de Mos Marieke, van El Benno, DeGroot Jeroen, Jahr Holger, van Schie Hans T M, van Arkel Ewoud R, Tol Hans, Heijboer Rien, van Osch Gerjo J V M, Verhaar Jan A N
Department of Orthopaedics, Erasmus MC University Medical Center, Rotterdam, The Netherlands.
Am J Sports Med. 2007 Sep;35(9):1549-56. doi: 10.1177/0363546507301885. Epub 2007 May 3.
Understanding biochemical and structural changes of the extracellular matrix in Achilles tendinosis might be important for developing mechanism-based therapies.
In Achilles tendinosis, changes occur in biochemical composition and collagen turnover rate.
Descriptive laboratory study.
From 10 patients undergoing surgery for Achilles tendinopathy, 1 tendinosis biopsy specimen and 1 biopsy specimen of macroscopically healthy tendon tissue adjacent to the lesion were collected. Furthermore, biopsy samples were collected from 3 donors with asymptomatic Achilles tendons. Water content, collagen content, percentage of denatured collagen, amount of lysine hydroxylation, number of enzymatic and nonenzymatic crosslinks, matrix metalloproteinase activity, and matrix metalloproteinase and collagen gene-expression levels were analyzed.
In tendinotic lesions, the water content was highest, and collagen content was subnormal with higher amounts of denatured/damaged collagen. Low pentosidine levels in tendinotic tissue indicated the presence of relatively young collagenous matrix. More hydroxylated lysine residues were present in tendinotic samples, but enzymatic crosslinks revealed no differences between tendinotic, adjacent, and healthy samples. In tendinotic specimens, matrix metalloproteinase activity was higher, matrix metalloproteinase gene-expression profile was altered, and collagen type I and III gene expression were upregulated.
In Achilles tendinosis, the collagen turnover rate is increased, and the natural biochemical composition of the collagenous matrix is compromised.
Although tendon tissue directly adjacent to an Achilles tendinosis lesion looks macroscopically healthy, histological and biochemical degenerative changes in adjacent tissue are evident, which may have implications for surgical interventions.
了解跟腱病中细胞外基质的生化和结构变化对于开发基于机制的治疗方法可能很重要。
在跟腱病中，生化组成和胶原转换率会发生变化。
描述性实验室研究。
从10例接受跟腱病手术的患者中，采集1份跟腱病活检标本和1份病变相邻的宏观健康肌腱组织活检标本。此外，从3名无症状跟腱的捐赠者中采集活检样本。分析了水分含量、胶原含量、变性胶原百分比、赖氨酸羟化量、酶促和非酶促交联数量、基质金属蛋白酶活性以及基质金属蛋白酶和胶原基因表达水平。
在跟腱病病变中，水分含量最高，胶原含量低于正常水平，变性/损伤胶原含量更高。跟腱病组织中低水平的戊糖苷表明存在相对年轻的胶原基质。跟腱病样本中存在更多的羟化赖氨酸残基，但酶促交联在跟腱病、相邻和健康样本之间没有差异。在跟腱病标本中，基质金属蛋白酶活性更高，基质金属蛋白酶基因表达谱改变，I型和III型胶原基因表达上调。
在跟腱病中，胶原转换率增加，胶原基质的天然生化组成受到损害。
尽管跟腱病病变直接相邻的肌腱组织在宏观上看起来健康，但相邻组织的组织学和生化退行性变化很明显，这可能对手术干预有影响。
