Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta
Autor: | Cecil K. Joseph, Anas Younes, Richard Kolesnick, Shalini Mathias, Chu-Cheng Kan, Irene Orlow |
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Rok vydání: | 1993 |
Předmět: |
Ceramide
Thymoma Molecular Sequence Data Sphingomyelin phosphodiesterase Biology Ceramides Substrate Specificity chemistry.chemical_compound Mice ENPP7 Tumor Cells Cultured Animals Amino Acid Sequence Beta (finance) Protein kinase A Receptor Multidisciplinary Cell-Free System Dose-Response Relationship Drug Thymus Neoplasms Cell biology Sphingomyelins Kinetics Sphingomyelin Phosphodiesterase Biochemistry chemistry Type C Phospholipases Interleukin-2 Signal transduction Sphingomyelin Protein Kinases Interleukin-1 Signal Transduction |
Zdroj: | Science (New York, N.Y.). 259(5094) |
ISSN: | 0036-8075 |
Popis: | 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. |
Databáze: | OpenAIRE |
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