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Ultrastructural localization of sulfated and unsulfated keratan sulfate in normal and macular corneal dystrophy type I.

Lewis, David and Davies, Yvonne and Nieduszynski, Ian A. and Lawrence, Fiona and Quantock, Andrew J. and Bonshek, Richard and Fullwood, Nigel J. (2000) Ultrastructural localization of sulfated and unsulfated keratan sulfate in normal and macular corneal dystrophy type I. Glycobiology, 10 (3). pp. 305-312.

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Abstract

Keratan sulfate (KS) proteoglycans are of importance for the maintenance of corneal transparency as evidenced in the condition macular corneal dystrophy type I (MCD I), a disorder involving the absence of KS sulfation, in which the cornea becomes opaque. In this transmission electron microscope study quantitative immuno- and histochemical methods have been used to examine a normal and MCD I cornea. The monoclonal antibody, 5-D-4, has been used to localize sulfated KS and the lectin Erythrina cristagalli agglutinin (ECA) to localize poly N-acetyllactosamine (unsulfated KS). In normal cornea high levels of sulfated KS were detected in the stroma, Bowman’s layer, and Descemet’s membrane and low levels in the keratocytes, epithelium and endothelium. Furthermore, in normal cornea, negligible levels of labeling were found for N-acetyllactosamine (unsulfated KS). In the MCD I cornea sulfated KS was not detected anywhere, but a specific distribution of N-acetyllactosamine (unsulfated KS) was evident: deposits found in the stroma, keratocytes, and endothelium labeled heavily as did the disrupted posterior region of Descemet’s membrane. However, the actual cytoplasm of cells and the undisrupted regions of stroma revealed low levels of labeling. In conclusion, little or no unsulfated KS is present in normal cornea, but in MCD I cornea the abnormal unsulfated KS was localized in deposits and did not associate with the collagen fibrils of the corneal stroma. This study has also shown that ECA is an effective probe for unsulfated KS.

Item Type: Article
Journal or Publication Title: Glycobiology
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Science and Technology > Lancaster Environment Centre
Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 9096
Deposited By: Dr Nigel J Fullwood
Deposited On: 23 May 2008 13:38
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 18:31
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/9096

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