Abstract
Elevated expression of phospholipase D (PLD) in rat fibroblasts overexpressing a tyrosine kinase leads to cell transformation. However, it has been difficult to get elevated expression of PLD in normal rat fibroblasts. Using transient transfection and an inducible expression system, we were able to get elevated expression of PLD1 and PLD2 in 3Y1 rat fibroblasts. Elevated expression of either PLD1 or PLD2 in 3Y1 cells led to apoptosis in the absence of serum. Elevated PLD expression resulted in reduced cell viability and the cleavage of the caspase 3 substrates poly-ADP-ribose polymerase (PARP) and protein kinase C δ. Elevated PLD expression also stimulated cytochrome c release, indicating that the mitochondrial apoptosis pathway was activated. Thus, while elevated PLD expression can transform cells with elevated tyrosine kinase expression, elevated expression of PLD activity in normal cells renders cells sensitive to apoptotic insult.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 474-477 |
| Number of pages | 4 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 298 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2002 |
| Externally published | Yes |
Bibliographical note
Funding Information:We thank M. Frohman (SUNY, Stony Brook) for the hPLD1 and mPLD2 genes used to generate the inducible PLD expression vectors. This investigation was supported by National Institutes of Health Grant CA46677. Research Centers in Minority Institutions award RR-03037 from the National Center for Research Resources of the National Institutes of Health, which supports infrastructure and instrumentation in the Biological Sciences Department at Hunter College, is also acknowledged.