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J Biol Chem, Vol. 273, Issue 47, 31245-31251, November 20, 1998
From the Institute of Cell Biology and Immunology, University of
Stuttgart, D-70569 Stuttgart, Germany, and The role, origin, and mode of action of the lipid
messenger ceramide in programmed cell death and its linkage to
receptor-associated apoptotic signal proteins is still unresolved. We
show here in Kym-1 rhabdomyosarcoma cells that tumor necrosis factor
(TNF)-induced apoptosis is preceded by a multiphasic increase in
intracellular ceramide levels. Distinct enzymes were found to
contribute to three waves of ceramide, neutral sphingomyelinase,
ceramide synthase, and acid sphingomyelinase, with peak activities at
1-2, 40, and around 200 min, respectively, the latter coinciding with
progression to irreversible damage. In parallel with ceramide
generation, TNF-mediated inhibition of glucosylceramide and
sphingomyelin (SM) synthase prevents the immediate metabolization of
this lipid mediator. In the presence of
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone (Z-VAD-fmk) or
benzyloxycarbonyl-Asp-Glu-Val-Asp-chloromethyl ketone (Z-DEVD-cmk), a
broad spectrum and a caspase 3-selective inhibitor, respectively,
glucosylceramide and SM synthase activity remains unaffected by TNF,
and intracellular ceramide accumulation is not observed. Our results
show that several lipid enzymes contribute to generation of ceramide in
response to TNF and identify glucosylceramide and SM synthase as
important regulators of the kinetics and magnitude of intracellular
ceramide accumulation. As glucosylceramide and SM synthase activity is
caspase-sensitive, our data suggest a novel functional link between
caspase(s) and ceramide during apoptotic processes.
Tumor Necrosis Factor Induces Ceramide Oscillations and
Negatively Controls Sphingolipid Synthases by Caspases in Apoptotic
Kym-1 Cells
er,
, Institute for
Organic Chemistry and Biochemistry, University of Bonn,
D-53121 Bonn, Germany
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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