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Science 22 January 1993: Vol. 259. no. 5094, pp. 519 - 522 DOI: 10.1126/science.8424175
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Articles
Science, Vol 259, Issue 5094, 519-522
Copyright © 1993 by American Association for the Advancement of Science
Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta
S Mathias,
A Younes,
CC Kan,
I Orlow,
C Joseph,
and
RN Kolesnick
Laboratory of Signal Transduction, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
The mechanism of interleukin-1 (IL-1) signaling is unknown. Tumor necrosis factor-alpha uses a signal transduction pathway that involves sphingomyelin hydrolysis to ceramide and stimulation of a ceramide-activated protein kinase. In intact EL4 thymoma cells, IL-1 beta similarly stimulated a rapid decrease of sphingomyelin and an elevation of ceramide, and enhanced ceramide-activated protein kinase activity. This cascade was also activated by IL-1 beta in a cell-free system, demonstrating tight coupling to the receptor. Exogenous sphingomyelinase, but not phospholipases A2, C, or D, in combination with phorbol ester replaced IL-1 beta to stimulate IL-2 secretion. Thus, IL-1 beta signals through the sphingomyelin pathway.
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- Ceramide Reduces Endothelium-Dependent Vasodilation by Increasing Superoxide Production in Small Bovine Coronary Arteries.
- D. X. Zhang, A.-P. Zou, and P.-L. Li (2001)
Circ. Res.
88, 824-831
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