title: Augmenting the articular cartilage-implant interface: Functionalizing with a collagen adhesion protein.
abstract: The lack of integration between implants and articular cartilage is an unsolved problem that negatively impacts the development of treatments for focal cartilage defects. Many approaches attempt to increase the number of matrix-producing cells that can migrate to the interface, which may help to reinforce the boundary over time but does not address the problems associated with an initially unstable interface. The objective of this study was to develop a bioadhesive implant to create an immediate bond with the extracellular matrix components of articular cartilage. We hypothesized that implant-bound collagen adhesion protein (CNA) would increase the interfacial strength between a poly(vinly alcohol) implant and an articular cartilage immediately after implantation, without preventing cell migration into the implant. By way of a series of in vitro immunohistochemical and mechanical experiments, we demonstrated that (i) free CNA can bind to articular cartilage, (ii) implant-bound CNA can bind to collagen type II and (iii) implants functionalized with CNA result in a fourfold increase in interfacial strength with cartilage relative to untreated implants at day zero. Of note, the interfacial strength significantly decreased after 21 days in culture, which may be an indication that the protein itself has lost its effectiveness. Our data suggest that functionalizing scaffolds with CNA may be a viable approach toward creating an initially stable interface between scaffolds and articular cartilage. Further efforts are required to ensure long-term interface stability.
authors.affiliation: Hospital for Special Surgery, New York, New York, USA.
authors.forename: Aliza A
authors.initials: AA
authors.lastname: Allon
authors.forename: Kenneth W
authors.initials: KW
authors.lastname: Ng
authors.forename: Sommer
authors.initials: S
authors.lastname: Hammoud
authors.forename: Brooke H
authors.initials: BH
authors.lastname: Russell
authors.forename: Casey M
authors.initials: CM
authors.lastname: Jones
authors.forename: Jose J
authors.initials: JJ
authors.lastname: Rivera
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Schwartz
authors.forename: Magnus
authors.initials: M
authors.lastname: Hook
authors.forename: Suzzane A
authors.initials: SA
authors.lastname: Maher
mesh_terms: D018829:Adhesins, Bacterial / Q000494:pharmacology*; D000268:Adhesiveness / Q000187:drug effects; D000818:Animals; D001672:Biocompatible Materials / Q000494:pharmacology; D002358:Cartilage, Articular / Q000187:drug effects* / Q000502:physiology*; D002417:Cattle; D003094:Collagen / Q000378:metabolism; D016650:Fluorescein-5-isothiocyanate / Q000378:metabolism; D006025:Glycosaminoglycans / Q000378:metabolism; D008422:Materials Testing; D008856:Microscopy, Fluorescence; D019736:Prostheses and Implants; D011485:Protein Binding / Q000187:drug effects; D013194:Staining and Labeling; D054457:Tissue Scaffolds
chemical_list: D018829:Adhesins, Bacterial; D001672:Biocompatible Materials; D006025:Glycosaminoglycans; C048165:adhesin, Staphylococcus aureus; D003094:Collagen; D016650:Fluorescein-5-isothiocyanate