Matrix metalloproteinases and tissue inhibitors of metalloproteinases in joint fluid of the patients with loose artificial hip joints.
Matrix metalloproteinases and tissue inhibitors of metalloproteinases in joint fluid of the patients with loose artificial hip joints.
复制标题
人工髋关节松动患者关节液中基质金属蛋白酶和金属蛋白酶组织抑制剂的研究
DOI:
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复制
发表时间:
1999
期刊:
影响因子:
--
通讯作者:
Y. Konttinen
中科院分区:
文献类型:
--
作者:
I. Takei;M. Takagi;S. Santavirta;H. Ida;M. Hamasaki;M. Ishii;S. Fukushima;T. Ogino;Y. Konttinen
The pseudojoint cavity formed in patients undergoing total hip arthroplasty (THA) is later remodeled to synovial membrane-like tissue, which produces pseudosynovial fluid. This pseudosynovium also is an important source of matrix metalloproteinases (MMPs). As it is widely speculated that synovial fluid MMPs may contribute to local tissue degradation in rheumatoid arthritis (RA) and osteoarthritis (OA), we hypothesize that locally produced MMPs are found in the pseudosynovial fluid, via which they have access to the implant-host interface, and that if they retain their proteolytic potential, they might contribute to aseptic loosening. Enzyme-linked immunosorbent assay (ELISA), immunoblotting, and zymography were used to analyze MMPs and tissue inhibitors of metalloproteinases (TIMPs) in synovial fluid in aseptic loosening, which was compared to RA and OA. Pseudosynovial THA fluid was characterized using low levels of MMP-1 but moderate levels of MMP-13 and MT1-MMP (MMP-14). Due to the lack of an appropriate assay, MMP-13 and MT1-MMP were not similarly assessed, but the immunoblotting indicated that they were in the 56 kD intermediate proteolytically processed forms. The MMP-9 level was intermediate between RA and OA. MMP-2 was on a significant level, but there were no differences among study groups. The THA group also was characterized using relatively high levels of TIMP-1 and TIMP-2. Accordingly, MMP-9 and MMP-2 were found to occur in the 92 kD and 72 kD proenzyme form, respectively, with full activity retained in all study groups. The data suggest that proMMP-2-TIMP-2 and proMMP-9-TIMP-1 complexes are formed in the pseudosynovial fluid due to the excess of TIMPs over MMPs in aseptic loosening of THA. TIMP-complexed MMPs are resistant to MMP-mediated proteolytic activation, which may explain their latency and proenzyme zymogen form. Thus, formation of stabilizing proMMP-TIMP complexes enable transportation of proMMPs far from their original site of production. Due to motion-associated cyclic changes of the intra-articular pressure, fluid-phase MMPs stabilized by TIMPs might be absorbed to implant surfaces and interface tissues and help to dissect the implant/cement-to-bone interface in situ. Consequently, they may contribute to local proteolytic/tissue destructive events and aseptic loosening.
DOI:
10.3109/17453679408995454
发表时间:
1994
期刊:
Acta orthopaedica Scandinavica
影响因子:
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作者:
Takagi,M;Konttinen,YT;Santavirta,S;Sorsa,T;Eisen,AZ;Nordsletten,L;Suda,A
通讯作者:
Suda,A
DOI:
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发表时间:
1993-07
期刊:
The Journal of biological chemistry
影响因子:
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作者:
A. Strongin;B. Marmer;G. A. Grant;G. Goldberg
通讯作者:
A. Strongin;B. Marmer;G. A. Grant;G. Goldberg
DOI:
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发表时间:
1986-05
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen
通讯作者:
G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen