Extracellular Matrix Assembly: A Multiscale Deconstruction
Open accessAbstract
The biochemical and biophysical properties of the extracellular matrix (ECM) dictate tissue-specific cell behaviour. The molecules that are associated with the ECM of each tissue, including collagens, proteoglycans, laminins and fibronectin, and the manner in which they are assembled determine the structure and the organization of the resultant ECM. The product is a specific ECM signature that is comprised of unique compositional and topographical features that both reflect and facilitate the functional requirements of the tissue.
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Collagen type I is the major constituent of the dermis, interlaced with other important ECM components such as collagen III and VII, fibronectin, vitronectin, hyaluronic acid, and glycosaminoglycans, such as heparin.
“Unlike Matrigel, the major constituent of the dermis is collagen type I, which is interlaced with other important ECM components such as collagen III and VII [23,24], fibronectin [25], vitronectin [11], hyaluronic acid [26,27], and glycosaminoglycans, such as heparin [28], all of which contribute to key physiological skin functions.”
From Efficient Generation of Skin Organoids from Pluripotent Cells via Defined Extracellular Matrix Cues and Morphogen Gradients in a Spindle‐Shaped Microfluidic Device (2024) · cites this paper as [24]
The citation to this source is attached specifically to vitronectin. In our copy, searches for vitronectin and dermis found vitronectin only in the References section; the substantive ECM passages do not establish that it is a component of the dermis. (LLM, conf=0.72)
Experimental — accuracy not yet measuredTGF-β is an important cytokine that promotes collagen production.
“Transforming growth factor-β (TGF-β) is an important cytokine that promotes collagen production (Mouw et al., 2014).”
From A Frog Peptide Ameliorates Skin Photoaging Through Scavenging Reactive Oxygen Species (2022) · cites this paper as Mouw et al., 2014
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- Authors
- Mouw, J. K., Ou, G., & Weaver, V. M.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Weaver, Valerie M.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-11-05
- Volume
- 15
- Issue
- 12
- Pages
- 771-785
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC4682873
- OpenAlex
- W2023026872
- Cited by
- 1,534
- References
- 182
- Citations by year
- 2026: 118 · 2025: 130 · 2024: 172 · 2023: 162 · 2022: 138 · 2021: 179 · 2020: 164 · 2019: 134 · 2018: 109 · 2017: 111 · 2016: 76 · 2015: 35 · 2014: 2
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- U.S. Department of Defense
- National Cancer Institute (U01CA151925, R01CA085492, R01CA138818, U54CA143836)
- National Institute of Environmental Health Sciences (U01ES019458)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Keywords
- extracellular matrix assembly, collagen, proteoglycans, laminin, fibronectin, ECM composition, cell behavior
- MeSH terms
- Animals, Basement Membrane, Extracellular Matrix, Humans, Neurons, Proteoglycans, Extracellular Matrix Proteins
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