Northwestern Medicine scientists have demonstrated that cancer cells -- and not normal cells -- can be killed by eliminating either the FAS receptor
, also known as CD95, or its binding component, CD95 ligand.
Various methods to inhibit apoptosis including the cell surface Fas receptor
(FAS) pathway inhibitors (also known as CD95L pathway inhibitor), caspase inhibitors, overexpression of anti-apoptotic genes and small interfering ribonucleic acid (RNA) therapy are discussed.
the study pointed out how protein-protein interactions between Fas receptor
and Fas-associated death domain protein (FADD) mechanistically control DISC formation.
Fas ligand was significantly decreased levels following 15 and 30 minutes stimulation; Fas receptor
decreased at all time points.
Markedly improved survival was also observed when a Fas receptor
fusion protein was injected subcutaneously 12 hours after CLP to act as a decoy for FasL binding.
After ligand binding, Fas receptor
oligomerization results in the activation of caspase-8, which is upstream of caspase-3, causing the activation of apoptosis (Haunstetter and Izumo 1998).