Structural interactions between collagen and proteoglycans are elucidated by three-dimensional electron tomography of bovine cornea
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Interactions between collagens and proteoglycans help define the structure and function of extracellular matrices. The cornea, which contains proteoglycans with keratan sulphate or chondroitin/dermatan sulphate glycosaminoglycan chains, is an excellent model system in which to study collagen-proteoglycan structures and interactions. Here, we present the first three-dimensional electron microscopic reconstructions of the cornea, and these include corneas from which glycosaminoglycans have been selectively removed by enzymatic digestion. Our reconstructions show that narrow collagen fibrils associate with sulphated proteoglycans that appear as extended, variable-length linear structures. The proteoglycan network appears to tether two or more collagen fibrils, and thus organize the matrix with enough spatial specificity to fulfill the requirements for corneal transparency. Based on the data, we propose that the characteristic pseudohexagonal fibril arrangement in cornea is controlled by the balance of a repulsive force arising from osmotic pressure and an attractive force due to the thermal motion of the proteoglycans.
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Three-dimensional electron tomographic reconstructions of bovine cornea showed that collagen fibrils were not lying on a perfect hexagonal lattice and that there was nothing systematic in the geometry of connections of adjacent or next nearest collagen fibrils.
“From the reconstructions, it was evident that the collagen fibrils were not laying on a perfect hexagonal lattice, and also that there was nothing systematic in the geometry of the connections of adjacent or next nearest collagen fibrils.”
From Corneal structure and transparency (2015) · cites this paper as Lewis et al., 2010
It is very difficult to see how a Fibonacci quasi-crystalline fibril arrangement could arise spontaneously in a cornea, especially given non-systematic interactions between collagen fibrils and proteoglycans.
“However, it is very difficult to see how a Fibonacci quasi-crystalline fibril arrangement could arise spontaneously in a cornea, especially in the light of non-systematic interactions between collagen fibrils and proteoglycans (see below – Lewis et al., 2010).”
From Corneal structure and transparency (2015) · cites this paper as Lewis et al., 2010
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Research works printed but not linked: 19
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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
Self-citation
- Authors
- Lewis, P. N., Pinali, C., Young, R. D., Meek, K. M., Quantock, A. J., & Knupp, C.
- Affiliations
- Cardiff University (GB)
- Corresponding author
- Knupp, Carlo
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 18
- Issue
- 2
- Pages
- 239-245
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2149496973
- Cited by
- 139
- References
- 0
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 8 · 2023: 12 · 2022: 11 · 2021: 7 · 2020: 7 · 2019: 8 · 2018: 8 · 2017: 11 · 2016: 10 · 2015: 12 · 2014: 10 · 2013: 13 · 2012: 2
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- Royal Society
- Biotechnology and Biological Sciences Research Council (BBS/B/10994, BB/D001919/1, BB/F022077/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Corneal surgery and disorders
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Keywords
- cornea, extracellular matrix, glycosaminoglycans, keratan sulfate, collagen fibrils, corneal transparency, osmotic pressure, thermal motion
- MeSH terms
- Animals, Cattle, Chondroitinases and Chondroitin Lyases, Collagen, Cornea, Glycosaminoglycans, Glycoside Hydrolases, Models, Molecular, Proteoglycans, Electron Microscope Tomography
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