Membrane-type-1 matrix metalloproteinase is abundantly expressed in fibroblasts and osteoclasts at the bone-implant interface of aseptically loosened joint …
T Pap, G Pap, KM Hummel, JK Franz… - The Journal of …, 1999 - europepmc.org
T Pap, G Pap, KM Hummel, JK Franz, E Jeisy, I Sainsbury, RE Gay, M Billingham…
The Journal of Rheumatology, 1999•europepmc.orgObjective To investigate the distribution pattern of membrane-type-1 matrix
metalloproteinase (MT1-MMP) within the synovial-like interface membranes of failed
prosthetic joints. Methods Interface tissue around loose arthroplasties containing both
fibrous membrane and attached bone was obtained from 6 patients at revision surgery. In
situ hybridization with digoxigenin labeled RNA probes was applied to investigate MT1-
MMP expression in paraffin sections of the samples. In addition, double labeling using …
metalloproteinase (MT1-MMP) within the synovial-like interface membranes of failed
prosthetic joints. Methods Interface tissue around loose arthroplasties containing both
fibrous membrane and attached bone was obtained from 6 patients at revision surgery. In
situ hybridization with digoxigenin labeled RNA probes was applied to investigate MT1-
MMP expression in paraffin sections of the samples. In addition, double labeling using …
Objective
To investigate the distribution pattern of membrane-type-1 matrix metalloproteinase (MT1-MMP) within the synovial-like interface membranes of failed prosthetic joints.
Methods
Interface tissue around loose arthroplasties containing both fibrous membrane and attached bone was obtained from 6 patients at revision surgery. In situ hybridization with digoxigenin labeled RNA probes was applied to investigate MT1-MMP expression in paraffin sections of the samples. In addition, double labeling using immunohistochemistry was performed to characterize MT1-MMP producing cells.
Results
Apart from being present in fibroblasts, MT1-MMP was also found expressed in osteoclasts at sites of bone resorption. Our results revealed no expression of MT1-MMP at parts of the membrane that originally had been located next to the prosthesis. In contrast, abundant staining for MT1-MMP was observed at sites attached to bone. MT1-MMP mRNA expression was more intense at those sites of bone resorption covered by a thicker interface membrane.
Conclusion
These results indicate a role for MT1-MMP not only in matrix degradation by fibroblasts but also in osteoclast mediated bone resorption. Given the ability of MT1-MMP to activate MMP2 and MMP13, they suggest also that osteoclasts might contribute to matrix degradation by activating these MMP. This could be of potential interest not only for other conditions in which bone resorption by fibroproliferative tissue plays a role, but also to design novel strategies to prevent loosening of prosthetic joints.
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