The collagen family members as cell adhesion proteins
Abstract
The collagen family of extracellular matrix proteins has played a fundamental role in the evolution of multicellular animals. At the present, 28 triple helical proteins have been named as collagens and they can be divided into several subgroups based on their structural and functional properties. In tissues, the cells are anchored to collagenous structures. Often the interaction is indirect and mediated by matrix glycoproteins, but cells also express receptors, which have the ability to directly bind to the triple helical domains in collagens. Some receptors bind to sites that are abundant in all collagens. However, increasing evidence indicates that the coevolution of collagens and cell adhesion mechanisms has given rise to receptors that bind to specific motifs in collagens. These receptors may also recognize the different members of the large collagen family in a selective manner. This review summarizes the present knowledge about the properties of collagen subtypes as cell adhesion proteins. BioEssays 29:1001–1010, 2007. © 2007 Wiley Periodicals, Inc.
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Collagen possesses properties suitable for anti-adhesion applications, including excellent biocompatibility, biodegradability, hydrophilicity, non-immunogenicity, and ability to act as a physical barrier against fibrin bridge formation.
“Collagen possesses unique properties that make it highly suitable for anti-adhesion applications, including excellent biocompatibility, biodegradability, hydrophilicity, and non-immunogenicity, in addition to its ability to act as a physical barrier against fibrin bridge formation [20,21].”
From Biomaterials in Postoperative Adhesion Barriers and Uterine Tissue Engineering (2025) · cites this paper as [20]
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Biomaterials in Postoperative Adhesion Barriers and Uterine Tissue Engineering
Fazel Anvari-Yazdi, A., Badea, I., & Chen, X. (2025) · Gels · doi:10.3390/gels11060441 · Cited by 20 · see citing works
- Authors
- Heino, J.
- Affiliations
- University of Turku (FI)
- Corresponding author
- Heino, Jyrki
- ORCID
- Heino, Jyrki
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2007-09-17
- Volume
- 29
- Issue
- 10
- Pages
- 1001-1010
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2110119922
- Cited by
- 439
- References
- 2
- Citations by year
- 2026: 16 · 2025: 15 · 2024: 23 · 2023: 43 · 2022: 35 · 2021: 26 · 2020: 24 · 2019: 29 · 2018: 23 · 2017: 24 · 2016: 19 · 2015: 26 · 2014: 13 · 2013: 24 · 2012: 14
- FWCI
- 1.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- BioEssays (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- collagen, cell adhesion, collagen receptor, extracellular matrix, triple helix, collagen types, receptor specificity
- MeSH terms
- Animals, Binding Sites, Cell Adhesion, Collagen, Extracellular Matrix, Glycoproteins, Humans, Models, Molecular, Protein Binding, Protein Denaturation, Protein Structure, Secondary, Amino Acid Motifs, Receptors, Collagen
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