry
Volume343
Issue number1-2
DOIs
Publication statusPublished - 2010 Oct 1

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Signal Transduction
Apoptosis
CD95 Antigens
Phosphorylation
Serine
Small Interfering RNA
Anti-Idiotypic Antibodies
erythrogenic toxin
Antibodies
Transcription
Integrins
Glycine
Up-Regulation
Down-Regulation
Chemical activation
Association reactions
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Cite this

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abstract = "We identify integrin αvβ3 and Fas as receptors for the streptococcal pyrogenic exotoxin B (SPE B), and G308S (SPE B mutant, glycine at residue 308 is changed to serine), which interacts with Fas only, in our previous study. Here, we explore the signal pathways that regulate proapoptotic protein expression after SPE B stimulation. We find that both SPE B and G308S can stimulate the serine phosphorylation of p53, and p53 phosphorylation is inhibited by the anti-Fas antibody but not by anti-αVβ3 antibody. p38 inhibitor and siRNA decrease the activation and translocation of p53 into the nucleus, which executes its transcription activity. These results indicate that after SPE B treatment, p53 is activated and p38 is the upstream of p53. p38 siRNA also decreases the binding of p53 to the bax promoter and interferes with the association of p53 and STAT1. p53, p38, and STAT1 siRNAs downregulate SPE B-induced Bax expression. This shows that SPE B activates the bax promoter via p38/p53 signal pathways through the Fas receptor, and that STAT1 acts as a coactivator of p53. In addition, p38 and p53 siRNAs inhibit SPE B-induced apoptosis. This is consistent with the findings that SPE B upregulates Bax expression through p38/p53 signal pathways that enhance cell apoptosis.",
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Bax is upregulated by p53 signal pathway in the SPE B-induced apoptosis. / Lee, Wei-Ting; Chang, Chia Wen.

In: Molecular and Cellular Biochemistry, Vol. 343, No. 1-2, 01.10.2010, p. 271-279.

Research output: Contribution to journalArticle

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