Corneal Dermatopontin Interacts with Keratan Sulfate Proteoglycans
Loading...
Links to Files
Permanent Link
Collections
Author/Creator ORCID
Date
2022-08
Department
Program
Citation of Original Publication
Rights
This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
Subjects
Abstract
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