Collagens, proteoglycans, MMP-2, MMP-9 and TIMPs in human achilles tendon rupture
Collagens, proteoglycans, MMP-2, MMP-9 and TIMPs in human achilles tendon rupture
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DOI：
10.1007/s11999-008-0255-y
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发表时间：
2008-07-01
影响因子：
4.2
通讯作者：
Maffulli, Nicola
中科院分区：
文献类型：
--
作者：
Karousou, Evgenia;Ronga, Mario;Maffulli, Nicola
肌腱的完整性取决于细胞外基质（ECM）的代谢，这是由蛋白水解酶调节。然而，目前还不清楚哪些酶在肌腱断裂中起作用。我们研究了ECM的19人跟腱断裂，比较的标本收获接近断裂的标本从一个明显健康的地区在同一肌腱收获的组成。我们使用实时PCR、酶谱和FACE分析比较了I型胶原、核心蛋白聚糖和多功能蛋白聚糖的基因表达，包括参与其代谢的酶，如基质金属蛋白酶（MMP-2和-9）和金属蛋白酶的组织抑制剂（TIMP-1和-2）。我们发现蛋白多糖核心蛋白核心蛋白聚糖和多功能蛋白聚糖，I型胶原，MMPs和TIMPs在肌腱断裂中的基因表达更高。反映酶活性表达的酶谱分析证实了蛋白质水平的基因表达数据。宏观健康区域的碳水化合物含量高于破裂区域。在破裂区域，我们发现核心蛋白合成增加，但没有正常的糖胺聚糖产生。破裂区域的组织在分子水平上经历了显著的重排，并支持MMPs在病理学中的作用。
Tendon integrity depends on the extracellular matrix (ECM) metabolism which is regulated by proteolytic enzymes. However, it is unclear which enzymes play a role in tendon rupture. We studied the ECM of 19 ruptured human Achilles tendons, comparing the composition of specimens harvested close to the rupture with specimens harvested from an apparently healthy area in the same tendon. We compared gene expression of collagen Type I, decorin, and versican including enzymes involved in their metabolism as matrix metalloproteases (MMP-2 and -9) and tissue inhibitory of metalloproteinase (TIMP-1 and -2) using real-time PCR, zymography and FACE analysis. We found greater gene expression of proteoglycan core protein decorin and versican, collagen Type I, MMPs and TIMPs in the tendon rupture. Zymography analysis, reflecting expression of enzymatic activity, confirmed the gene expression data at protein level. Carbohydrate content was greater in the macroscopically healthy area than in the ruptured area. In the ruptured area, we found increased core protein synthesis but without the normal glycosaminoglycan production. The tissue in the area of rupture undergoes marked rearrangement at molecular levels and supports the role of MMPs in the pathology.