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Down-regulation of CREB-binding protein expression blocks thrombin-mediated endothelial activation by inhibiting

Jing Chen1, Hong Jiang, Jian Yang

  • 1Department of Cardiology, Renmin Hospital, Wuhan University, Wuhan 430060, China.

International Journal of Cardiology
|October 8, 2010
PubMed

Insights

CREB-binding protein (CBP) regulates endothelial activation by influencing NF-κB signaling. Reducing CBP levels can help return endothelial cells to a quiescent state, potentially aiding in atherosclerosis treatment.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • CREB-binding protein (CBP) is a co-activator with histone acetyltransferase (HAT) activity.
  • Endothelial activation plays a key role in inflammatory processes and vascular diseases.

Purpose of the Study:

  • To investigate the role of CBP in thrombin-induced endothelial activation.
  • To elucidate the underlying molecular mechanisms involving NF-κB signaling.

Main Methods:

  • Assessed leukocyte-endothelial adhesion.
  • Quantified adhesion molecule expression using RT-PCR and Western blot.
  • Evaluated NF-κB activation and acetylation, alongside CBP-HAT activity.

Main Results:

  • CBP knockdown significantly reduced thrombin-induced leukocyte-endothelial adhesion.
  • Expression of adhesion molecules (VCAM-1, ICAM-1, E-selectin) was decreased.
  • Thrombin-mediated NF-κB activation, NF-κB acetylation, and CBP-HAT activity were suppressed by CBP silencing.

Conclusions:

  • CBP is crucial in regulating endothelial activation through an NF-κB-dependent pathway.
  • Down-regulating CBP may restore endothelial cells from a pro-inflammatory state to quiescence.
  • These findings suggest a potential therapeutic role for CBP modulation in atherosclerosis.
Abstract

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