松弛素通过激活人THP-1细胞中的核因子κB诱导基质金属蛋白酶-9。

Relaxin induces matrix metalloproteinase-9 through activation of nuclear factor kappa B in human THP-1 cells.

作者信息

Ho Teh-Yuan, Bagnell Carol A

机构信息

Department of Animal Sciences, Rutgers University, New Brunswick, NJ 08901, USA.

出版信息

Ann N Y Acad Sci. 2005 May;1041:314-6. doi: 10.1196/annals.1282.049.

DOI:10.1196/annals.1282.049

PMID:15956726

Abstract

Matrix metalloproteinase (MMP) and relaxin are important for tissue remodeling and wound repair. Macrophages populate wound sites and secrete MMPs. Nuclear factor kappa B (NF-kappaB) is linked to MMP gene regulation. Thus, a monocyte/macrophage cell line, THP-1, was used to study the mechanism of relaxin's action on MMPs. Relaxin increased MMP-9 protein and activity in THP-1 cell-conditioned media, with no significant change in MMP-2 activity. NF-kappaB DNA binding activity was elevated in response to relaxin, and supershift assay showed activation of both NF-kappaB subunits p50 and p65. Relaxin also reduced NF-kappaB inhibitor protein, IkappaB-alpha. In conclusion, these data suggest that relaxin-induced MMP-9 expression in THP-1 cells involves NF-kappaB activation.

摘要

基质金属蛋白酶（MMP）和松弛素对于组织重塑和伤口修复很重要。巨噬细胞聚集在伤口部位并分泌MMP。核因子κB（NF-κB）与MMP基因调控有关。因此，使用单核细胞/巨噬细胞系THP-1来研究松弛素对MMP作用的机制。松弛素增加了THP-1细胞条件培养基中MMP-9的蛋白和活性，而MMP-2活性没有显著变化。响应松弛素，NF-κB DNA结合活性升高，超迁移分析显示NF-κB亚基p50和p65均被激活。松弛素还降低了NF-κB抑制蛋白IκB-α。总之，这些数据表明，松弛素诱导THP-1细胞中MMP-9的表达涉及NF-κB的激活。