金属蛋白酶诱导因子表达增加在人工关节无菌性松动中的作用及意义

目的研究松动人工关节假体界膜中细胞外基质金属蛋白酶诱导因子(EMMPRIN)的表达,探讨其在人工关节无菌性松动发生发展中的作用。方法16例无菌性松动人工髋关节界膜标本采用免疫组织化学染色和反转录一多聚酶联免疫反应(RT-PCR)法,观察界膜中EMMPRIN的蛋白及mRNA表达。8例股骨颈骨折后髋关节滑膜做为对照。结果在界膜内衬层、内衬层下的巨噬细胞、成纤维细胞内及血管周围发现免疫反应强阳性的EMMPRIN表达。界膜组EMMPRIN的表达量明显高于正常滑膜组(Z=-3．252,P=0．001)。14例界膜标本EMMPRINmRNA的表达阳性。结论界膜中过度表达的EMMPRIN通过上调基质金属蛋白酶(MMPs)促进假体周围的骨破坏。选择性地抑制EMMPRIN生物活性,可能是防治人工关节无菌性松动的新途径。

Significance and role of increased expression of extracellular matrix metalloproteinase induced in the aseptic loosening of prostheses

Objective To investigate the expression of extracellular matrix metalloproteinase induced (EMMPRIN) in the interface tissue, and explore the role of EMMPRIN in the aseptic loosening of prostheses. Methods Immunohistochemistry was performed to characterize the EMMPRIN-expressing cells at sites of interface tissue around aseptic loosened hip prostheses in 16 cases. Reverse trancription-polymerase chain reaction ( RT-PCR) was performed to study the existence of EMMPRIN mRNA in interface tissue samples. And it was followed up by computer assisted image analysis in order to detect the A values of their experession. Synovium of hip joint of 8 femoral neck fracture were in control group. Results Strong immunostaining of EMMPRIN was found in the macrophages and fibroblasts of lining-like layers and vascular endothelium of synovial membrane-like interface tissue around loosened prostheses. Expression of EMMPRIN was significantly higher in interface tissue than the control synovium (z= -3. 252, P = 0. 001). RT-PCR of interface tissue samples disclosed the presence of EMMPRIN mRNA of 14 cases. In interface tissue, the A value of EMMPRIN increased significantly compared to control synovium (P < 0. 01). Conclusion Over-expression of EMMPRIN up-regulates the production of matrix metalloproteinase ( MMPs) in the interface tissue. And it can promote the bone destruction around prostheses. Thereby it may be one of methods to prevent and treat aseptic loosening of prostheses by repression the biology activity of EMMPRIN.