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Negative regulation of phosphatidylinositol 3-kinase and Akt signalling pathway by PKC

Hui C Wen1, Wan C Huang, Adnan Ali

  • 1Department of Pharmacology, College of Medicine, National Taiwan University, Taipei, Taiwan.

Cellular Signalling
|October 29, 2002
PubMed

Insights

Protein Kinase C (PKC) negatively regulates the phosphatidylinositol 3-kinase/Akt signaling pathway. PKC inhibition increases Akt phosphorylation, while activation by PMA attenuates it, clarifying PKC

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Biochemistry

Background:

  • The regulation of the phosphatidylinositol 3-kinase/Akt cascade is complex.
  • The specific role of protein kinase C (PKC) in this pathway remains unclear.

Purpose of the Study:

  • To investigate the role of protein kinase C (PKC) in regulating the phosphatidylinositol 3-kinase/Akt signaling pathway.

Main Methods:

  • Utilized A549 and HEK293 cell lines.
  • Employed PKC inhibitors (Ro 31-8220, bisindolylmaleimide VIII, LY 379196) and activators (PMA).
  • Assessed Akt/PKB phosphorylation, integrin-linked kinase (ILK) activity, and effects of inhibitors for phosphatidylinositol 3-kinase (PI3K), PIP(3)-dependent kinases (PDK), and phosphatases (PP2A, PP2B).

Main Results:

  • PKC inhibition led to increased Akt/PKB phosphorylation at Ser 473 and enhanced ILK activity.
  • Increased Akt phosphorylation was dependent on PI3K and PDK activity.
  • PMA treatment attenuated Akt/PKB phosphorylation.
  • PKC inhibition did not affect phosphatase activity.

Conclusions:

  • Protein kinase C (PKC) negatively regulates the phosphatidylinositol 3-kinase/Akt signaling pathway.
  • This study elucidates a novel regulatory mechanism within a critical cellular signaling network.

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