Ceramide Kinase Regulates the Production of Tumor Necrosis Factor α (TNFα) via Inhibition of TNFα-converting Enzyme *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 286, Issue: 50, Page: 42808-42817
2011
- 60Citations
- 59Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations60
- Citation Indexes60
- 60
- CrossRef49
- Captures59
- Readers59
- 59
Article Description
Tumor necrosis factor α (TNFα) is a well known cytokine involved in systemic and acute inflammation. In this study, we demonstrate that ceramide 1-phosphate (C1P) produced by ceramide kinase (CERK) is a negative regulator of LPS-induced TNFα secretion. Specifically, bone marrow-derived macrophages isolated from CERK knock-out mice ( CERK −/− ) generated higher levels of TNFα than the wild-type mice ( CERK +/+ ) in response to LPS. An increase in basal TNFα secretion was also observed in CERK −/− murine embryonic fibroblasts, which was rescued by re-expression of wild-type CERK. This effect was due to increased secretion and not transcription. The secretion of TNFα is regulated by TNFα-converting enzyme (TACE also known as ADAM17), and importantly, the activity of TACE was higher in cell extracts from CERK −/− as compared with wild type. In vitro analysis also demonstrated that C1P is a potent inhibitor of this enzyme, in stark contrast to ceramide and sphingosine 1-phosphate. Furthermore, TACE specifically bound C1P with high affinity. Finally, several putative C1P-binding sites were identified via homology throughout the protein sequence of TACE. These results indicate that C1P produced by CERK has a negative effect on the processing/secretion of TNFα via modulation of TACE activity.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002192582086997X; http://dx.doi.org/10.1074/jbc.m111.310169; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=83355166948&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22009748; https://linkinghub.elsevier.com/retrieve/pii/S002192582086997X; http://www.jbc.org/lookup/doi/10.1074/jbc.M111.310169; https://syndication.highwire.org/content/doi/10.1074/jbc.M111.310169; https://dx.doi.org/10.1074/jbc.m111.310169; http://www.jbc.org/article/S002192582086997X/abstract; http://www.jbc.org/article/S002192582086997X/fulltext; http://www.jbc.org/article/S002192582086997X/pdf; https://www.jbc.org/article/S0021-9258(20)86997-X/abstract; http://www.jbc.org/cgi/doi/10.1074/jbc.M111.310169; http://www.jbc.org/content/286/50/42808.abstract; http://www.jbc.org/content/286/50/42808.full; http://www.jbc.org/content/286/50/42808.full.pdf; http://www.jbc.org/content/286/50/42808; https://www.jbc.org/content/286/50/42808
Elsevier BV
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