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

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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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A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222
A matrix metalloproteinase expressed on the surface of invasive tumour cells
Sato, H., Takino, T., Okada, Y., Cao, J. P., Shinagawa, A., Yamamoto, E., & Seiki, M. (1994) · Nature · doi:10.1038/370061a0 · Cited by 2,534
Cell Biology: a Laboratory Handbook
Harris, A. (1995) · Journal of Medical Genetics · doi:10.1136/jmg.32.9.759 · Cited by 1,230
Cellular Mechanisms for Human Procollagenase-3 (MMP-13) Activation
Knäuper, V., Will, H., López-Otı́n, C., Smith, B., Atkinson, S. J., Stanton, H., Hembry, R. M., & Murphy, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17124 · Cited by 747
92-kD type IV collagenase mediates invasion of human cytotrophoblasts.
Librach, C. L., Werb, Z., Fitzgerald, M. L., Chiu, K., Corwin, N., Esteves, R. A., Grobelny, D. W., Galardy, R. E., Damsky, C. H., & Fisher, S. J. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.113.2.437 · Cited by 718
Proteolytic Activity of Human Osteoclast Cathepsin K
Bossard, M. J., Tomaszek, T. A., Thompson, S. K., Amegadzie, B. Y., Hanning, C. R., Jones, C. S., Kurdyla, J., McNulty, D. E., Drake, F. H., Gowen, M., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12517 · Cited by 500
Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas.
Okada, A., Bellocq, J. P., Rouyer, N., Chenard, M., Rio, M., Chambon, P., & Basset, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2730 · Cited by 499
Identification of the Second Membrane-type Matrix Metalloproteinase (MT-MMP-2) Gene from a Human Placenta cDNA Library
Takino, T., Sato, H., Shinagawa, A., & Seiki, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.23013 · Cited by 471
Expression of matrix metalloproteinase-2 and -9 during early human wound healing.
Salo, T. A., Mäkelä, M., Kylmäniemi, M., Autio‐Harmainen, H., & Larjava, H. (1994) · PubMed · Cited by 406
Transmembrane-deletion Mutants of the Membrane-type Matrix Metalloproteinase-1 Process Progelatinase A and Express Intrinsic Matrix-degrading Activity
Pei, D., & Weiss, S. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.9135 · Cited by 389

Show all 50 references

Research works printed but not linked: 3

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

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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: Sato, Takuya
Heegaard, Anne-Marie
Delaissé, Jean-Marie
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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Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts

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