Cited by 39Collagen: Extraction and CharacterizationConnective tissue disorders researchBlood properties and coagulation

The collαgen III fibril has a “flexi-rod” structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

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Parkin, J. Des, San Antonio, James D., Persikov, Anton V., Dagher, Hayat, Dalgleish, Raymond, Jensen, Shane T., Jeunemaitre, Xavier, Savige, Judy·2017·PLOS ONE

Abstract

Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.

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  1. [26]EJ M, editor (1984) Chemistry of the collagens and their distribution New York: Elsevier pp 41– 82
  2. [100]Piez KA, Reddi AH (1984) Extracellular matrix biochemistry. New York; Oxford: Elsevier.

Authors
Parkin, J. D., San Antonio, J. D., Persikov, A. V., Dagher, H., Dalgleish, R., Jensen, S. T., Jeunemaitre, X., & Savige, J.
Affiliations
  • The University of Melbourne (AU)
  • Princeton University (US)
  • University of Leicester (GB)
  • University of Pennsylvania (US)
Corresponding author
  • Parkin, J. Des
  • Persikov, Anton V.
  • Dagher, Hayat
  • Dalgleish, Raymond
  • Jensen, Shane T.
  • Savige, Judy
Venue
PLOS ONE
Published
2017-07-13
Volume
12
Issue
7
Pages
e0175582
ISSN
1932-6203 (ISSN-L)
OpenAlex
W2734776539
Cited by
39
References
123
Citations by year
2026: 8 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 1
FWCI
1.08
Type
journal article
Language
en
Open access
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Minerva Access (University of Melbourne) (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
  • Leicester Research Archive (University of Leicester) (submittedVersion, cc-by)
Funders
Stryker
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Blood properties and coagulation
Keywords
type III collagen, collagen fibril structure, hemostasis, von Willebrand factor binding, alpha2beta1 integrin, glycoprotein VI, COL3A1, fibril formation, ligand-binding domain, wound healing, embryonic development
MeSH terms
Amino Acid Sequence, Binding Sites, Hemostasis, Humans, Platelet Membrane Glycoproteins, Protein Binding, von Willebrand Factor, Collagen Type III, Integrin alpha2beta1, Protein Stability, Protein Interaction Maps

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