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Activates NF-
B in Acid
Sphingomyelinase-deficient Mouse Embryonic Fibroblasts
(Received for publication, December 18, 1996, and in revised form, February 14, 1997)
From the Neuroscience Laboratory, Institute of Biochemistry,
Faculty of Medicine, University of Cologne,
Joseph-Stelzmann-Strasse 52, D-50931 Cologne, Germany
Tumor necrosis factor 
(TNF-) is one of the
most potent inducer of the nuclear transcription factor 
B (NF-B).
Activation of NF-B is initiated by phosphorylation of the inhibitory
subunit of the IB--NF-B complex. This leads to the
dissociation of the complex and degradation of IB-. NF-B is
translocated into the nucleus. The sphingomyelin pathway is thought to
mediate the TNF--induced activation of NF-B by its second
messenger ceramide. We have used the recently established acid
sphingomyelinase-deficient mouse line
(asmase
/ mice) to evaluate the role of acid
sphingomyelinase in the TNF--induced signal transduction pathway.
Here we present experimental evidence that acid sphingomyelinase is not
involved in the TNF--induced activation of NF-B. TNF-
treatment induced the dissociation and degradation of IB- and the
nuclear translocation of NF-B in embryonic fibroblasts derived from
asmase/ and wild type mice
indiscriminately.
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