How Matrix Metalloproteinases Regulate Cell Behavior

Sternlicht, Mark D.; Werb, Zena

doi:10.1146/annurev.cellbio.17.1.463

Cited by 3,959Protease and Inhibitor MechanismsTGF-β signaling in diseasesBlood Coagulation and Thrombosis Mechanisms

How Matrix Metalloproteinases Regulate Cell Behavior

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Sternlicht, Mark D., Werb, Zena·2001·Annual Review of Cell and Developmental Biology

DOI 10.1146/annurev.cellbio.17.1.463PMC PMC2792593

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Abstract

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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Macrophages regulate ECM content and remodeling by secretion of proteases and inhibitors, such as MMPs and TIMPs.
“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]
The Introduction (page unavailable) says macrophages secrete MMP12, MMPs remodel the ECM, and TIMPs are secreted inhibitors of MMPs. It does not establish that macrophages secrete TIMPs or that this regulation occurs specifically in the final phase of healing. (LLM, conf=0.86)
Experimental — accuracy not yet measured
MMPs can affect cell behavior by cleaving circulating, cell surface and pericellular molecules.
“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]
MMPs can facilitate release of cell surface and matrix bound growth factors and cytokines and can also cleave cell surface receptors.
“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]
MMPs are proteolytic proteins that hydrolyze components of the extracellular matrix.
“Matrix metalloproteinases are proteolytic proteins that hydrolyze components of the extracellular matrix.”
From Foreign body reaction to biomaterials (2008) · cites this paper as [138]
MMPs directly influence the composition of the ECM and in turn can impact cell movement, growth, differentiation and survival.
“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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Authors: Sternlicht, M. D., & Werb, Z.
Affiliations: University of California, San Francisco (US)
ORCID: Sternlicht, Mark D.
Werb, Zena
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
DOI: 10.1146/annurev.cellbio.17.1.463
PMC: PMC2792593
OpenAlex: W2128049766
Cited by: 3,959
References: 238
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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