The Collagen Family
Open accessAbstract
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. Four collagens are type II membrane proteins that also exist in a soluble form released from the cell surface by shedding. Collagens play structural roles and contribute to mechanical properties, organization, and shape of tissues. They interact with cells via several receptor families and regulate their proliferation, migration, and differentiation. Some collagens have a restricted tissue distribution and hence specific biological functions.
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Among the collagens tested, collagen I, III, and V are classified as fibril-forming collagens, collagen IV forms network structures, and collagen VI forms beaded filaments.
“Among the collagens tested, collagen I, III, and V are classified as fibril-forming collagens, while collagen IV forms network structures, and collagen VI forms beaded filaments64.”
From Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins (2025) · cites this paper as [64]
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“There are at least 28 distinct varieties of collagen known to exist [60].”
- Authors
- Ricard-Blum, S.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-12-15
- Volume
- 3
- Issue
- 1
- Pages
- a004978-a004978
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3003457
- OpenAlex
- W2160075959
- Cited by
- 2,305
- References
- 2
- Citations by year
- 2026: 196 · 2025: 250 · 2024: 300 · 2023: 266 · 2022: 272 · 2021: 232 · 2020: 190 · 2019: 128 · 2018: 107 · 2017: 79 · 2016: 88 · 2015: 63 · 2014: 56 · 2013: 40 · 2012: 21
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Centre National de la Recherche Scientifique (UMR 5086)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- collagen, triple-helical domain, extracellular matrix, collagen receptor, cell proliferation, cell migration, cell differentiation, tissue mechanical properties, tissue organization
- MeSH terms
- Collagen, Mutation, Promoter Regions, Genetic, Protein Conformation, Genetic Variation, Protein Structure, Tertiary, Receptors, Collagen
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