CCK induces apoptosis by stimulating death signaling pathways in rat pancreatic acinar cells, including caspase activation, cytochrome C release, and mitochondrial depolarization [ 68].
We now understand that host immune cells and tissue pathophysiologic "death mechanisms" can stimulate necrosis (death of internal cell organelles) or apoptosis (due to "death programming") cell signalling [ 5].
The complex role of mitochondria in mammalian cell death was highlighted when several studies elucidated resident mitochondrial proteins were able to stimulate cell death directly.
Both proteins form membrane pores through this oligomerization to release effector proteins to stimulate cell death.
Coincident with these activities, astrocytes affect microglial metabolic activities and stimulate cell death pathways.
Whereas proteins of the Bcl-2 family (e.g., Bcl-2, Bcl-xL or Mcl-1) exert antiapoptotic activity, the Bax and Bak proteins stimulate cell death [26].
A general conservation in function between PrgI and the Bcl-2 protein family is readily apparent; both form membrane pores via a helix-turn-helix motif through oligomerization to release effectors to stimulate cell death.
This is consistent with a general conservation in function between PrgI and the Bcl-2 family of proteins that includes Bcl-xL; both form membrane pores through oligomerization using a conserved helix-turn-helix motif to release effectors to stimulate cell death.
We used TNF and Fas antibody to stimulate cell death.
