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Cited by 145Bone Metabolism and DiseasesProtease and Inhibitor MechanismsBone and Dental Protein Studies

A scrutiny of matrix metalloproteinases in osteoclasts: evidence for heterogeneity and for the presence of MMPs synthesized by other cells

Andersen, Thomas L., del Carmen Ovejero, Maria, Kirkegaard, Tove, Lenhard, Thomas, Foged, Niels T., Delaissé, Jean-Marie·2004·Bone
DOI 10.1016/j.bone.2004.06.019
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Abstract

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.

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Authors
Andersen, T. L., del Carmen Ovejero, M., Kirkegaard, T., Lenhard, T., Foged, N. T., & Delaissé, J.-M.
Affiliations
  • Vejle Sygehus (DK)
  • Center for Clinical & Basic Research (DK)
Corresponding author
Andersen, Thomas L.
ORCID
Venue
Bone
Publisher
Elsevier BV
Published
2004-11
Volume
35
Issue
5
Pages
1107-1119
ISSN
  • 1873-2763 (ISSN-L)
  • 8756-3282
DOI
10.1016/j.bone.2004.06.019
OpenAlex
W2010224562
Cited by
145
References
78
Citations by year
2026: 2 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 7 · 2019: 7 · 2018: 7 · 2017: 6 · 2016: 8 · 2015: 4 · 2014: 8 · 2013: 9 · 2012: 9
FWCI
2.01
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Bone (publishedVersion)
  • PubMed (publishedVersion)
  • University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
Keywords
matrix metalloproteinases, osteoclasts, MMP-9, MMP-14, MMP-3, MMP-10, MMP-12, MMP-2, MMP-13, bone resorption, species differences, matrix metalloproteinase inhibitors
MeSH terms
Animals, Bone Resorption, Cells, Cultured, Metalloendopeptidases, Metatarsal Bones, Osteoclasts, Rabbits, Skull, Tibia, Blotting, Northern, Blotting, Western, Gene Expression, Collagenases, In Situ Hybridization, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9, Matrix Metalloproteinases, Protein Transport, Mice, Rats, Matrix Metalloproteinase 10, Matrix Metalloproteinase 13

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