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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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“Matrix metalloproteinases (MMPs) are soluble or membranebound zinc-dependent proteases that can degrade or proteolytically modify all the essential extracellular matrix (ECM) components, including collagens, fibronectin, and proteoglycan (Sternlicht and Werb, 2001;Werb, 1997; Yong et al., 2001).”
BackgroundTakács, E., Nyilas, R., Szepesi, Z., Baracskay, P., Karlsen, B., Røsvold, T., Bjørkum, A. A., Czurkó, A., Kovács, Z., Kékesi, A. K., et al. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.03.003 · Cited by 63
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Structural and functional changes in the alveolar bone osteoclasts of estrogen‐treated rats
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α-Ionone Protects Against UVB-Induced Photoaging in Human Dermal Fibroblasts
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The role of matrix metalloproteinases in liver function and disease
Mitropoulou, G., Kompoura, V., Saffioti, F., & Mavroeidis, V. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl27127 · Cited by 14
Van Pham, P., Dang, L. T.-T., Dinh, U. T., Truong, H. T.-T., Huynh, B. N., Van Le, D., & Phan, N. K. (2014) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-013-9706-1 · Cited by 8
Peripheral immune-derived matrix metalloproteinase promotes stress susceptibility
Russo, S., Cathomas, F., Lin, H.-Y., Chan, K., Li, L., Durand-de Cuttoli, R., Parise, L., Aubry, A., Muhareb, S., Desland, F., et al. (2023) · doi:10.21203/rs.3.rs-1647827/v1 · Cited by 189
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
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