Matrix metalloproteinase-1 expression induced by IL-1β requires acid sphingomyelinase

被引:20
作者
Bauer, Jessica [1 ]
Huy, Christian [1 ]
Brenmoehl, Julia [2 ]
Obermeier, Florian [1 ]
Bock, Juergen [1 ]
机构
[1] Univ Hosp Regensburg, Dept Internal Med 1, D-93042 Regensburg, Germany
[2] Univ Hosp Jena, Dept Internal Med 2, Jena, Germany
关键词
Extracellular matrix degradation; Collagen breakdown; Ceramide; Inflammation; Lipid metabolism; Imipramine; NF-KAPPA-B; INFLAMMATORY-BOWEL-DISEASE; PROTEIN-KINASE PATHWAYS; COLLAGENASE MMP-1; INDUCED APOPTOSIS; BINDING-PROTEIN; TERMINAL KINASE; CERAMIDE; ACTIVATION; FIBROBLAST;
D O I
10.1016/j.febslet.2009.02.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Matrix metalloproteinase-1 (MMP-1) is increased in inflammatory conditions leading to destruction of extracellular matrix. Many inflammatory stimuli activate sphingomyelinases (SMases), which generate ceramide. We aimed to de. ne the relevance and type of SMase responsible for the regulation of MMP-1. Acid sphingomyelinase (ASM)-deficient human fibroblasts failed to phosphorylate extracellular signal-regulated kinase (ERK), or upregulate MMP-1 mRNA and protein expression upon stimulation with interleukin-1 beta (IL-1 beta), whereas phosphorylation of p38 mitogen-activated protein kinase and IL-8 production remained unaffected. Transfection of ASM restored MMP-1 production. Addition of exogenous SMase was sufficient to restore activation of ERK and increase MMP-1 mRNA. Inhibition of ASM with imipramine completely abrogated MMP-1 induction. The results suggest that IL-1 beta-induced expression of MMP-1 is dependent on ASM. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:915 / 920
页数:6
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