title: Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan.
abstract: Collagen has found use as a scaffold material for tissue engineering as well as a coating material for implants with a view to enhancing osseointegration through mimicry of the bone extracellular matrix in vivo. The aim of this study was to compare the collagen types I, II, and III with regard to their ability to bind the small leucine-rich proteoglycans (SLRPs) decorin and biglycan during fibrillogenesis in vitro in phosphate buffer. In addition, the influence of SLRPs on the proportion of collagen molecules incorporated into fibrils during fibrillogenesis in vitro at high and low ionic strength was investigated, as were their effects on the morphology of collagen fibrils and the speed of fibrillogenesis. Considerably more biglycan than decorin was bound by all three collagen types. Collagen II bound significantly more SLRPs in fibrils than collagen I and III. Decorin and biglycan decreased the proportion of collagen molecules of all three collagen types incorporated into fibrils in similar fashion. Biglycan affected neither fibril diameter nor the speed of fibrillogenesis. Decorin reduced the fibril diameter of all three collagen types. The differences in SLRP-binding ability between collagen types could be of significance when selecting collagen type and/or SLRPs as scaffold materials for tissue engineering or implant coatings.
authors.affiliation: Institute of Material Science, Max Bergmann Center of Biomaterials, Technische Universität Dresden, 01069 Dresden, Germany. Timothy.Douglas@mailbox.tu.dresden.de
authors.forename: Timothy
authors.initials: T
authors.lastname: Douglas
authors.forename: Sascha
authors.initials: S
authors.lastname: Heinemann
authors.forename: Susanne
authors.initials: S
authors.lastname: Bierbaum
authors.forename: Dieter
authors.initials: D
authors.lastname: Scharnweber
authors.forename: Hartmut
authors.initials: H
authors.lastname: Worch
mesh_terms: D000818:Animals; D058578:Biglycan; D002417:Cattle; D020099:Coated Materials, Biocompatible / Q000737:chemistry; D024042:Collagen Type I / Q000737:chemistry*; D024043:Collagen Type II / Q000737:chemistry*; D024061:Collagen Type III / Q000737:chemistry*; D058575:Decorin; D005109:Extracellular Matrix / Q000737:chemistry; D016326:Extracellular Matrix Proteins / Q000737:chemistry*; D006801:Humans; D016348:Osseointegration; D011509:Proteoglycans / Q000737:chemistry*; D023822:Tissue Engineering / Q000379:methods
chemical_list: C546884:BGN protein, human; D058578:Biglycan; D020099:Coated Materials, Biocompatible; D024042:Collagen Type I; D024043:Collagen Type II; D024061:Collagen Type III; C546878:DCN protein, human; D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans