The Membrane-Anchored MMP Inhibitor RECK Is a Key Regulator of Extracellular Matrix Integrity and Angiogenesis
Open accessAbstract
Matrix metalloproteinases (MMPs) are essential for proper extracellular matrix remodeling. We previously found that a membrane-anchored glycoprotein, RECK, negatively regulates MMP-9 and inhibits tumor invasion and metastasis. Here we show that RECK regulates two other MMPs, MMP-2 and MT1-MMP, known to be involved in cancer progression, that mice lacking a functional RECK gene die around E10.5 with defects in collagen fibrils, the basal lamina, and vascular development, and that this phenotype is partially suppressed by MMP-2 null mutation. Also, vascular sprouting is dramatically suppressed in tumors derived from RECK-expressing fibrosarcoma cells grown in nude mice. These results support a role for RECK in the regulation of MMP-2 in vivo and implicate RECK downregulation in tumor angiogenesis.
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RECK is a membrane-anchored MMP inhibitor whose reduced expression or inactivation seems critical for invasiveness and metastasis of various cancers, including glioma.
“RECK is a membrane-anchored MMP inhibitor whose reduced expression or inactivation seems to be critical for the invasiveness and metastasis of various cancers, including glioma cancer (7, 46).”
From MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators (2008) · cites this paper as [46]
These MMP inhibitors regulate MMP activity posttranslationally.
“Concurring with previously published reports (12, 46), our data indicate that these MMP inhibitors regulate MMP activity posttranslationally.”
From MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators (2008) · cites this paper as [46]
RECK is a GPI-anchored protein that binds and inhibits metalloproteases including ADAM10.
“RECK is a GPI-anchored protein that binds and inhibits metalloproteases that include ADAM10 (18–21).”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [20]
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New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108 · see citing works
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575 · see citing works
Matrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929 · see citing works
Strategies for MMP inhibition in cancer: innovations for the post-trial era
Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349 · see citing works
MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators
Gabriely, G., Wurdinger, T., Kesari, S., Esau, C. C., Burchard, J., Linsley, P. S., & Krichevsky, A. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00479-08 · Cited by 888 · see citing works
Matrix metalloproteases in aberrant fibrotic tissue remodeling
Pardo, A., & Selman, M. (2006) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200601-012tk · Cited by 260 · see citing works
RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity
Muraguchi, T., Takegami, Y., Ohtsuka, T., Kitajima, S., Chandana, E. P. S., Omura, A., Miki, T., Takahashi, R., Matsumoto, N., Ludwig, A., et al. (2007) · Nature Neuroscience · doi:10.1038/nn1922 · Cited by 149 · see citing works
Self-citationA Genomic Comparison of <i>in vivo</i> and <i>in vitro</i> Brain Microvascular Endothelial Cells
Calabria, A. R., & Shusta, E. V. (2008) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600518 · Cited by 109 · see citing works
MMP14 in sarcoma: a regulator of tumor microenvironment communication in connective tissues
Gonzalez-Molina, J., Gramolelli, S., Liao, Z., Carlson, J. W., Ojala, P. M., & Lehti, K. (2019) · Cells · doi:10.3390/cells8090991 · Cited by 89 · see citing works
GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein
Nakamura, M., Li, Y., Choi, B.-R., Matas-Rico, E., Troncoso, J., Takahashi, C., & Sockanathan, S. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe6178 · Cited by 38 · see citing works
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- Authors
- Oh, J., Takahashi, R., Kondo, S., Mizoguchi, A., Adachi, E., Sasahara, R. M., Nishimura, S., Imamura, Y., Kitayama, H., Alexander, D. B., Ide, C., Horan, T. P., Arakawa, T., Yoshida, H., Nishikawa, S.-I., Itoh, Y., Seiki, M., Itohara, S., Takahashi, C., & Noda, M.
- Affiliations
- Kyoto University (JP)
- Kitasato University (JP)
- RIKEN Center for Brain Science (JP)
- Amgen (United States) (US)
- Institute of Medical Science, The University of Tokyo (JP)
- Corresponding author
- Noda, Makoto
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-12
- Volume
- 107
- Issue
- 6
- Pages
- 789-800
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2152667145
- Cited by
- 728
- References
- 1
- Citations by year
- 2026: 12 · 2025: 14 · 2024: 11 · 2023: 16 · 2022: 17 · 2021: 27 · 2020: 22 · 2019: 30 · 2018: 25 · 2017: 23 · 2016: 29 · 2015: 39 · 2014: 36 · 2013: 38 · 2012: 45
- FWCI
- 10.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Kyoto University Research Information Repository (Kyoto University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Angiogenesis and VEGF in Cancer
- Keywords
- RECK, matrix metalloproteinases, MMP-2, MT1-MMP, MMP-9, extracellular matrix remodeling, angiogenesis, tumor angiogenesis, collagen fibrils, basement membrane, vascular development, tumor invasion, fibrosarcoma, metastasis
- MeSH terms
- Animals, Cells, Cultured, Embryo, Mammalian, Extracellular Matrix, Humans, Immunohistochemistry, Membrane Glycoproteins, Metalloendopeptidases, Mice, Nude, Muscle, Smooth, Vascular, Mutation, Neoplasm Transplantation, Neoplasms, Experimental, Neovascularization, Pathologic, Transfection, Tumor Cells, Cultured, Down-Regulation, Gene Targeting, Neovascularization, Physiologic, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9, Matrix Metalloproteinases, Mice, Matrix Metalloproteinases, Membrane-Associated, Matrix Metalloproteinase 14, GPI-Linked Proteins, Matrix Metalloproteinase Inhibitors
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