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滑液和血清中软骨寡聚基质蛋白的小片段作为软骨降解的标志物。

Small fragments of cartilage oligomeric matrix protein in synovial fluid and serum as markers for cartilage degradation.

作者信息

Neidhart M, Hauser N, Paulsson M, DiCesare P E, Michel B A, Häuselmann H J

机构信息

Department of Rheumatology, University Hospital Zürich, Switzerland.

出版信息

Br J Rheumatol. 1997 Nov;36(11):1151-60. doi: 10.1093/rheumatology/36.11.1151.

DOI:10.1093/rheumatology/36.11.1151
PMID:9402858
Abstract

We determined the tissue distribution of cartilage oligomeric matrix protein (COMP) in man and evaluated COMP in synovial fluid (SF) and serum. COMP was purified from human articular cartilage. Polyclonal antibodies were used to detect COMP in tissue cryosections and protein extracts. COMP was determined quantitatively and qualitatively in SF and serum by competitive enzyme-linked immunosorbent assay and immunoblotting. Knee joint SF was taken from nine cadaveric and six living controls, 52 patients with osteoarthritis (OA), 85 patients with rheumatoid arthritis (RA) and 60 patients with other forms of inflammatory arthritis. The degradative potential of SF on native COMP was tested in vitro. The highest concentrations of COMP were measured in articular cartilage and meniscus, the lowest in rib and trachea. Compared with controls, the concentrations of COMP in SF and serum were elevated in 36 and 50% of the patients. A total of 84% of patients with RA and 60% of patients with other forms of inflammatory arthritis showed significant amounts of low-molecular-weight COMP fragments (50-70 kDa) in SF. In contrast, SF fragments were present in only 21% of the OA patients. Furthermore, 13% of SF taken from patients with RA or other forms of inflammatory arthritis were able to degrade COMP in vitro. Using inhibitors, the involvement of serine proteinases could be demonstrated in only 8% of the cases. Based on these results, the absolute levels of COMP in SF and serum, and its fragmentation pattern in SF, seem to be promising as markers of joint tissue metabolism.

摘要

我们测定了人软骨寡聚基质蛋白(COMP)的组织分布,并评估了滑液(SF)和血清中的COMP。COMP从人关节软骨中纯化得到。使用多克隆抗体在组织冰冻切片和蛋白提取物中检测COMP。通过竞争性酶联免疫吸附测定和免疫印迹法定量和定性测定SF和血清中的COMP。膝关节SF取自9例尸体对照和6例活体对照、52例骨关节炎(OA)患者、85例类风湿关节炎(RA)患者和60例其他形式炎性关节炎患者。体外测试了SF对天然COMP的降解潜力。COMP在关节软骨和半月板中的浓度最高,在肋骨和气管中的浓度最低。与对照组相比,36%的患者SF中COMP浓度升高,50%的患者血清中COMP浓度升高。总共84%的RA患者和60%的其他形式炎性关节炎患者的SF中显示出大量低分子量COMP片段(50 - 70 kDa)。相比之下,仅21%的OA患者的SF中有片段。此外,取自RA或其他形式炎性关节炎患者的SF中有13%能够在体外降解COMP。使用抑制剂,仅在8%的病例中证实丝氨酸蛋白酶参与其中。基于这些结果,SF和血清中COMP的绝对水平及其在SF中的片段化模式似乎有望成为关节组织代谢的标志物。

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