The effects of recombinant vitronectin fragments on the human osteosarcoma cell line behavior

Abstract

Vitronectin (VN) regulates various cellular responses, such as cell adhesion, spreading, and migration through ligand-cell surface receptor in vascular epithelial cells. In this study, three recombinant vitronectin fragments were cloned and expressed as soluble fusion individual proteins, and their biological function was analyzed. Among these, recombinant vitronectin fragment I (rVN-FI

amino acids 1-130) protein promoted HOS cell adhesion, spreading, and migration compared to recombinant vitronectin fragment II (rVN-FII

amino acids 131-303) protein and recombinant vitronectin fragment III (rVN-FIII

amino acids 304-459) protein. Moreover, function-blocking inhibition assay using monoclonal antibody against integrin subunits revealed that αV integrin subunit played key a role in HOS cell adhesion, and αVβ3 and αVβ5 integrins acted as receptor of rVN-FI protein. rVN-FI-derived synthetic peptides containing Arg-Gly-Asp (RGD) motif, P6 (AECKPQVTRGDV) and P7 (PQVTRGDVFTMP) completely blocked the adhesion of HOS cell to VN. These results indicate that rVN-FI protein showed biological functions on osteoblast-like HOS cells. Thus, rVN-FI protein of human vitronectin may have potential application on bone tissue regeneration-related tissue engineering.