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

被引:19
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
来源
FEBS LETTERS | 2009年 / 583卷 / 05期
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
相关论文
共 40 条
  • [1] ALBOUZ S, 1981, BIOMED EXPRESS, V35, P218
  • [2] Matrix metalloproteinase levels are elevated in inflammatory bowel disease
    Baugh, MD
    Perry, MJ
    Hollander, AP
    Davies, DR
    Cross, SS
    Lobo, AJ
    Taylor, CJ
    Evans, GS
    [J]. GASTROENTEROLOGY, 1999, 117 (04) : 814 - 822
  • [3] Bu Shizhong, 2006, FASEB J, V20, P184
  • [4] CHURCHMEN EH, 2007, J INHERIT METAB DIS, V30, P654
  • [5] IL-17 stimulates MMP-1 expression in primary human cardiac fibroblasts via p38 MAPK- and ERK1/2-dependent C/EBP-β, NF-κB, and AP-1 activation
    Cortez, Dolores M.
    Feldman, Marc D.
    Mummidi, Srinivas
    Valente, Anthony J.
    Steffensen, Bjorn
    Vincenti, Matthew
    Barnes, Jeffrey L.
    Chandrasekar, Bysani
    [J]. AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, 2007, 293 (06): : H3356 - H3365
  • [6] Cytokine-suppressive anti-inflammatory drugs (CSAIDs) inhibit invasion and MMP-1 production of ovarian carcinoma cells
    Denkert, C
    Koch, I
    Berger, S
    Köbel, M
    Siegert, A
    Hauptmann, S
    [J]. CANCER LETTERS, 2003, 195 (01) : 101 - 109
  • [7] Purification, localization, and expression of human intestinal alkaline sphingomyelinase
    Duan, RD
    Cheng, YJ
    Hansen, G
    Hertervig, E
    Liu, JJ
    Syk, I
    Sjöström, H
    Nilsson, Å
    [J]. JOURNAL OF LIPID RESEARCH, 2003, 44 (06) : 1241 - 1250
  • [8] Ceramide- and ERK-dependent pathway for the activation of CCAAT/enhancer binding protein by interleukin-1β in hepatocytes
    Giltiay, NV
    Karakashian, AA
    Alimov, AP
    Ligthle, S
    Nikolova-Karakashian, MN
    [J]. JOURNAL OF LIPID RESEARCH, 2005, 46 (11) : 2497 - 2505
  • [9] Sphingomyelinases:: enzymology and membrane activity
    Goñi, FM
    Alonso, A
    [J]. FEBS LETTERS, 2002, 531 (01) : 38 - 46
  • [10] Acidic sphingomyelinase mediates entry of N-gonorrhoeae into nonphagocytic cells
    Grassme, H
    Gulbins, E
    Brenner, B
    Ferlinz, K
    Sandhoff, K
    Harzer, K
    Lang, F
    Meyer, TF
    [J]. CELL, 1997, 91 (05) : 605 - 615