Department of Orthopaedics, Lund University, Skåne University Hospital, Malmö SE-205 02, Sweden.
BMC Musculoskelet Disord. 2013 Jan 9;14:18. doi: 10.1186/1471-2474-14-18.
BACKGROUND: It remains to be shown whether OA shares molecular similarities between different joints in humans. This study provides evidence for similarities in cartilage molecular damage in osteoarthritic (OA) joints. METHODS: Articular cartilage from osteoarthritic hip joints were analysed and compared to non-OA controls regarding collagen, glycosaminoglycan and water content. Femoral heads from 16 osteoarthritic (OA) and 20 reference patients were obtained from hip replacement surgery due to OA and femoral neck fracture, respectively. Cartilage histological changes were assessed by Mankin grading and denatured collagen type II immunostaining and cartilage was extracted by α-chymotrypsin. Hydroxyproline and Alcian blue binding assays were used to measure collagen and glycosaminoglycan (GAG) content, respectively. RESULTS: Mankin and immunohistology scores were significantly higher in hip OA samples than in reference samples. Cartilage water content was 6% higher in OA samples than in references. 2.5 times more collagen was extracted from OA than from reference samples. There was a positive association between water content and percentage of extractable collagen pool (ECP) in both groups. The amounts of collagen per wet and dry weights did not differ statistically between OA and reference cartilage. % Extractable collagen was not related to collagen per dry weight in either group. However when collagen was expressed by wet weight there was a negative correlation between % extractable and collagen in OA cartilage. The amount of GAG per wet weight was similar in both groups but the amount of GAG per dry weight was higher in OA samples compared to reference samples, which suggests a capacity for GAG biosynthesis in hip OA cartilage. Neither of the studied parameters was related to age in either group. CONCLUSIONS: Increased collagen extractability and water content in human hip cartilage is associated with OA pathology and can be observed at early stages of the degenerative hip OA process. Our results suggest a common degradative pathway of collagen in articular cartilage of different joints. Furthermore, the study suggests that biochemical changes precede more overt OA changes and that chondrocytes may have a capability to compensate molecular loss in the early phase of OA.
背景：OA 是否在人类不同关节之间具有分子相似性仍有待证实。本研究为 OA 关节软骨分子损伤的相似性提供了证据。
方法：分析了来自 OA 髋关节的关节软骨，并将其与非 OA 对照组进行了比较，比较了胶原、糖胺聚糖和水含量。由于 OA 和股骨颈骨折，从髋关节置换手术中获得了 16 个 OA（OA）和 20 个对照患者的股骨头。通过 Mankin 分级和变性 II 型胶原免疫染色评估软骨组织学变化，并通过α-糜蛋白酶提取软骨。羟脯氨酸和阿利新蓝结合测定法分别用于测量胶原和糖胺聚糖（GAG）含量。
结果：髋关节 OA 样本的 Mankin 和免疫组织化学评分明显高于参考样本。OA 样本的软骨含水量比参考样本高 6%。从 OA 样本中提取的胶原比参考样本多 2.5 倍。两组中，水含量与可提取胶原池（ECP）的百分比之间存在正相关。OA 和参考软骨的胶原湿重和干重之间的数量没有统计学差异。%可提取胶原与两组中的胶原干重无关。然而，当以湿重表示胶原时，OA 软骨中可提取胶原与胶原之间呈负相关。两组的 GAG 湿重含量相似，但 OA 样本的 GAG 干重含量高于参考样本，这表明髋关节 OA 软骨中 GAG 生物合成的能力。两组中，没有研究参数与年龄相关。
结论：人类髋关节软骨中胶原提取能力和含水量的增加与 OA 病理相关，并且可以在退行性髋关节 OA 过程的早期阶段观察到。我们的研究结果表明不同关节的关节软骨中存在共同的胶原降解途径。此外，该研究表明，生化变化先于更明显的 OA 变化，并且软骨细胞在 OA 的早期阶段可能具有补偿分子丢失的能力。
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