Lectin binding sites in normal, scarred, and lattice dystrophy corneas. Issue 1 (January 1991)

• Record Type: Journal Article
• Authors: Bishop, P N; Bonshek, R E; Jones, C J; Ridgway, A E; Stoddart, R W
• Is Part Of: British journal of ophthalmology. Volume 75:Issue 1(1991)
• Page Start: 22
• Page End: 27
• Publication Date: 1991-01
• Subjects: Ophthalmology -- Periodicals; 617.7
• DOI: 10.1136/bjo.75.1.22
• Languages: English
• ISSNs: 0007-1161

Abstract

Abstract : Normal, scarred, and dystrophic corneas were histochemically probed with a panel of 16 lectins by means of an avidin-biotin revealing system. Normal corneal epithelial cells, keratocytes, and endothelial cells expressed at least two distinct N-linked oligosaccharide subsets, of the non-bisected, biantennary and bisected, bi-/triantennary types. Corneal scars stained variably with the lectin subsets described above, and with Maclura pomifera agglutinin. Lattice dystrophy corneas showed a loss of the oligosaccharide expression observed on the plasma membranes of normal epithelial cells, and there was concurrent deposition of extracellular glycoprotein within the corneal stroma, which was of the same oligosaccharide subsets as were lost from the epithelial cell plasma membranes. This extracellular stromal glycoprotein was far more widely deposited than the amyloid and extended well beyond the stromal scarring. We propose that these observations are related and that in lattice corneal dystrophy a glycoprotein(s) is shed from the plasma membranes of epithelial cells and sequestrated within the corneal stroma, where it subsequently stimulates amyloid deposition.