Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice.
Open accessAbstract
Macrophages secrete a variety of proteinases that are thought to participate in remodeling of the extracellular matrix associated with inflammatory processes. We have eliminated expression of the macrophage metalloelastase (MME) gene by targeted disruption to assess the role of this protein in macrophage-mediated proteolysis. We found that the macrophages of MME-deficient (MME-/-) mice have a markedly diminished capacity to degrade extracellular matrix components. In addition, MME-/- macrophages are essentially unable to penetrate reconstituted basement membranes in vitro and in vivo. MME is therefore required for macrophage-mediated extracellular matrix proteolysis and tissue invasion.
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MMP12 encodes a potent protease that degrades elastin, the major component of elastic fibers.
“MMP12 encodes a potent protease that degrades elastin, the major component of elastic fibers54.”
From A genomics approach reveals insights into the importance of gene losses for mammalian adaptations (2018) · cites this paper as [54]
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- [11]Ho, M. & Springer, T. A. (1983) J. Biol. Chem. 258, 632–634.
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- Authors
- Shipley, J. M., Wesselschmidt, R. L., Kobayashi, D. K., Ley, T. J., & Shapiro, S. D.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1996-04-30
- Volume
- 93
- Issue
- 9
- Pages
- 3942-3946
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC39464
- OpenAlex
- W2149587786
- Cited by
- 502
- References
- 0
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 13 · 2023: 11 · 2022: 8 · 2021: 8 · 2020: 11 · 2019: 11 · 2018: 13 · 2017: 20 · 2016: 14 · 2015: 13 · 2014: 22 · 2013: 16 · 2012: 17
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL029594, HL 29594, HL 50472, R01HL050472, HL55160-01, R01HL055160)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
- Keywords
- macrophage metalloelastase, matrix metalloproteinase-12, macrophages, extracellular matrix degradation, proteolysis, basement membrane invasion, tissue invasion, knockout mice, inflammation, matrix remodeling
- MeSH terms
- Animals, Base Sequence, Basement Membrane, Cloning, Molecular, Elastin, Extracellular Matrix, Inflammation, Metalloendopeptidases, Mice, Inbred Strains, Molecular Sequence Data, Recombinant Proteins, Transfection, Gene Library, Polymerase Chain Reaction, Macrophages, Peritoneal, DNA Primers, Mice, Matrix Metalloproteinase 12
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