Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities

Delaissé, Jean‐Marie; Andersen, Thomas L.; Engsig, Michael T.; Henriksen, Kim; Troen, Tine; Blavier, Laurence

doi:10.1002/jemt.10374

Cited by 341Bone Metabolism and DiseasesProtease and Inhibitor MechanismsBone and Dental Protein Studies

Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities

Delaissé, Jean‐Marie, Andersen, Thomas L., Engsig, Michael T., Henriksen, Kim, Troen, Tine, Blavier, Laurence·2003·Microscopy Research and Technique

DOI 10.1002/jemt.10374

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Abstract

The best established proteolytic event of osteoclasts is bone matrix solubilization by the cysteine proteinase cathepsin K. Here, however, we draw the attention on osteoclastic activities depending on matrix metalloproteinases (MMPs). We discuss the observations supporting that MMPs contribute significantly to bone matrix solubilization in specific areas of the skeleton and in some developmental and pathological situations. Our discussion takes into account (1) the characteristics of the bone remodeling persisting in the absence of cathepsin K, (2) the ultrastructure of the resorption zone in response to inactivation of MMPs and of cathepsin K in different bone types, (3) bone resorption levels in MMP knockout mice compared to wild‐type mice, (4) the identification of MMPs in osteoclasts and surrounding cells, and (5) the effect of different bone pathologies on the serum concentrations of specific collagen fragments believed to discriminate between cathepsin K and MMP cleavage. Next, we provide evidence that MMPs are very critical for osteoclast migration, thereby controlling also the cell‐matrix interactions required for cell attachment/detachment. The evidence supporting this role is based on a model of osteoclast recruitment in primitive long bones, an assay of osteoclast invasion through collagen gel, and the effect of proteinase inhibitors/knockouts in these models. Furthermore, we mention observations indicating a role of MMPs in initiation of bone resorption. Finally, we emphasize the many distinct ways MMPs may alter focally the extracellular environment thereby regulating the osteoclast behavior. Although the understanding of MMPs in osteoclast biology is rapidly expanding, it is suspected that important roles remain to be discovered. Microsc. Res. Tech. 61:504–513, 2003. © 2003 Wiley‐Liss, Inc.

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While osteoclasts express both cathepsin K and MMPs, which contribute differently to bone resorption, BLCs do not express cathepsin K but can efficiently remove nonmineralized fibrillary collagen mediated through their highly active MMPs.
“While osteoclasts express both of these enzymes types, which contribute differently to bone resorption,120 BLCs do not express cathepsin K but can efficiently remove nonmineralized fibrillary collagen (present either on the quiescent bone surface or in resorption lacunae after osteoclastic activity)113 mediated through their highly active MMPs.121”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [120]
Osteoclasts initiate osteoprogenitor cell expansion by activating osteoprogenitor reservoirs located in proximity to the eroded bone surface consisting of BLCs, canopy cells and pericytes.
“A study by Matic et al.137 led to the development of a model in which osteoclasts initiate osteoprogenitor cell expansion (see following section) by activating osteoprogenitor reservoirs located in proximity to the eroded bone surface consisting of BLCs, canopy cells and pericytes.120”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [120]

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Authors: Delaissé, J., Andersen, T. L., Engsig, M. T., Henriksen, K., Troen, T., & Blavier, L.
Affiliations: Center for Clinical & Basic Research (DK)
Corresponding author: Andersen, Thomas L.
ORCID: Delaissé, Jean‐Marie
Andersen, Thomas L.
Henriksen, Kim
Venue: Microscopy Research and Technique
Publisher: Wiley
Published: 2003-07-18
Volume: 61
Issue: 6
Pages: 504-513
ISSN: 1059-910X (ISSN-L)
1097-0029
DOI: 10.1002/jemt.10374
OpenAlex: W2005603603
Cited by: 341
References: 109
Citations by year: 2026: 6 · 2025: 7 · 2024: 11 · 2023: 10 · 2022: 15 · 2021: 18 · 2020: 14 · 2019: 12 · 2018: 10 · 2017: 10 · 2016: 11 · 2015: 25 · 2014: 22 · 2013: 16 · 2012: 25
FWCI: 1.35
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Microscopy Research and Technique (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, cathepsin K, osteoclasts, bone resorption, bone remodeling, osteoclast migration, cell-matrix interactions, bone pathology
MeSH terms: Animals, Cathepsins, Cell Movement, Humans, Osteoclasts, Signal Transduction, Bone Remodeling, Matrix Metalloproteinases, Cathepsin K

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Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities

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