Increased matrix metalloproteinases as possible cause of osseoarticular tissue destruction in long-term haemodialysis and β2-microglobulin amyloidosis

K. Ohashi1,2,3, R. Kawai2, M. Hara2,3, Y. Okada4, S. Tachibana5, Y. Ogura6
1Department of Pathology, Faculty of Medicine, Tokyo Medical and Dental University, Tokyo, Japan
2Department of Pathology, Toranomon Hospital, Tokyo, Japan
3Okinaka Memorial Institute of Medical Research, Tokyo, Japan
4Department of Molecular Immunology and Pathology, Cancer Research Institute, Kanazawa University, Ishikawa, Japan
5Department of Orthopaedic Surgery, Toranomon Hospital, Tokyo, Japan
6Kidney Center, Toranomon Hospital, Tokyo, Japan

Tóm tắt

Immunolocalization of matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs) in periarticular tissues of β2-microglobulin amyloidosis patients was investigated. MMP-1 (interstitial collagenase) the most strongly expressed of the MMPs, was localized in the synovial lining cells, mesenchymal cells in granulation tissue and nodular amyloid deposits, and chondrocytes within areas of cartilage erosion. Expression of MMP-1 was correlated with the degree of macrophage infiltration and synovial cell hyperplasia, but it was not correlated with the degree of amyloid deposition or haemodialysis period. Expression of MMP-1 appeared more intense than that of TIMP-1 and TIMP-2 in highly inflammatory cases. MMP-2 was mildly expressed in the interstitial fibroblasts and MMP-3 was faintly stained in the extracellular matrix of the synovial membrane. MMP-9 (gelatinase B) was found to be strongly positive in the osteoclasts which increased in the progressing osteolytic lesion from the destructive arthropathy. These results suggest involvement of MMPs in inflammation with an imbalance between expression of MMPs and TIMPs being closely related to pathogenesis of the destructive arthropathy.

Tài liệu tham khảo

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