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Related Experiment Videos

Signaling pathways regulating murine cardiac CREB phosphorylation.

Bailing Li1, Marcia A Kaetzel, John R Dedman

  • 1Department of Genome Science, University of Cincinnati Genome Research Institute, Cincinnati, OH 45237-0505, USA. libl@email.uc.edu

Biochemical and Biophysical Research Communications
|September 26, 2006
PubMed
Summary

Cardiac CREB phosphorylation is signal-specific, primarily mediated by Protein Kinase C epsilon (PKCε) translocation to the nucleus, not by PKA, CaMKII, or p90RSK, challenging previous findings in other tissues.

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Area of Science:

  • Cardiovascular Physiology
  • Molecular Biology
  • Cell Signaling

Background:

  • Cyclic AMP response element-binding protein (CREB) phosphorylation at Serine 133 (S133) is a critical step in cardiac gene regulation.
  • Understanding the specific signaling pathways that control cardiac CREB-S133 phosphorylation is essential for elucidating cardiac function and disease.

Purpose of the Study:

  • To define the signaling pathways regulating cardiac CREB-S133 phosphorylation in the mouse heart.
  • To investigate the roles of Protein Kinase A (PKA), Ca2+/calmodulin-dependent kinase II (CaMKII), and Protein Kinase C (PKC) in mediating CREB-S133 phosphorylation.

Main Methods:

  • Utilized the Langendorff heart perfusion model in mice.
  • Stimulated hearts with isoproterenol (ISO), endothelin-1 (ET-1), and phorbol 12-myristate 13-acetate (TPA).

Related Experiment Videos

  • Assessed the activation of key signaling molecules including PKA, CaMKII, PKC, p90RSK, and ERK1/2, and measured CREB-S133 phosphorylation.

    • Main Results:

    • TPA uniquely induced CREB-S133 phosphorylation, while ISO activated PKA and ET-1 activated CaMKII.
    • PKC and p90RSK were activated by all three stimuli; however, ERK1/2 inhibition did not affect TPA-induced CREB-S133 phosphorylation.
    • Evidence suggests PKC epsilon (PKCε) translocation to the nucleus mediates CREB phosphorylation specifically upon TPA stimulation.

    Conclusions:

    • Cardiac CREB-S133 phosphorylation is not a multi-signal target as observed in other tissues.
    • PKCε is identified as the primary kinase responsible for CREB-S133 phosphorylation in the murine heart, highlighting signal specificity.