Tumor necrosis factor α stimulates sphingomyelinase through the 55 kDa receptor in HL‐60 cells

Yanaga, Fumi; Watson, Steve P.

doi:10.1016/0014-5793(92)81493-6

Cited by 62 publications

(40 citation statements)

References 23 publications

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“…2B). In accordance with previous observations on fibroblasts (39) or leukemic cells (9,10,46), TNF-␣ also caused a considerable (20%) breakdown of phosphatidylcholine, parallel to the SPM cycle, which also occurred at 14°C (Fig. 2A).…”

Section: Low Temperatures and Hypertonic Media Inhibit Receptormediatsupporting

confidence: 92%

“…Indeed, down-modulation of the TNF receptors is a result of the internalization of p60 receptor (60). Since the p60 receptor triggers the SPM pathway (10,13,61), it is therefore likely that, under conditions where internalization is blocked, the reversibility of SPM degradation is not due to down-regulation of the TNF receptor.…”

Section: Low Temperatures and Hypertonic Media Inhibit Receptormediatmentioning

confidence: 99%

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Low Temperatures and Hypertonicity Do Not Block Cytokine-induced Stimulation of the Sphingomyelin Pathway but Inhibit Nuclear Factor-κB Activation

Andrieu

Salvayre

Jaffrézou

et al. 1995

Journal of Biological Chemistry

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In order to better understand the significance of tumor necrosis factor-␣ (TNF-␣) and interleukin-1␤ (IL-1␤)-receptor internalization in the sphingomyelin pathway signal transduction, we investigated receptor signaling under conditions in which receptor internalization is blocked. We demonstrate that human recombinant TNF-␣ and IL-1␤ both induced sphingomyelin and phosphatidylcholine hydrolysis at either 4, 14, or 37°C in human skin fibroblasts and U937 monocytic cells. Cytokine-induced sphingomyelin degradation also occurred when endocytosis was inhibited by incubating the cells in hypertonic medium. While internalization was not required for the production of ceramide, activation of the transcription factor NF-B was strongly reduced when cells were stimulated with TNF at low temperature or in hypertonic medium. Under these conditions, activation of NF-B by the cell-permeant C 2 -ceramide (N-acetylsphingosine), by exogenous sphingomyelinase or by phorbol myristate acetate was also inhibited. These results suggest that low temperature and hypertonicity, two inhibitors of receptor internalization: (i) do not affect the TNF-␣-or IL-1␤-induced sphingomyelin hydrolysis, but (ii) do inhibit a step distal to ceramide of the intracellular signaling pathway leading to NF-B activation.

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Section: Low Temperatures and Hypertonic Media Inhibit Receptormediatsupporting

confidence: 92%

Section: Low Temperatures and Hypertonic Media Inhibit Receptormediatmentioning

confidence: 99%

Low Temperatures and Hypertonicity Do Not Block Cytokine-induced Stimulation of the Sphingomyelin Pathway but Inhibit Nuclear Factor-κB Activation

Andrieu

Salvayre

Jaffrézou

et al. 1995

Journal of Biological Chemistry

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“…Concurrently with sphingomyelin hydrolysis, TNF-a is known to stimulate PtdCho degradation [28,29,33,43,4.51 (see also Figs 1, 2, 4 and 6). …”

Section: Since Incorporation Of [3h]choline Into Sphingomyelin Is a Tmentioning

confidence: 97%

Comparative Study of the Metabolic Pools of Sphingomyelin and Phosphatidylcholine Sensitive to Tumor Necrosis Factor

Andrieu

Salvayre

Levade

1996

European Journal of Biochemistry

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The metabolism and localization of the pools of sphingomyelin and phosphatidylcholine (PtdCho) which are hydrolyzed upon activation of the sphingomyelin signal transduction pathway were studied in human skin fibroblasts treated with tumor necrosis factor a (TNF-a). In a first series of experiments, cellular phospholipids were labeled with [3H]choline under conditions that inhibit the vesicular traffic to the plasma membrane. Thus, in human fibroblasts metabolically labeled in the presence of brefeldin A, monensin or at 20°C, the arrival of newly synthesized sphingomyelin to the cell surface was prevented, supporting previous conclusions for a vesicular mechanism of sphingomyelin transport to the plasma membrane. Under these conditions, TNF-a induced the hydrolysis of PtdCho but did not promote the hydrolysis of 3H-labeled sphingomyelin, suggesting that the sphingomyelin signaling pool resides in a compartment distal to the Golgi apparatus, and possibly in the plasma membrane. TNF was also unable to trigger the breakdown of a radioactive sphingomyelin, [cerumide-'Hlsphingomyelin, exogenously added to the cells to label the exoplasmic side of the cell surface. However, TNF caused PtdCho and sphingomyelin degradation in fibroblasts that had been treated with bacterial sphingomyelinase to degrade the sphingomyelin pool of the external leaflet of the plasma membrane. A similar result was obtained at 4"C, i.e. under conditions which inhibit endocytosis, thereby excluding the endosomes as a potential site for TNF-induced sphingomyelin hydrolysis. Altogether, these results strongly argue for a localization of the sphingomyelin signaling pool at the inner leaflet of the plasma membrane, but neither in the endolysosoma1 nor the Golgi compartments. In addition, when ['Hlcholine-labeled fibroblasts were treated under non-lytic conditions with bacterial phospholipase C to degrade the external pool of PtdCho, TNF was still able to stimulate the hydrolysis of PtdCho. This demonstrates that the pool of PtdCho involved in TNF-a signaling (and which is hydrolyzed concurrently with sphingomyelin to generate diacylglycerol), is not located in the outer leaflet of the plasma membrane.

