Fig. 4: N-terminal domain of FasL is essential for its translocation to raft and cell-death activation | Cell Death & Disease

Fig. 4: N-terminal domain of FasL is essential for its translocation to raft and cell-death activation

From: Impairment of Fas-ligand–caveolin-1 interaction inhibits Fas-ligand translocation to rafts and Fas-ligand-induced cell death

Fig. 4

a The distribution of wild-type and mutant forms of FasL between raft (4–6) and non-raft (9,10) fractions was assessed using corresponding antibodies. b Expression levels of FasL and its mutant forms in the specified time periods were estimated by immunoblot analysis with anti-FasL Abs. Survival of HeLa cells overexpressing FasL variants, incubated with tetracycline during the indicated intervals (chart). Cell viability was determined by the neutral-red uptake assay. Results are presented as mean ± s.e.m of three independent experiments (each in triplicate). c Caveolin-1 knockdown by siRNA in HeLa-pcDNA4/TO-FasL cells decreases FasL cytotoxic effect. HeLa-pcDNA4/TO-FasL cells were transfected with psiRNA-h7SK-caveolin or psiRNA-h7SK-scramble control. Cell lysates were stained with anti-FasL mAbs (upper panel) and anti-caveolin-1 Abs (lower panel). Survival of HeLa-pcDNA4/TO-FasL cells transfected with psiRNA-h7SK-caveolin or psiRNA-h7SK-scramble control (chart). Cell viability was determined by the neutral-red uptake method. Results are presented as mean ± s.e.m. of four experiments (each in triplicate)

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