Different architectures of collagen fibrils enforce different fibrillogenesis mechanisms
Open accessAbstract
According to current knowledge on collagen fibril-logenesis, collagen fibrils are formed by a cooperative process involving lateral fusion of small protofibrils. Almost all the experimental research, however, was carried out on tendon collagen, whose fibrils are characterized by approximately straight subfibrils. By contrast, in most tissues the collagen fibril sub-units follow a helical course in which geometrical constraints prevent lateral fusions, thereby implying a different mechanism where collagen fibrils grow by addition of individual microfibrils rather than by lateral fusion of pre-assembled subfibrils. The proc-ess at the origin of these fibrils may provide a simple, automatic explanation for the remarkable uniformity in fibrils size observed in most tissues without re-quiring the intervention of unknown mechanisms of diameter control. Other mechanisms of growth con-trol remain indispensable to terminate the fibril-logenesis process in tendons and ligaments.
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In vitro, fibrils formed by collagen I and collagen V are larger than those found in vivo, indicating additional mechanisms such as microfibrillar coiling or collagen-bound disaccharides regulate fibril diameter.
“However, it was noticed that, in vitro, the fibrils formed by collagen I and collagen V are larger than those found in vivo. This indicates that there may be additional mechanisms such as microfibrillar coiling (Raspanti, 2010) or collagen-bound disaccharides (Harding et al., 1980) that regulate fibril diameter.”
From Corneal structure and transparency (2015) · cites this paper as Raspanti, 2010
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“can [12], but also tenascin [13], perlecan [14], matrilin”
BackgroundChondroitin Sulfate Perlecan Enhances Collagen Fibril Formation
Kvist, A. J., Johnson, A. E., Mörgelin, M., Gustafsson, E., Bengtsson, E., Lindblom, K., Aszódi, A., Fässler, R., Sasaki, T., Timpl, R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607892200 · Cited by 102 · see citing works
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Research works printed but not linked: 6
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Corneal structure and transparency
Meek, K. M., & Knupp, C. (2015) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2015.07.001 · Cited by 853 · see citing works
- Authors
- Raspanti, M.
- Affiliations
- University of Insubria (IT)
- Corresponding author
- Raspanti, Mario
- ORCID
- Raspanti, Mario
- Venue
- Journal of Biomedical Science and Engineering
- Publisher
- Scientific Research Publishing, Inc.
- Published
- 2010
- Volume
- 03
- Issue
- 12
- Pages
- 1169-1174
- ISSN
- 1937-6871 (ISSN-L)
- 1937-688X
- OpenAlex
- W1979524110
- Cited by
- 5
- References
- 2
- Citations by year
- 2017: 1 · 2015: 2 · 2012: 1
- FWCI
- 0.26
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- Journal of Biomedical Science and Engineering (publishedVersion, cc-by)
- IrInSubria (University of Insubria) (submittedVersion, other-oa)
- 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 › Orthopedics and Sports Medicine › Tendon Structure and Treatment
- Keywords
- collagen fibrillogenesis, tendon collagen
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