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“…However, other reports indicate no changes in ceramide with TNF-␣ for several hours (24). There is also some controversy as to whether this sphingomyelinase activity is plasma membrane-bound, cytosolic, or lysosomal, or some combination of these (14,23,25,26), but many models proposed rely on this rapid (5-30 min) switching on and off of sphingomyelinase to activate the apoptotic signal. Contrary to the model, several laboratories have reported that ceramide is not necessary for TNF-␣ activation of nuclear factor-B and that the observed effects of ceramide might be nonphysiological (27)(28)(29)(30).…”

mentioning

confidence: 99%

Anti-immunoglobulin-induced Apoptosis in WEHI 231 Cells Involves the Slow Formation of Ceramide from Sphingomyelin and Is Blocked by bcl-xL

Wiesner

Kilkus²,

Gottschalk

et al. 1997

Journal of Biological Chemistry

116

119

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Prolonged (>24 h) exposure to anti-IgM (an antigen surrogate that induces membrane cross-linking and apoptosis) induced a 3-fold increase in the mass of endogenous ceramide measured by 32 P labeling by diacylglycerol kinase and a 4-fold increase in ceramide as measured by metabolic labeling with [ 3 H]palmitate in a B-lymphocyte cell line, WEHI 231. This correlated with the induction of apoptosis. Shorter exposure times to anti-IgM (up to 8 h) failed to elicit apoptosis and did not elicit increased ceramide formation. After 8 h, apoptosis occurs concomitantly with ceramide formation over the next 40 h. Further, we showed that exogenous ceramide mimicked anti-IgM-induced apoptosis and that apoptosis was potentiated in serum-free media. Treatment of cells with an inhibitor of ceramide catabolism, Noleoylethanolamine, increased both ceramide formation and apoptosis and accelerated apoptosis induced by anti-IgM. To examine further how ceramide metabolism is involved in apoptosis, we derived cell lines from a small population of cells resistant to N-oleoylethanolamine. These cell lines were selected based on an altered ceramide metabolic pathway, were resistant to apoptosis induced by anti-IgM, and showed no significant increase in ceramide when challenged with anti-IgM. The basis of this resistance was shown to be the failure to activate neutral sphingomyelinase activity following 24-h treatment with anti-IgM, in contrast to the 2-fold increase in neutral sphingomyelinase activity observed in wild type cells. We have shown previously that transfection of WEHI cells with bcl-x L conferred resistance to anti-IgMinduced apoptosis, whereas transfection with bcl-2 did not (Gottschalk, A., Boise, L., Thompson, C., and Quintans, J. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 7350 -7354). In this study, these bcl-x L transfectants also displayed increased resistance to exogenous N-acetylsphingosine (C 2 -ceramide) or N-hexanoylsphingosine (C 6 -ceramide). However, when challenged with anti-IgM the bcl-x L transfectants produced levels of ceramide similar to wild type cells, suggesting that ceramide formation is upstream of bcl-x L and that it is a major determinant of B-cell death.Apoptosis (1) can be induced readily in lymphocytes by means of irradiation, corticosteroids, or cross-linking of their antigen receptors. The apoptotic response of the murine Blymphoma WEHI 231 cell line to the cross-linking of surface IgM receptors provides a model to study the induction of physiological cell death (apoptosis) in lymphocytes (2-4). In WEHI 231, the response is specifically triggered via surface IgM since cross-linking other surface proteins such as IgD, Fc receptor, or major histocompatibility complex class II have no effect (5). Apoptosis is reversed by both phorbol esters and by bacterial lipopolysaccharide (6). Apoptosis can also be reversed by the removal of the antigen prior to 12 h of exposure, emphasizing its slow acting nature compared with necrosis and some types of apoptosis. We showed recently that the time course and ...

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Tumor necrosis factor α stimulates sphingomyelinase through the 55 kDa receptor in HL‐60 cells

Cited by 62 publications

References 23 publications

Low Temperatures and Hypertonicity Do Not Block Cytokine-induced Stimulation of the Sphingomyelin Pathway but Inhibit Nuclear Factor-κB Activation

Low Temperatures and Hypertonicity Do Not Block Cytokine-induced Stimulation of the Sphingomyelin Pathway but Inhibit Nuclear Factor-κB Activation

Comparative Study of the Metabolic Pools of Sphingomyelin and Phosphatidylcholine Sensitive to Tumor Necrosis Factor

Anti-immunoglobulin-induced Apoptosis in WEHI 231 Cells Involves the Slow Formation of Ceramide from Sphingomyelin and Is Blocked by bcl-xL

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