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J Biol Chem, Vol. 273, Issue 18, 11313-11320, May 1, 1998
-induced Cell Death
§,
,,§,§**, and§
From the Departments of Tumor necrosis factor- TNF Medicine and
§ Cell Biology, Duke University Medical Center, Durham,
North Carolina 27710, the ** Veterans Administration Geriatrics Research
and Clinical Center, Durham, North Carolina 27710, and
Laboratoire de Biochimie, Institut Louis Bugnard,
31403 Toulouse, France
(TNF)-induced cell
death involves a diverse array of mediators and regulators including
proteases, reactive oxygen species, the sphingolipid ceramide, and
Bcl-2. It is not known, however, if and how these components are
connected. We have previously reported that GSH inhibits, in
vitro, the neutral magnesium-dependent
sphingomyelinase (N-SMase) from Molt-4 leukemia cells. In this study,
GSH was found to reversibly inhibit the N-SMase from human mammary
carcinoma MCF7 cells. Treatment of MCF7 cells with TNF induced a
marked decrease in the level of cellular GSH, which was accompanied by
hydrolysis of sphingomyelin and generation of ceramide. Pretreatment of
cells with GSH, GSH-methylester, or N-acetylcysteine, a
precursor of GSH biosynthesis, inhibited the TNF-induced
sphingomyelin hydrolysis and ceramide generation as well as cell death.
Furthermore, no significant changes in GSH levels were observed in MCF7
cells treated with either bacterial SMase or ceramide, and GSH did not
protect cells from death induced by ceramide. Taken together, these
results show that GSH depletion occurs upstream of activation of
N-SMase in the TNF signaling pathway.
has been shown to activate at least two groups of caspases
involved in the initiation and "execution" phases of apoptosis. Therefore, additional studies were conducted to determine the relationship of GSH and the death proteases. Evidence is provided to
demonstrate that depletion of GSH is dependent on activity of
interleukin-1
-converting enzyme-like proteases but is upstream of
the site of action of Bcl-2 and of the execution phase caspases. Taken
together, these studies demonstrate a critical role for GSH in TNF
action and in connecting major components in the pathways leading to
cell death.
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