A scrutiny of matrix metalloproteinases in osteoclasts: evidence for heterogeneity and for the presence of MMPs synthesized by other cells
| Autor: | Jean-Marie Delaissé, Tove Kirkegaard, Thomas Levin Andersen, Niels T. Foged, Thomas Lenhard, Maria del Carmen Ovejero |
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| Rok vydání: | 2004 |
| Předmět: |
musculoskeletal diseases
Cell signaling Pathology medicine.medical_specialty Histology Physiology Endocrinology Diabetes and Metabolism Blotting Western Gene Expression Osteoclasts In situ hybridization Matrix metalloproteinase Biology Bone tissue Bone resorption Mice Matrix Metalloproteinase 10 Osteoclast Matrix Metalloproteinase 13 medicine Animals Collagenases Bone Resorption Cells Cultured In Situ Hybridization Metatarsal Bones Tibia Skull Metalloendopeptidases Blotting Northern Matrix Metalloproteinases Rats Resorption Cell biology Protein Transport medicine.anatomical_structure Matrix Metalloproteinase 9 Knockout mouse Matrix Metalloproteinase 2 Rabbits |
| Zdroj: | Andersen, T L, del Carmen Ovejero, M, Kirkegaard, T, Lenhard, T, Foged, N T & Delaissé, J-M 2004, ' A scrutiny of matrix metalloproteinases in osteoclasts: evidence for heterogeneity and for the presence of MMPs synthesized by other cells ', Bone, vol. 35, no. 5, pp. 1107-19 . https://doi.org/10.1016/j.bone.2004.06.019 |
| ISSN: | 8756-3282 |
| DOI: | 10.1016/j.bone.2004.06.019 |
| Popis: | Udgivelsesdato: 2004-Nov Genetic diseases and knockout mice stress the importance of matrix metalloproteinases (MMPs) in skeletal turnover. Our study aims at clarifying which MMPs are expressed by osteoclasts. Previous analyses of this basic question led to conflicting reports in the literature. In the present study, we used a variety of approaches: PCR, Northern blots, Slot blots, in situ hybridization, and immunohistochemistry. We analyzed osteoclasts in culture as well as osteoclasts in native bone at different locations and compared mouse and rabbit osteoclasts. Osteoclasts express MMP-9 and -14 in all conditions, although to a variable extent, and they are able to synthesize MMP-3, -10, and -12, at least under some circumstances. The induction of a given MMP in osteoclasts is influenced by its environment (e.g., osteoclast culture vs. native bone, and various sites within the same bone) and depends on the species (e.g., mouse vs. rabbit). Osteoclasts show high amounts of MMP-2 and -13 protein presumably made to a large extent by other cells, thereby documenting how proteinases of nonosteoclastic origin may contribute to osteoclast activities and giving insight in why the resorptive activity of purified osteoclasts appears insensitive to MMP inhibitors. Our study shows that the confusion about osteoclastic MMPs in the literature reflects the remarkable ability of osteoclasts to adapt to their environment, as required by the structural or functional diversity of bone tissue. Our observations provide basic information needed for understanding the emerging role of MMPs in controlling cell signaling and bone resorption. |
| Databáze: | OpenAIRE |
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