Type V collagen controls the initiation of collagen fibril assembly
Open accessAbstract
Vertebrate collagen fibrils are heterotypically composed of a quantitatively major and minor fibril collagen. In non-cartilaginous tissues, type I collagen accounts for the majority of the collagen mass, and collagen type V, the functions of which are poorly understood, is a minor component. Type V collagen has been implicated in the regulation of fibril diameter, and we reported recently preliminary evidence that type V collagen is required for collagen fibril nucleation (Wenstrup, R. J., Florer, J. B., Cole, W. G., Willing, M. C., and Birk, D. E. (2004) J. Cell. Biochem. 92, 113-124). The purpose of this study was to define the roles of type V collagen in the regulation of collagen fibrillogenesis and matrix assembly. Mouse embryos completely deficient in pro-alpha1(V) chains were created by homologous recombination. The col5a1-/- animals die in early embryogenesis, at approximately embryonic day 10. The type V collagen-deficient mice demonstrate a virtual lack of collagen fibril formation. In contrast, the col5a1+/- animals are viable. The reduced type V collagen content is associated with a 50% reduction in fibril number and dermal collagen content. In addition, relatively normal, cylindrical fibrils are assembled with a second population of large, structurally abnormal collagen fibrils. The structural properties of the abnormal matrix are decreased relative to the wild type control animals. These data indicate a central role for the evolutionary, ancient type V collagen in the regulation of fibrillogenesis. The complete dependence of fibril formation on type V collagen is indicative of the critical role of the latter in early fibril initiation. In addition, this fibril collagen is important in the determination of fibril structure and matrix organization.
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Collagen V is abundantly distributed in a variety of tissues as heterotrimers, which co-assemble with collagen I to form heterotypic fibrils.
“This collagen is abundantly distributed in a variety of tissues as heterotrimers, which co-assemble with collagen I to form heterotypic fibrils [42].”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [42]
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“An inverse relationship has been found between fibril diameter and the amount of collagen type III or V towards collagen type I [45].”
Background
- Authors
- Wenstrup, R. J., Florer, J. B., Brunskill, E. W., Bell, S. M., Chervoneva, I., & Birk, D. E.
- Affiliations
- Cincinnati Children's Hospital Medical Center (US)
- University of Cincinnati (US)
- Thomas Jefferson University (US)
- Corresponding author
- Wenstrup, Richard J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 279
- Issue
- 51
- Pages
- 53331-53337
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2012792811
- Cited by
- 545
- References
- 42
- Citations by year
- 2026: 25 · 2025: 23 · 2024: 24 · 2023: 24 · 2022: 27 · 2021: 40 · 2020: 33 · 2019: 29 · 2018: 21 · 2017: 33 · 2016: 25 · 2015: 30 · 2014: 28 · 2013: 31 · 2012: 27
- FWCI
- 7.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Eye Institute (R01EY005129, EY05129)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR047054, AR47054)
- 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
- type V collagen, collagen fibril assembly, fibril formation, fibril nucleation, type I collagen, embryonic lethality, skin collagen, extracellular matrix organization, fibril diameter
- MeSH terms
- Animals, Collagen, DNA, Electrophoresis, Polyacrylamide Gel, Embryo, Mammalian, Exons, Extracellular Matrix, Genetic Vectors, Genotype, Microscopy, Electron, Models, Biological, Models, Genetic, Skin, Time Factors, Blotting, Western, In Situ Hybridization, Cell Culture Techniques, Collagen Type V, Microscopy, Electron, Transmission, Mice
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