Changes in the composition of the extracellular matrix in patellar tendinopathy
Changes in the composition of the extracellular matrix in patellar tendinopathy
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DOI：
10.1016/j.matbio.2009.04.001
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发表时间：
2009-05-01
期刊：
影响因子：
6.9
通讯作者：
Handley, Christopher J.
中科院分区：
文献类型：
--
作者：
Samiric, Tom;Parkinson, John;Handley, Christopher J.
目的：比较正常人髌腱和表现出慢性过度使用性肌腱病的肌腱中蛋白多糖和胶原的化学水平和 mRNA 表达。方法：使用木瓜蛋白酶消化的样品通过分光光度法测量硫酸化糖胺聚糖和羟脯氨酸含量。使用特异性抗体通过蛋白质印迹分析去糖基化的蛋白聚糖核心蛋白。通过相对定量 RT-PCR 检测从冷冻肌腱样本中分离出的总 mRNA 中的核心蛋白聚糖、双糖链蛋白聚糖、纤维调节蛋白、多功能蛋白聚糖、聚集蛋白聚糖和 I 型、II 型和 III 型胶原蛋白，并标准化为 3-磷酸甘油醛脱氢酶。 结果：与正常肌腱相比，病理肌腱中的硫酸化糖胺聚糖含量显着增加。这是由于大的聚集蛋白聚糖多能蛋白聚糖和聚集蛋白聚糖以及小蛋白聚糖双聚糖和纤维调节蛋白的沉积增加，但核心蛋白聚糖不增加。聚集蛋白聚糖和多功能蛋白聚糖在正常和病理肌腱中均广泛降解，双糖链蛋白聚糖在病理肌腱中更加破碎，而在正常和病理肌腱中主要存在完整的纤维调节蛋白和核心蛋白聚糖。病理肌腱中总胶原蛋白含量变化较大，但总胶原蛋白水平没有变化。病理组织和正常肌腱的所有基因均无显着差异，但 p 值接近 0.05，表明病理组织中 I 型胶原蛋白和纤维调节蛋白有下调趋势，而多功能蛋白聚糖和 III 型基因有上调趋势。结论：在髌腱病中观察到的蛋白多糖和胶原蛋白水平的变化似乎主要是由于这些大分子代谢周转的变化。这些大分子表达的变化可能在此过程中不起主要作用。 (C) 2009 Elsevier B.V. 保留所有权利。
Objective: To compare the chemical levels and mRNA expression of proteoglycan and collagen in normal human patellar tendons and tendons exhibiting chronic overuse tendinopathy.Methods: Sulfated glycosaminoglycan and hydroxyproline content were investigated by spectrophotometric measurement using papain-digested samples. Deglycosylated proteoglycan core proteins were analysed by Western blot using specific antibodies. Total mRNA isolated from samples of frozen tendons was assayed by relative quantitative RT-PCR for decorin, biglycan, fibromodulin, versican, aggrecan, and collagens Type I, II and III and normalised to glyceraldehyde-3-phosphate dehydrogenase.Results: There was a significant increase in sulfated glycosaminoglycan content in pathologic tendons compared to normal. This was attributed to an increased deposition of the large aggregating proteoglycans versican and aggrecan and the small proteoglycans biglycan and fibromodulin, but not decorin. Aggrecan and versican were extensively degraded in both normal and pathologic tendons, biglycan was more fragmented in the pathologic tendons while predominantly intact fibromodulin and decorin were present in normal and pathologic tendons. There was a greater range in total collagen content but no change in the level of total collagen in pathologic tendons. There were no significant differences between the pathologic and normal tendon for all genes, however p values close to 0.05 indicated a trend in downregulation of Type I collagen and fibromodulin, and upregulation in versican and Type III genes in pathologic tissue.Conclusion: The changes in proteoglycan and collagen levels observed in patellar tendinopathy appear to be primarily due to changes in the metabolic turnover of these macromolecules. Changes in the expression of these macromolecules may not play a major role in this process. (C) 2009 Elsevier B.V. All rights reserved.