Normally sulphated and highly sulphated glycosaminoglycans (GAG) affecting fibrillogenesis of type I and type II collagen in vitro.
Proteoglycans (PG) and glycosaminoglycans (GAG) influence the aggregation of collagen molecules during fibrillogenesis and the ultimate fibril width. The current in vitro experiments suggest that collagen type II may interact more strongly with highly sulphated GAG than type I collagen. Electron microscopic investigations indicate that, after addition of highly sulphated GAG, the fibrils of type II collagen become significantly (p less than 0.001) thicker than fibrils of a control experiment.
D002809:Chondroitin Sulfates / Q000494:pharmacology; D003080:Cold Temperature; D003094:Collagen; D003871:Dermatan Sulfate / Q000494:pharmacology; D006025:Glycosaminoglycans / Q000494:pharmacology*; D006358:Hot Temperature; D006820:Hyaluronic Acid / Q000494:pharmacology; D007632:Keratan Sulfate / Q000494:pharmacology; D046911:Macromolecular Substances; D010426:Pentosan Sulfuric Polyester / Q000494:pharmacology; D013329:Structure-Activity Relationship
D006025:Glycosaminoglycans; D046911:Macromolecular Substances; D003871:Dermatan Sulfate; D010426:Pentosan Sulfuric Polyester; C010034:Arteparon; D006820:Hyaluronic Acid; D002809:Chondroitin Sulfates; D003094:Collagen; D007632:Keratan Sulfate