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Updated: Jun 10, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
Published on: August 6, 2020
Activation of RASSF2A by p300 induces late apoptosis through histone hyperacetylation
Chungang Liu1, Yunhui Pan, Xiuli Wang
1School of Life Science, Northeast Normal University, Changchun 130024, Peoples Republic of China.
Abstract:
Both RASSF2A (Ras-associated family 2A) and p300 are implicated in apoptosis. However, little is known about the interrelationship between these two proteins in induction of apoptosis. Here we show that p300 was able to induce late apoptosis through up-regulation of RASSF2A in human gastric cancer cells SGC-7901 (p53-mutant). Our data demonstrated that p300 stimulated RASSF2A expression in 293T cells in cooperation with the transcription factor Sp1. Results of ChIP (chromatin immunoprecipitation) assays revealed that p300 induced histones H3 and H4 hyperacetylation at RASSF2A promoter. Moreover, p300 and Sp1 reciprocally facilitated their binding to RASSF2A promoter. Overall, data arising from this study indicate that Sp1-mediated RASSF2A gene transcription is activated by p300 through histone acetylation, and this activation plays an important role in inducing late apoptosis.
Insights
p300 protein induces late apoptosis by increasing Ras-associated family 2A (RASSF2A) expression in gastric cancer cells. This occurs via Sp1 transcription factor cooperation and histone acetylation at the RASSF2A promoter.
Area of Science:
- Molecular Biology
- Cell Biology
- Cancer Research
Background:
- Ras-associated family 2A (RASSF2A) and p300 are involved in apoptosis.
- The precise relationship between RASSF2A and p300 in apoptosis induction is not well understood.
Purpose of the Study:
- To investigate the interrelationship between p300 and RASSF2A in the induction of apoptosis.
- To elucidate the molecular mechanisms by which p300 influences RASSF2A expression and subsequent apoptosis.
Main Methods:
- Cell culture of human gastric cancer SGC-7901 (p53-mutant) and 293T cells.
- Analysis of RASSF2A expression and apoptosis induction.
- Chromatin immunoprecipitation (ChIP) assays to assess histone acetylation and protein binding.
- Investigation of the role of transcription factor Sp1.
Main Results:
- p300 induces late apoptosis through up-regulation of RASSF2A in SGC-7901 cells.
- p300 stimulates RASSF2A expression in 293T cells, cooperating with Sp1.
- p300 induces histone H3 and H4 hyperacetylation at the RASSF2A promoter.
- p300 and Sp1 exhibit reciprocal facilitation of binding to the RASSF2A promoter.
Conclusions:
- Sp1-mediated RASSF2A gene transcription is activated by p300 via histone acetylation.
- This p300-mediated activation of RASSF2A plays a significant role in inducing late apoptosis.
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