Cited by 545Collagen: Extraction and CharacterizationConnective tissue disorders researchCellular Mechanics and Interactions

Type V collagen controls the initiation of collagen fibril assembly

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Wenstrup, Richard J., Florer, Jane B., Brunskill, Eric W., Bell, Sheila M., Chervoneva, Inna, Birk, David E.·2004·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1074/jbc.m409622200

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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
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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