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Related Experiment Videos

Altered kinase C function in transformed BALB/c3T3 cells.

H C Yang1

  • 1Division of Medical Oncology, Harbor-UCLA Medical Center, Torrance 90509.

Experimental Cell Research
|July 1, 1989
PubMed
Summary
This summary is machine-generated.

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Kinase C activity, marked by an 80-kDa phosphoprotein (pp80), was reduced in transformed mouse cells. This decrease was linked to kinase C

Area of Science:

  • Cell biology
  • Biochemistry
  • Cancer research

Background:

  • Protein kinase C (PKC) plays a crucial role in cellular signaling pathways.
  • Altered PKC activity is implicated in the transformation of cells by oncogenes and carcinogens.
  • Understanding PKC function in transformed cells is vital for cancer research.

Purpose of the Study:

  • To compare protein kinase C (PKC) function in untransformed and chemically or virally transformed mouse fibroblast cell lines.
  • To investigate the phosphorylation of an 80-kDa substrate protein (pp80) as a marker for PKC activity.
  • To determine the impact of cell transformation on PKC levels and substrate phosphorylation.

Main Methods:

  • Comparative analysis of PKC function in A31 (untransformed) and BPA31, DA31, KA31 (transformed) BALB/c 3T3 cell lines.

Related Experiment Videos

  • Measurement of 80-kDa kinase C dependent phosphoprotein (pp80) levels as an in vivo marker of PKC activity.
  • Assessment of total cell lysate PKC levels and substrate protein amounts.
  • Evaluation of PKC affinity for cellular fractions.

    • Main Results:

    • The 80-kDa kinase C dependent phosphoprotein (pp80) was significantly decreased in all transformed cell lines compared to untransformed cells.
    • While the 80-kDa substrate protein level was similar in BPA31 and A31 cells, pp80 phosphorylation was reduced in BPA31 cells.
    • Total cell lysate PKC levels were lower in transformed cells, but this difference did not fully explain the reduced pp80 phosphorylation.
    • Increased affinity of PKC for the membrane fraction in BPA31 cells was observed, potentially explaining decreased pp80 phosphorylation.

    Conclusions:

    • Cell transformation leads to a marked decrease in kinase C activity, as indicated by reduced pp80 phosphorylation.
    • The observed decrease in PKC activity is not solely due to lower total PKC levels in transformed cells.
    • Altered subcellular localization of kinase C, specifically increased membrane affinity, may contribute to the diminished phosphorylation of pp80 in transformed cells.