Cross-linking and the molecular packing of corneal collagen
Abstract
We have quantitatively characterized, for the first time, the cross-linking in bovine cornea collagen as a function of age. The major iminium reducible cross-links were dehydro-hydroxylysinonorleucine (deH-HLNL) and dehydro-histidinohydroxymerodesmosine (deH-HHMD). The former rapidly diminished after birth; however, the latter persisted in mature animals at a level of 0.3 - 0.4 moles/mole of collagen. A nonreducible cross-link, histidinohydroxylysinonorleucine (HHL), previously found only in skin, was also found to be a major mature cross-link in cornea. The presence of HHL indicates that cornea fibrils have a molecular packing similar to skin collagen. However, like deH-HHMD, the HHL content in corneal fibrils only reaches a maximum value with time about half that of skin. These data suggest that the corneal fibrils are comprised of discrete filaments that are internally stabilized by HHL and deH-HHMD cross-links. This pattern of intermolecular cross-linking would facilitate the special collagen swelling property required for corneal transparency.
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Microfibrils have a right-handed twist within the fibrils and are stabilised by covalent intermolecular and intramolecular crosslinks.
“Microfibrils have a right-handed twist within the fibrils (Orgel et al., 2006), and are stabilised by covalent intermolecular and intramolecular crosslinks (Yamauchi et al., 1996).”
From Corneal structure and transparency (2015) · cites this paper as Yamauchi et al., 1996
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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
- Yamauchi, M., Chandler, G. S., Tanzawa, H., & Katz, E. P.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Chiba University (JP)
- UConn Health (US)
- Corresponding author
- Yamauchi, Mitsuo
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1996-02
- Volume
- 219
- Issue
- 2
- Pages
- 311-315
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2032366105
- Cited by
- 45
- References
- 0
- Citations by year
- 2024: 2 · 2023: 1 · 2019: 4 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 1 · 2013: 2 · 2012: 2
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR037604, AR 37604)
- National Institute of Dental and Craniofacial Research (DE10489, R01DE010489)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Corneal surgery and disorders
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Corneal Surgery and Treatments
- Keywords
- corneal collagen, collagen cross-linking, molecular packing, corneal aging, corneal transparency, collagen fibrils, cornea, skin collagen
- MeSH terms
- Aging, Animals, Cattle, Chromatography, High Pressure Liquid, Collagen, Cornea, Cross-Linking Reagents, Desmosine, Dipeptides, Histidine, Models, Structural, Skin
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