Corneal Dermatopontin Interacts with Keratan Sulfate Proteoglycans
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Dermatopontin is an extracellular matrix protein with many functions, amongst which is the involvement in collagen fibrils’ organization. It has been isolated from bovine corneal stroma, alone and in a complex with keratan sulfate proteoglycans, using 7 M urea followed by ion-exchange chromatography. Chromatographic and antibody-based studies suggest that dermatopontin binds to lumican and keratocan keratan sulfate proteoglycans (KSPGs), and that it binds directly to corneal keratan sulfate chains. As the protein cores of KS-PGs are known to bind collagen, our results suggest that the KS chains act as spacers between DPT and proteoglycans, and hence collagen fibrils. This would contribute to the pattern of organization of the fibrils that is required for corneal transparency, and may explain why loss of keratan sulfate chains would result in disorganization of the collagen fibrils in the corneal stroma leading to opacity and blindness, and may also explain the effect of knocking out the DPT gene in mouse, resulting in disturbing the collagen organization and increase in the inter-fibril distance