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Cited by 214Protease and Inhibitor MechanismsBone Metabolism and DiseasesBone and Dental Protein Studies

The DOI matches its Crossref record; 49 of the 50 references it cites were found in a registry or an index.

Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts

Sato, Takuya, Ovejero, Maria del Carmen, Hou, Peng, Heegaard, Anne-Marie, Kumegawa, Masayoshi, Tækker Foged, Niels, Delaissé, Jean-Marie·1997·Journal of Cell Science
DOI 10.1242/jcs.110.5.589
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Abstract

The osteoclasts are the cells responsible for bone resorption. Matrix metalloproteinases (MMPs) appear crucial for this process. To identify possible MMP expression in osteoclasts, we amplified osteoclast cDNA fragments having homology with MMP genes, and used them as a probe to screen a rabbit osteoclast cDNA library. We obtained a cDNA of 1,972 bp encoding a polypeptide of 582 amino acids that showed more than 92% identity to human, mouse, and rat membrane-type 1 MMP (MT1-MMP), a cell surface proteinase believed to trigger cancer cell invasion. By northern blotting, MT1-MMP was found to be highly expressed in purified osteoclasts when compared with alveolar macrophages and bone stromal cells, as well as with various tissues. In situ hybridization on bone sections showed that MT1-MMP is expressed also in osteoclasts in vivo. Antibodies recognizing MT1-MMP reacted with specific plasma membrane areas corresponding to lamellipodia and podosomes involved, respectively, in migratory and attachment activities of the osteoclasts. These observations highlight how cells might bring MT1-MMP into contact with focal points of the extracellular matrix, and are compatible with a role of MT1-MMP in migratory and attachment activities of the osteoclast.

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Crossref · 10.1242/jcs.110.5.589

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Research works printed but not linked: 3

  1. Delaissé, 1992, Mechanism of mineral solubilization and matrix degradation in osteoclastic bone resorption, 289
  2. Helfrich, 1994, Isolation of osteoclasts and osteoclast membranes, 128
  3. Sato, 1994, A simple method for isolation of rabbit osteoclasts, Dentistry in Japan, 31, 3

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Metadata

Authors
Sato, T., Ovejero, M. D. C., Hou, P., Heegaard, A.-M., Kumegawa, M., Tækker Foged, N., & Delaissé, J.-M.
Affiliations
  • Center for Clinical & Basic Research (DK)
  • 1 Department of Basic Research, Center for Clinical & Basic Research, Ballerup Byvej 222, DK-2750 Ballerup, Denmark
  • Meikai University (JP)
ORCID
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
1997-03-01
Volume
110
Issue
5
Pages
589-596
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
DOI
10.1242/jcs.110.5.589
OpenAlex
W2118837944
Cited by
214
References
50
Citations by year
2025: 3 · 2024: 1 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 5 · 2014: 8 · 2013: 10 · 2012: 4
FWCI
4.37
Type
journal article
Language
en
Open access
closed
Licence
www.biologists.com/user-licence-1-1/ (vor)
Locations
  • Journal of Cell Science (publishedVersion)
  • PubMed (publishedVersion)
  • HighWire Press Open Archive (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
Keywords
MT1-MMP, membrane-type matrix metalloproteinases, osteoclasts, bone resorption, cDNA cloning, gene expression, lamellipodia, podosomes, cell migration, cell attachment, extracellular matrix
MeSH terms
Amino Acid Sequence, Animals, Base Sequence, Humans, Immunohistochemistry, Metalloendopeptidases, Molecular Sequence Data, Osteoclasts, Rabbits, Blotting, Northern, Sequence Homology, Amino Acid, In Situ Hybridization, DNA, Complementary, Matrix Metalloproteinases, Membrane-Associated, Matrix Metalloproteinase 14

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