Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.585225
Title: Proteoglycans as dynamic regulators of the organised collagen fibril architecture in the cornea : an electron tomography study of the mouse corneal stroma
Author: Parfitt, Geraint
Awarding Body: Cardiff University
Current Institution: Cardiff University
Date of Award: 2011
Availability of Full Text:
Access through EThOS:
Access through Institution:
Abstract:
The cornea is the primary refractive element of the eye and is also fundamental to the protection of the visual system. Collagen is the major constituent of the cornea, where it is organised in a lattice that enables corneal transparency. Proteoglycan macromolecules are thought to regulate the diameter and spatial order of collagen fibrils in the cornea, which are both pre-requisites for corneal transparency, although the mechanisms by which they organise fibrils are not fully elucidated. This investigation examined the morphology, morphometry and organisation of proteoglycans three-dimensionally, in both normal and genetically altered mouse corneas, to gain a greater understanding of proteoglycan structure-function relationships. In summary, we found that proteoglycans are primarily responsible for the remarkable collagen organisation in the mouse cornea, which allows for corneal transparency. The self- association of proteoglycans into complexes is likely to result in a robust attachment of neighbouring fibrils and provides biomechanical strength, whilst sulphation patterns are seen to have a direct effect on the aggregation potential of proteoglycans. Removal of proteoglycans, particularly lumican, affects the regulation of both fibril size and spatial order, both required for corneal transparency.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.585225  DOI: Not available
Share: