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How Matrix Metalloproteinases Regulate Cell Behavior
Open accessAbstract
The matrix metalloproteinases (MMPs) constitute a multigene family of over 25 secreted and cell surface enzymes that process or degrade numerous pericellular substrates. Their targets include other proteinases, proteinase inhibitors, clotting factors, chemotactic molecules, latent growth factors, growth factor-binding proteins, cell surface receptors, cell-cell adhesion molecules, and virtually all structural extracellular matrix proteins. Thus MMPs are able to regulate many biologic processes and are closely regulated themselves. We review recent advances that help to explain how MMPs work, how they are controlled, and how they influence biologic behavior. These advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled. MMPs participate in numerous normal and abnormal processes, and there are new insights into the key substrates and mechanisms responsible for regulating some of these processes in vivo. Our knowledge in the field of MMP biology is rapidly expanding, yet we still do not fully understand how these enzymes regulate most processes of development, homeostasis, and disease.
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“In the final phase of healing, macrophages also regulate ECM content and remodeling by secretion of proteases and their inhibitors, such as matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinase (TIMPs) [75–77].”
From Transition from inflammation to proliferation: a critical step during wound healing (2016) · cites this paper as [76]
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“MMPs also can affect cell behavior by cleaving circulating, cell surface and pericellular molecules.”
From Foreign body reaction to biomaterials (2008) · cites this paper as [138]
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“MMPs can facilitate release of cell surface and matrix bound growth factors and cytokines and can also cleave cell surface receptors.”
From Foreign body reaction to biomaterials (2008) · cites this paper as [138]
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“Matrix metalloproteinases are proteolytic proteins that hydrolyze components of the extracellular matrix.”
From Foreign body reaction to biomaterials (2008) · cites this paper as [138]
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“MMPs directly influence the composition of the ECM and in turn can impact cell movement, growth, differentiation and survival.[138]”
From Foreign body reaction to biomaterials (2008) · cites this paper as [138]
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“The matrix metalloprotease (MMP) family of enzymes affects cellular and organoid development by degrading ECM proteins124.”
From Towards organoid culture without Matrigel (2021) · cites this paper as [124]
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Cited by
Sorted by citations
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
Self-citationMatrix Metalloproteinases: Regulators of the Tumor Microenvironment
Kessenbrock, K., Plaks, V., & Werb, Z. (2010) · Cell · doi:10.1016/j.cell.2010.03.015 · Cited by 5,151
Self-citationForeign body reaction to biomaterials
Anderson, J. M., Rodriguez, A., & Chang, D. T. (2008) · Seminars in Immunology · doi:10.1016/j.smim.2007.11.004 · Cited by 5,138
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Lutolf, M. P., & Hubbell, J. A. (2005) · Nature Biotechnology · doi:10.1038/nbt1055 · Cited by 4,551
Metadata
- Authors
- Sternlicht, M. D., & Werb, Z.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2001-11
- Volume
- 17
- Issue
- 1
- Pages
- 463-516
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- PMC
- PMC2792593
- OpenAlex
- W2128049766
- Cited by
- 3,959
- References
- 237
- Citations by year
- 2026: 41 · 2025: 72 · 2024: 85 · 2023: 95 · 2022: 101 · 2021: 119 · 2020: 139 · 2019: 123 · 2018: 149 · 2017: 149 · 2016: 148 · 2015: 163 · 2014: 183 · 2013: 195 · 2012: 200
- FWCI
- 11.86
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (CA37395, CA72006, P01CA072006, CA-58207, R37CA037395, P50CA058207, R01CA037395)
- 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
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- matrix metalloproteinases, extracellular matrix degradation, MMP regulation, MMP activation, matrix metalloproteinase inhibition, MMP secretion, cell behavior, adhesion molecules, protease inhibitors
- MeSH terms
- Animals, Bone and Bones, Cell Communication, Extracellular Matrix, Humans, Neoplasms, Protein Processing, Post-Translational, Transcription, Genetic, Signal Transduction, Extracellular Matrix Proteins, Neovascularization, Physiologic, Tissue Inhibitor of Metalloproteinases, Matrix Metalloproteinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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