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LncRNA Meg3 protects endothelial function by regulating the DNA damage response.

Mohamed Sham Shihabudeen Haider Ali1, Xiao Cheng1, Matthew Moran1

  • 1Department of Biochemistry, University of Nebraska-Lincoln, Beadle Center, 1901 Vine St, Lincoln, NE 68588, USA.

Nucleic Acids Research
|November 27, 2018
PubMed
Summary

Long non-coding RNA Meg3 and protein PTBP3 regulate endothelial function via the DNA damage response and p53 signaling. Their interaction impacts cell death and proliferation, offering potential therapeutic targets.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Long non-coding RNAs (lncRNAs) are increasingly recognized for their regulatory roles in cellular processes.
  • The interplay between lncRNAs, DNA damage response (DDR), and endothelial cell (EC) function is not well-defined.
  • p53 signaling is a critical pathway in DDR, controlling apoptosis and proliferation.

Purpose of the Study:

  • To investigate the role of lncRNA maternally expressed gene 3 (Meg3) in regulating endothelial function through the DNA damage response (DDR).
  • To elucidate the mechanism by which Meg3 influences p53 signaling and its downstream effects on endothelial cells.
  • To identify potential therapeutic targets for restoring endothelial homeostasis.

Main Methods:

  • Investigated the interaction between Meg3 and polypyrimidine tract binding protein 3 (PTBP3) in endothelial cells.
  • Analyzed the impact of Meg3 and PTBP3 silencing on DNA damage, p53 signaling activation, and target gene expression.
  • Assessed the effects on endothelial cell apoptosis and proliferation using various molecular and cellular assays.
  • Examined the association of p53 with Mdm2 and with the promoters of p53 target genes.

Main Results:

  • Meg3 expression is induced by p53 activation in endothelial cells.
  • Meg3 silencing leads to DNA damage, p53 activation, increased apoptosis, and reduced proliferation in ECs.
  • Meg3 regulates the interaction of p53 with Mdm2 and its binding to target gene promoters.
  • PTBP3 silencing mimics the effects of Meg3 deficiency, suggesting a cooperative role in restraining p53 activation.

Conclusions:

  • Meg3 and PTBP3 form a regulatory complex that modulates p53 signaling in endothelial cells.
  • This novel Meg3-PTBP3-p53 axis plays a crucial role in maintaining endothelial homeostasis.
  • Targeting the Meg3-PTBP3 interaction presents a potential therapeutic strategy for endothelial dysfunction.