Hofmeister, Robert and Wiegmann, Katja and Korherr, Christian and Bernardo, Katussevani and Krönke, Martin and Falk, Werner (1997) Activation of acid sphingomyelinase by interleukin-1 (IL-1) requires the IL-1 receptor accessory protein. JOURNAL OF BIOLOGICAL CHEMISTRY, 272 (44). pp. 27730-27736. ISSN 0021-9258, 1083-351X
Full text not available from this repository.Abstract
The cytokine interleukin-1 (IL-1) plays an important role in inflammation and regulation of immune responses, but the mechanisms of its signal transduction and cell activation processes are incompletely understood. Ceramide generated by sphingomyelinases (SMases) is known to function as an important second messenger molecule in the signaling pathway of IL-1 and tumor necrosis factor. To investigate the activation of SMases by IL-1, we used an IL-1 receptor type I (IL-1RI)-positive EL4 thymoma cell line, which is defective in IL-1R accessory protein (IL-1RAcP) expression. In this cell line (EL4D6/76), tumor necrosis factor induced ligand/receptor internalization, NF kappa B nuclear translocation, IL-2 production, and the activation of neutral (N)-SMase and acid (A)-SMase. In contrast, stimulation with IL-1 resulted only in the activation of N-SMase whereas ligand/receptor internalization, NF kappa B translocation, IL-2 production, and activation of A-SMase were not detected. Transfection of this functionally defective EL4D6/76 with IL-1RAcP cDNA restored these functions. These data suggest that A-SMase activity is strongly linked with the internalization of IL-1RI mediated by IL-1RAcP and that A-SMase and N-SMase are activated by different pathways.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TUMOR-NECROSIS-FACTOR; KAPPA-B ACTIVATION; CELL-FREE SYSTEM; SIGNAL-TRANSDUCTION; FACTOR-ALPHA; NEUTRAL SPHINGOMYELINASE; GROWTH SUPPRESSION; GENE-EXPRESSION; CYTO-TOXICITY; T-CELLS |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Innere Medizin I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 18 Oct 2023 09:43 |
| Last Modified: | 18 Oct 2023 09:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50467 |
Actions (login required)
 |
View Item |
