Siemianowicz Krzysztof, Gminski Jan, Goss Malgorzata, Francuz Tomasz, Likus Wirginia, Jurczak Teresa, Garczorz Wojciech
Department of Biochemistry, Silesian Medical University, 40-752 Katowice, Poland.
Exp Ther Med. 2010 Nov;1(6):1057-1060. doi: 10.3892/etm.2010.157. Epub 2010 Sep 29.
Matrix metalloproteases (MMPs) are a family of zinc-dependent endopeptidases that degrade extracellular matrix proteins. MMP-1 and MMP-2 are produced by endothelial cells and are involved in specific vascular pathologies, including atherosclerosis and aortal aneurysm. One of the most important differences between these two metalloproteases is the possibility of hydrolysis of elastin and collagen type IV by MMP-2, but not by MMP-1. Elastin-derived peptides are generated as a result of the degradation of elastin fibers. The aim of our study was to compare the production of MMP-1 and MMP-2 in cultured human arterial endothelial cells derived from vascular pathologies localized at three different sites, the coronary artery, iliac artery and aorta, measured as their concentration in cell culture medium. The second aim was to evaluate the influence of κ-elastin (at concentrations 0.1, 0.4, 1.0, 2.5 or 5.0 μg/ml) on the production of the evaluated metalloproteases in three endothelial cell lines. The production of MMP-1 was statistically significantly greater in endothelial cells derived from the aorta compared to that in the endothelium obtained from the coronary and iliac arteries. There were no statistically significant differences in the production of MMP-2 among the endothelial cell lines tested. The addition of κ-elastin at all evaluated concentrations did not statistically significantly influence the concentration of MMP-1 in the cultured coronary artery endothelium. Furthermore, no statistically significant differences were observed in the cultured iliac artery endothelium. In the cultured endothelium derived from the aorta, κ-elastin at concentrations of 0.1 and 0.4 μg/ml significantly increased the amount of MMP-1.
基质金属蛋白酶（MMPs）是一类锌依赖性内肽酶，可降解细胞外基质蛋白。MMP-1和MMP-2由内皮细胞产生，参与特定的血管病变，包括动脉粥样硬化和主动脉瘤。这两种金属蛋白酶之间最重要的区别之一是MMP-2能够水解弹性蛋白和IV型胶原蛋白，而MMP-1则不能。弹性蛋白衍生肽是弹性纤维降解的产物。我们研究的目的是比较来自三个不同部位（冠状动脉、髂动脉和主动脉）血管病变的培养人动脉内皮细胞中MMP-1和MMP-2的产生情况，以细胞培养基中的浓度来衡量。第二个目的是评估κ-弹性蛋白（浓度为0.1、0.4、1.0、2.5或5.0μg/ml）对三种内皮细胞系中所评估的金属蛋白酶产生的影响。与来自冠状动脉和髂动脉的内皮细胞相比，来自主动脉的内皮细胞中MMP-1的产生在统计学上显著更高。在所测试的内皮细胞系中，MMP-2的产生没有统计学上的显著差异。在所有评估浓度下添加κ-弹性蛋白对培养的冠状动脉内皮细胞中MMP-1的浓度没有统计学上的显著影响。此外，在培养的髂动脉内皮细胞中也未观察到统计学上的显著差异。在来自主动脉的培养内皮细胞中，浓度为0.1和0.4μg/ml的κ-弹性蛋白显著增加了MMP-1的量。
