Abstract
Background: The collagen-binding activity of vitronectin (VN) was found to be enhanced by glycosylation changes in vitro and during liver regeneration after partial hepatectomy. In this study, we propose a possible mechanism by which VN is activated to bind collagen by alteration of its glycosylation. Methods: Interaction between VN and type I collagen was characterized by enzyme-linked immunosorbent assay (ELISA). The effect of pH and glycosylation on the multimerization of VN was studied by analytical ultracentrifugation. Results: Sedimentation velocity analysis indicated that the multimerization of VN was more remarkable at pH 4.5, an optimal pH for collagen binding, than at pH 7.5. Neuraminidase- or N-glycosidase-treated VNs formed multimers larger than that of control VN incubated without an enzyme. By sedimentation equilibrium analysis, the deglycosylated VNs were found to remain in a multimer form at a guanidine–HCl (GdnHCl) concentration at which control VN dissociated into monomers. Conclusions: These results suggest that deglycosylated VN increased the size and stability of the multimer to eventually enhance the collagen-binding activity by a multivalent effect.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
