PMID: 8594658Oct 1, 1995Paper

Matrix metalloproteinase (MMP-9) in patients with rheumatoid arthritis

Ryūmachi. [Rheumatism]
M SekiT Sawai

Abstract

MMP-9 degrades type IV collagen, gelatin, type V collagen, and type XI collagen. We measured proMMP-9 and proMMP-9/TIMP-1 complex in sera and joint fluids by sandwich ELISA, and examined immunohistochemically the expression of these proteins in joint tissue from patients with rheumatoid arthritis (RA). ProMMP-9 was purified by the three chromatographic steps from the culture medium of HT1080 cells. Purified proMMP-9 and activated MMP-9 by APMA showed a single band of Mr92000, Mr67000, resectively on gelatin-zymography. We raised two monoclonal antibody colones 2G9, 8G7 against proMMP-9 with BALB/c mice. 2G9 and 8G7 reacted with proMMP-9 on Western blotting, and these clones reacted proMMP-9 and proMMP-9/TIMP-1 complex on sandwich ELISA, specifically. ProMMP-9 concentration in 86 sera (749.4+/-940.2 ng/ml) and 54 joint fluids (4539.9+/-7681.5 ng/ml) from patients with RA was significantly higher than those of patients with osteoarthritis and control. Immunohistochemistry with 2G9 showed that in rheumatoid synovium proMMP-9 localized in neutrophils and monocytes diffusely infiltrated the sublining layer. In addition, osteoclasts in rheumatoid subchondral bone were intensively stained. ProMMP-9 concentration in joint fluids from 3...Continue Reading

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