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pPKCδ activates SC35 splicing factor during H9c2 myoblastic differentiation

Susi Zara1, Mirella Falconi, Monica Rapino

  • 1Department of Drug Sciences, Faculty of Pharmacy, University G d'Annunzio, Chieti-Pescara, Italy. s.zara@unich.it

Histology and Histopathology
|December 1, 2010
PubMed

Insights

Phosphorylated Protein Kinase C delta (pPKCδ) interacts with splicing factor SC35 in the nucleus, activating transcription and influencing cardiomyoblast differentiation. This PKCδ-SC35 interaction is key to cardiac cell development.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cardiovascular Research

Background:

  • Protein Kinase C (PKC) isoforms are crucial for cardiac development and aging.
  • The nuclear interactions of PKC isoforms with specific substrates, like splicing factors, remain understudied.

Purpose of the Study:

  • Investigate the expression, localization, and interaction of PKC isoforms (α, δ, ε, ζ) with splicing factor SC35.
  • Determine the role of PKC isoforms in modulating the transcription machinery during cardiomyoblast differentiation.

Main Methods:

  • Utilized H9c2 cells induced to myoblast differentiation.
  • Employed western blotting, co-immunoprecipitation, and electron microscopy for analysis.
  • Assessed expression, distribution, and interaction of PKC isoforms and SC35.

Main Results:

  • PKCδ was the most expressed isoform in differentiated H9c2 cells.
  • Phosphorylated PKCδ (pPKCδ) showed increased nuclear interaction and co-localization with SC35.
  • No significant changes in PKCδ and SC35 distribution were observed between different serum conditions.

Conclusions:

  • pPKCδ activation of SC35 suggests a direct role in modulating transcription via nuclear interaction.
  • The pPKCδ-SC35 nuclear co-localization is critical for downstream transcriptional changes.
  • This interaction influences morphological modifications associated with cardiomyoblast differentiation.

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