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Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions
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Completion of genome sequences for many organisms allows a reasonably complete definition of the complement of extracellular matrix (ECM) proteins. In mammals this "core matrisome" comprises ∼300 proteins. In addition there are large numbers of ECM-modifying enzymes, ECM-binding growth factors, and other ECM-associated proteins. These different categories of ECM and ECM-associated proteins cooperate to assemble and remodel extracellular matrices and bind to cells through ECM receptors. Together with receptors for ECM-bound growth factors, they provide multiple inputs into cells to control survival, proliferation, differentiation, shape, polarity, and motility of cells. The evolution of ECM proteins was key in the transition to multicellularity, the arrangement of cells into tissue layers, and the elaboration of novel structures during vertebrate evolution. This key role of ECM is reflected in the diversity of ECM proteins and the modular domain structures of ECM proteins both allow their multiple interactions and, during evolution, development of novel protein architectures.
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“Hynes and Naba first presented the matrisomics concept in 2012, establishing a matrisome database (http://matrisomeproject.mit.edu/) which classifies ECM into core matrisome proteins, including collagens, proteoglycans, and glycoproteins, and matrisome‐associated proteins, encompassing secreted factors, regulators, and ECM‐affiliated proteins, thus providing a reliable reference for comprehensive”
From Bioactive scaffolds for tissue engineering: A review of decellularized extracellular matrix applications and innovations (2025) · cites this paper as [118]
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“Native ECM is complex; it contains over 300 different proteins, each of which has a different biological function and stiffness123.”
From Towards organoid culture without Matrigel (2021) · cites this paper as [123]
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Metadata
- Authors
- Hynes, R. O., & Naba, A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Hynes, R. O.
- ORCID
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-09-21
- Volume
- 4
- Issue
- 1
- Pages
- a004903-a004903
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3249625
- OpenAlex
- W2119792393
- Cited by
- 1,349
- References
- 86
- Citations by year
- 2026: 94 · 2025: 137 · 2024: 129 · 2023: 143 · 2022: 142 · 2021: 146 · 2020: 136 · 2019: 85 · 2018: 93 · 2017: 61 · 2016: 46 · 2015: 37 · 2014: 46 · 2013: 37 · 2012: 12
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (U54CA163109, P30CA014051)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- extracellular matrix, matrisome, ECM receptors, extracellular matrix remodeling, cell-matrix interactions, evolution of multicellularity, protein domain architecture, cell proliferation and differentiation
- MeSH terms
- Animals, Collagen, Glycoproteins, Humans, Proteoglycans, Integrins, Transforming Growth Factor beta, Extracellular Matrix Proteins, Evolution, Molecular
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