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Endotoxin activates de novo sphingolipid biosynthesis via nuclear factor kappa B-mediated upregulation of Sptlc2

文献类型： 外文期刊

作者： Chang, Zhi-Qiang 1 ; Lee, Su-Yeon 1 ; Kim, Hye-Jin 1 ; Kim, Jung Ran 1 ; Kim, Su-Jung 1 ; Hong, In-Kyung 1 ; Oh, Byung 1 ;

作者机构： 1.Gachon Univ Med & Sci, Lee Gil Ya Canc & Diabet Inst, Dept Mol Med, Inchon 406840, South Korea

2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China

3.Columbia Univ, Dept Med, Div Prevent Med & Nutr, New York, NY 10032 US

关键词： Inflammation;Ceramide;Serine palmitoyltransferase;Macrophage;NF kappa B

期刊名称：PROSTAGLANDINS & OTHER LIPID MEDIATORS （ 影响因子：3.072； 五年影响因子：3.393 ）

ISSN： 1098-8823

年卷期： 2011 年 94 卷 1-2 期

页码：

收录情况： SCI

摘要： Sphingolipids are membrane components and are involved in cell proliferation, apoptosis and metabolic regulation. In this study we investigated whether de novo sphingolipid biosynthesis in macrophages is regulated by inflammatory stimuli. Lipopolysaccharide (LPS) treatment upregulated Sptlc2, a subunit of serine palmitoyltransferase (SPT), mRNA and protein in Raw264.7 and mouse peritoneal macrophages, but Sptlc1, another subunit of SPT, was not altered. SPT activation by LPS elevated cellular levels of ceramides and sphingomyelin (SM). Pharmacological inhibition of nuclear factor kappa B (NF kappa B) prevented LPS-induced upregulation of Sptlc2 while transfection of p65 subunit of NF kappa B upregulated Sptlc2 and increased cellular ceramide levels. In contrast, MAP kinases were not involved in regulation of sphingolipid biosynthesis. Analysis of Sptlc2 promoter and chromatin immunoprecipitation (ChIP) assay showed that NF kappa B binding sites are located in Sptlc2 promoter region. Our results demonstrate that inflammatory stimuli activate de novo sphingolipid biosynthesis via NF kappa B and may play a critical role in lipid metabolism in macrophages. Crown Copyright (C) 2010 Published by Elsevier Inc. All rights reserved.

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