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  • Title: Fas/CD95/Apo-I activates the acidic sphingomyelinase via caspases.
    Author: Brenner B, Ferlinz K, Grassmé H, Weller M, Koppenhoefer U, Dichgans J, Sandhoff K, Lang F, Gulbins E.
    Journal: Cell Death Differ; 1998 Jan; 5(1):29-37. PubMed ID: 10200443.
    Abstract:
    Fas/CD95/Apo-I has been shown to stimulate a variety of molecules including several members of the caspase family and the acidic sphingomyelinase (Martin and Green 1995; Gulbins et al, 1995). Here, we demonstrate that Fas receptor-triggered activation of the acidic sphingomyelinase, consumption of sphingomyelin, release of ceramide, and subsequent activation of JNK and p38-K are regulated by caspases. Inhibition of caspases by Ac-YVAD-chloromethylketone or transient CrmA transfection prevented stimulation of acidic sphingomyelinase, release of ceramide and activation of JNK and p38-K upon Fas-receptor crosslinking. Likewise, Fas triggered apoptosis was almost completely blocked by Ac-YVAD-chloromethylketone or CrmA mediated inhibition of caspases. The results suggest a new signalling cascade from the Fas receptor via caspases to acidic sphingomyelinase, ceramide and JNK/p38-K.
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