Parfitt, Geraint ![]() ![]() ![]() ![]() |
Abstract
The spatial distribution of collagen fibrils in the corneal stroma is essential for corneal transparency and is primarily regulated by extrafibrillar proteoglycans, which are multi-functional polymers that interact with hybrid type I/V collagen fibrils. In order to understand more about proteoglycan organisation and collagen associations in the cornea, three-dimensional electron microscopy reconstructions of collagen-proteoglycan interactions in the anterior, mid and posterior stroma from a Chst5 knockout mouse, which lacks a keratan sulphate sulphotransferase, were obtained. Both longitudinal and transverse section show sinuous, oversized proteoglycans with near-periodic, orthogonal off-shoots. In many cases, these proteoglycans traverse over 400 nm of interfibrillar space interconnecting over 10 collagen fibrils. The reconstructions suggest that multiple chondroitin sulphate/dermatan sulphate proteoglycans have aggregated laterally and, possibly, end-to-end, with orthogonal extensions protruding from the main electron-dense stained filament. We suggest possible mechanisms as to how sulphation differences may lead to this increase in aggregation of proteoglycans in the Chst5-null mouse corneal stroma and how this relates to proteoglycan packing in healthy corneas.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Optometry and Vision Sciences |
Subjects: | R Medicine > RE Ophthalmology |
Uncontrolled Keywords: | Mouse cornea ; Collagen fibrils ; Proteoglycans ; Chst5 ; Three-dimensional reconstruction ; Electron microscopy |
Publisher: | Elsevier |
ISSN: | 1047-8477 |
Last Modified: | 19 Oct 2022 08:32 |
URI: | https://orca.cardiff.ac.uk/id/eprint/18116 |
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