mRNA expression of matrix metalloproteinases and tissue inhibitors of metalloproteinase in interface tissue around implants in loosening total hip arthroplasty

Ishiguro, Naoki; Itō, Takayasu; Kurokouchi, Kazutoshi; Iwahori, Yusuke; Nagaya, Ikuo; Hasegawa, Yikiharu; Iwata, Hiroji

doi:10.1002/(sici)1097-4636(199612)32:4<611::aid-jbm14>3.3.co;2-4

Cited by 10 publications

(13 citation statements)

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“…2 Wear particles 3,4 trigger the invasion of inflammatory cells into the interface tissue. Some cell populations of the interface tissue release matrix-degrading enzymes 5 and cytokines. 6 In the past, the roles of members of the enzyme family of matrix metalloproteinases (MMPs) in tissue degradation were investigated.…”

Section: Introductionsupporting

confidence: 60%

Interface membrane fibroblasts around aseptically loosened endoprostheses express MMP‐13

Wagner

Gollwitzer

Wernicke

et al. 2007

Journal Orthopaedic Research

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The objective of this article was to assess whether matrix metalloproteinase-13 (MMP-13) is produced by cells of the peri-implant interface tissues and to further characterize these cells. Tissue specimens were collected from the bone-prosthesis interface at the time of revision surgery of clinically loosened hip and knee arthroplasties (n ¼ 27). Synovial tissues from osteoarthritic patients and young patients with mild joint deformity were used as controls (n ¼ 6). Tissue samples were fixed in 4% PFA, decalcified with EDTA, and embedded in paraffin. Sections (4 mm) were stained with hematoxylin/eosin and for the osteoclastic marker enzyme tartrate resistant acid phosphatase. Monocytes/macrophages were characterized with a monoclonal antibody against CD68 and mRNAs encoding MMP-13 and a 1 collagen I (COL1A1) were detected by in situ hybridization. Cells expressing transcripts encoding MMP-13 were found in 70% of the interface tissues. These cells colocalized with a cell population expressing COL1A1 mRNA, and were fibroblastic in appearance. MMP-13 expressing cells were found in the close vicinity of osteoclasts and multinuclear giant cells. No signals for transcripts encoding MMP-13 were detected in multinuclear giant cells or in osteoclasts. Control tissues were negative for transcripts encoding MMP-13 mRNA. Fibroblasts of the interface from aseptically loosened endoprostheses selectively express MMP-13. By the expression and the release of MMP-13, these fibroblastic cells may contribute to the local degradation of the extracellular matrix and to bone resorption. ß

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Section: Introductionsupporting

confidence: 60%

Interface membrane fibroblasts around aseptically loosened endoprostheses express MMP‐13

Wagner

Gollwitzer

Wernicke

et al. 2007

Journal Orthopaedic Research

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“…Primer sequences were from published data for MMP and TIMP amplification and are listed in Table 1. 49,50 LNCaP and PC3 cDNAs were used to optimize the conditions for RT-PCR for each primer set by comparing different concentrations of magnesium chloride and different cycle numbers. The concentration that gave the strongest signal on a 2% agarose gel stained with ethidium bromide was chosen as the optimal concentration for that primer set.…”

Section: Polymerase Chain Reactionmentioning

confidence: 99%

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Daja

Niu

Zhao

et al. 2003

Prostate Cancer Prostatic Dis

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Stromal expression of some matrix metalloproteinases (MMPs) has been associated with increasing tumour burden in prostate cancer. We investigated the expression of mRNA (by RT-PCR) and protein (by zymography and western blotting) of MMPs and endogenous inhibitors (tissue inhibitors of metalloproteinases, TIMPs) in two parent epithelial prostate cancer cell lines and sublines of increasing invasive/metastatic potential. Expression of membrane type MMPs, MT1-MMP and MT3-MMP mRNA was higher in PC3-derived than in LNCaPderived lines, whereas MT2-MMP mRNA expression was higher in the LNCaPderived than in PC3-derived cell lines. Active MT1, MT2 and MT3-MMP protein levels were similar in all lines, but processed MT-MMPs, indicative of latent MMP activation, were increased in more aggressive sublines. Expression of MMP-1, MMP-13 and TIMP-1 was higher in the more aggressive sublines and may be implicated in invasive/metastatic ability. Regulation of MMP-1 and MMP-13 expression may offer important therapeutic options for treating patients with prostate cancer.

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“…The authors reported high levels of TIMP-1, -2, and -3 mRNA and have demonstrated the production of pro-MMP-2/TIMP-2, pro-MMP-9/TIMP-1, or MT1-MMP/MMP-2/TIMP-2 complexes. 23,37,38 Taken together, these results confirm that the understanding of bone-cell responses to biomaterials in terms of matrix deposition and metalloproteinase synthesis and secretion could provide optimum knowl-edge of the regulation of matrix synthesis and bone formation at the host-implant site. This will offer new strategies to elaborate improved devices for optimal osseointegration and long-term success of prostheses.…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinases MMP‐2, ‐9 and tissue inhibitors TIMP‐1, ‐2 expression and secretion by primary human osteoblast cells in response to titanium, zirconia, and alumina ceramics

Oum'Hamed

Garnotel

Josset

et al. 2003

J Biomedical Materials Res

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Osteogenic properties of bone cells are a key parameter governing osseointegration of implant devices. In this context, osteoblasts have a central role via extracellular matrix synthesis and remodeling that they regulate through different protease activity. In this study, we have analyzed the expression of two matrix metalloproteinases (MMPs): MMP-2 (72 kDa) and MMP-9 (92 kDa) and their specific tissue inhibitors TIMP-1 and TIMP-2 in primary human osteoblastic cells. The effect of titanium, zirconia, and alumina ceramics on the synthesis of these proteases was assessed using reverse transcriptase-polymerase chain reaction, enzyme-linked immunosorbent assay, and zymographic analysis. Our results showed that osteoblasts express MMP-2 and -9 mRNA. Furthermore, MMP-2 mRNA expression was decreased by titanium and increased by alumina whereas zirconia did not have any significant effect. Conversely, MMP-9 mRNA expression was stimulated by titanium but decreased with zirconia, whereas alumina induced no significant changes. Zymographic analysis has evidenced pro-MMP-2 gelatinolytic activity in all cell populations with time-dependent increase profile; pro-MMP-9, however, was not detected. Enzyme-linked immunosorbent assay data confirmed the production of MMP-2 and very low levels of MMP-9. In addition, TIMP-1 was secreted in 24-hcultured cells and increased to maximal level at 48 -72 h whereas TIMP-2 levels were very low. The interactions between human osteoblasts and the studied biomaterials altered both MMP-2, -9 and TIMP-1expression indicating that biomaterials may influence osseointegration and bone remodeling.

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mRNA expression of matrix metalloproteinases and tissue inhibitors of metalloproteinase in interface tissue around implants in loosening total hip arthroplasty

Cited by 10 publications

References 0 publications

Interface membrane fibroblasts around aseptically loosened endoprostheses express MMP‐13

Interface membrane fibroblasts around aseptically loosened endoprostheses express MMP‐13

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Matrix metalloproteinases MMP‐2, ‐9 and tissue inhibitors TIMP‐1, ‐2 expression and secretion by primary human osteoblast cells in response to titanium, zirconia, and alumina ceramics

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