Milz S, Sicking B, Sprecher C M, Putz R, Benjamin M
AO Research Institute, AO Foundation, Davos, Switzerland.
J Anat. 2007 Jul;211(1):1-7. doi: 10.1111/j.1469-7580.2007.00742.x. Epub 2007 May 28.
The triangular fibrocartilage complex (TFCC) transmits load from the wrist to the ulna and stabilizes the distal radioulnar joint. Damage to it is a major cause of wrist pain. Although its basic structure is well established, little is known of its molecular composition. We have analysed the immunohistochemical labelling pattern of the extracellular matrix of the articular disc and the meniscal homologue of the TFCC in nine elderly individuals (age range 69-96 years), using a panel of monoclonal antibodies directed against collagens, glycosaminoglycans, proteoglycans and cartilage oligomeric matrix protein (COMP). Although many of the molecules (types I, III and VI collagen, chondroitin 4 sulphate, dermatan sulphate and keratan sulphate, the oversulphated epitope of chondroitin 6 sulphate, versican and COMP) were found in all parts of the TFCC, aggrecan, link protein and type II collagen were restricted to the articular disc and to entheses. They were thus not a feature of the meniscal homologue. The shift in tissue phenotype within the TFCC, from a fibrocartilaginous articular disc to a more fibrous meniscal homologue, correlates with biomechanical data suggesting that the radial region is stiff and subject to considerable stress concentration. The presence of aggrecan, link protein and type II collagen in the articular disc could explain why the TFCC is destroyed in rheumatoid arthritis, given that it has been suggested that autoimmunity to these antigens results in the destruction of articular cartilage. The differential distribution of aggrecan within the TFCC is likely to be reflected by regional differences in water content and mobility on the radial and ulnar side. This needs to be taken into account in the design of improved MRI protocols for visualizing this ulnocarpal complex of the wrist.
三角纤维软骨复合体(TFCC)将来自腕部的负荷传递至尺骨,并稳定桡尺远侧关节。其损伤是腕部疼痛的主要原因。尽管其基本结构已明确,但对其分子组成却知之甚少。我们使用一组针对胶原蛋白、糖胺聚糖、蛋白聚糖和软骨寡聚基质蛋白(COMP)的单克隆抗体,分析了9名老年个体(年龄范围69 - 96岁)关节盘和TFCC半月板同源物细胞外基质的免疫组织化学标记模式。尽管在TFCC的所有部位都发现了许多分子(I型、III型和VI型胶原蛋白、硫酸软骨素4、硫酸皮肤素和硫酸角质素、硫酸软骨素6的过度硫酸化表位、多功能蛋白聚糖和COMP),但聚集蛋白聚糖、连接蛋白和II型胶原蛋白仅限于关节盘和韧带附着处。因此,它们不是半月板同源物的特征。TFCC内组织表型从纤维软骨性关节盘向更纤维性的半月板同源物转变,与生物力学数据相关,表明桡侧区域僵硬且承受相当大的应力集中。考虑到有人提出针对这些抗原的自身免疫会导致关节软骨破坏,关节盘中聚集蛋白聚糖、连接蛋白和II型胶原蛋白的存在可以解释为什么TFCC在类风湿性关节炎中会被破坏。TFCC内聚集蛋白聚糖的差异分布可能反映在桡侧和尺侧的含水量和流动性的区域差异上。在设计用于可视化腕部尺腕复合体的改进MRI方案时需要考虑到这一点。