An electron microscopical study of the influence of different glycosaminoglycans on the fibrillogenesis of collagen type I and II in vitro.
Proteoglycans (PG) and glycosaminoglycans (GAG) bind to collagen, and thus influence fibril formation. Polysaccharides interfere with the aggregation of collagen molecules and affect pattern formation. The morphological structure of type I and type II collagen was studied after adding different GAG to collagen solutions in test tubes in vitro. Electron microscopical investigations suggest that sulfated GAG change the aggregation behaviour of collagen molecules. Thus, the cross-striation pattern is changed. This effect seems to be based on the degree of sulfatation and not on the molecular weight of the GAG. Furthermore, GAG appear to have a stabilizing influence on the in vitro fibril formation.
D000818:Animals; D002417:Cattle; D002645:Chickens; D003094:Collagen / Q000378:metabolism*; D003238:Connective Tissue / Q000378:metabolism* / Q000648:ultrastructure; D006025:Glycosaminoglycans / Q000494:pharmacology*; D008854:Microscopy, Electron; D008970:Molecular Weight; D009210:Myofibrils / Q000502:physiology; D051381:Rats
D006025:Glycosaminoglycans; D003094:Collagen