Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation

Biochem Biophys Res Commun. 1998 Oct 9;251(1):199-203. doi: 10.1006/bbrc.1998.9422.


Cathepsin D, a lysosomal aspartic proteinase, has been shown to induce apoptosis of HeLa cells when overexpressed. To further understand regulatory mechanisms of cathepsin D-induced cell death, we examined whether lysosomal cysteine and aspartic proteinases are involved in apoptosis of PC12 cells following serum deprivation. In serum deprived culture, PC12 cells overexpressing cathepsin D died more rapidly than wild-type cells. When the active forms of cathepsins B and D were examined during the apoptotic process of wild-type cells, the amount of cathepsin B was drastically reduced 24 hr after the onset of culture, whereas that of cathepsin D considerably increased. The viability of PC12 cells overexpressing cathepsin B was significantly higher in serum-deprived culture than wild-type cells. In this situation, the amount of the cathepsin B protein did not decrease. The results suggest that there exists an apoptotic pathway regulated by lysosomal cathepsins B and D.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • Cathepsin B / physiology*
  • Cathepsin D / physiology*
  • Cell Survival / drug effects
  • Cells, Cultured
  • Culture Media, Serum-Free / pharmacology
  • In Situ Nick-End Labeling
  • Lysosomes / enzymology
  • Nerve Growth Factors / pharmacology
  • PC12 Cells / cytology
  • PC12 Cells / drug effects
  • PC12 Cells / enzymology*
  • Rats


  • Culture Media, Serum-Free
  • Nerve Growth Factors
  • Cathepsin B
  • Cathepsin D