Quantitative analysis of type I collagen fibril regulation by lumican and decorin using AFM.

Date publication

septembre 2013

Auteurs

Membres identifiés du Cancéropôle Est :
Dr BREZILLON Stéphane

Tous les auteurs :
Stamov DR, Muller A, Wegrowski Y, Brezillon S, Franz CM

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/23747391

Résumé

Lumican and decorin, two members of the small leucine-rich repeat proteoglycan (SLRP) family, have been implicated as regulators of collagen I fibril structure in different tissues. Both proteoglycans consist of a core protein and a glycosaminoglycan (GAG) chain, but quantitative information regarding the precise role of the protein and GAG moieties in regulating collagen structure is still limited. In this study, we used AFM imaging and a model system of aligned collagen I nanofibrils to investigate the role of lumican and decorin on collagen I fibril structure with high resolution. When co-assembled with collagen I, recombinant lumican or decorin proteins lacking the GAG chains decreased collagen fibril width to values below

Référence

J Struct Biol. 2013 Sep;183(3):394-403