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Membrane-type-1 matrix metalloproteinase is abundantly expressed in fibroblasts and osteoclasts at the bone-implant interface of aseptically loosened joint arthroplasties in situ.
J Rheumatol. 1999 Jan; 26(1):166-9.JR

Abstract

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.

Authors+Show Affiliations

WHO Collaborating Center for Molecular Biology and Novel Therapeutic Strategies for Rheumatic Diseases, Department of Rheumatology, University Hospital, Zurich, Switzerland. ruzpat@ruz.unizh.chNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9918259

Citation

Pap, T, et al. "Membrane-type-1 Matrix Metalloproteinase Is Abundantly Expressed in Fibroblasts and Osteoclasts at the Bone-implant Interface of Aseptically Loosened Joint Arthroplasties in Situ." The Journal of Rheumatology, vol. 26, no. 1, 1999, pp. 166-9.
Pap T, Pap G, Hummel KM, et al. Membrane-type-1 matrix metalloproteinase is abundantly expressed in fibroblasts and osteoclasts at the bone-implant interface of aseptically loosened joint arthroplasties in situ. J Rheumatol. 1999;26(1):166-9.
Pap, T., Pap, G., Hummel, K. M., Franz, J. K., Jeisy, E., Sainsbury, I., Gay, R. E., Billingham, M., Neumann, W., & Gay, S. (1999). Membrane-type-1 matrix metalloproteinase is abundantly expressed in fibroblasts and osteoclasts at the bone-implant interface of aseptically loosened joint arthroplasties in situ. The Journal of Rheumatology, 26(1), 166-9.
Pap T, et al. Membrane-type-1 Matrix Metalloproteinase Is Abundantly Expressed in Fibroblasts and Osteoclasts at the Bone-implant Interface of Aseptically Loosened Joint Arthroplasties in Situ. J Rheumatol. 1999;26(1):166-9. PubMed PMID: 9918259.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Membrane-type-1 matrix metalloproteinase is abundantly expressed in fibroblasts and osteoclasts at the bone-implant interface of aseptically loosened joint arthroplasties in situ. AU - Pap,T, AU - Pap,G, AU - Hummel,K M, AU - Franz,J K, AU - Jeisy,E, AU - Sainsbury,I, AU - Gay,R E, AU - Billingham,M, AU - Neumann,W, AU - Gay,S, PY - 1999/1/26/pubmed PY - 1999/1/26/medline PY - 1999/1/26/entrez SP - 166 EP - 9 JF - The Journal of rheumatology JO - J Rheumatol VL - 26 IS - 1 N2 - 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. SN - 0315-162X UR - https://www.unboundmedicine.com/medline/citation/9918259/Membrane_type_1_matrix_metalloproteinase_is_abundantly_expressed_in_fibroblasts_and_osteoclasts_at_the_bone_implant_interface_of_aseptically_loosened_joint_arthroplasties_in_situ_ DB - PRIME DP - Unbound Medicine ER -