Interferon (IFN) regulates immune responses and antitumor activity. Arginine–glycine–aspartic acid (RGD) peptides can specifically bind to integrin &agr;v&bgr;3, a transmembrane receptor that is highly expressed on the surface of various… Click to show full abstract
Interferon (IFN) regulates immune responses and antitumor activity. Arginine–glycine–aspartic acid (RGD) peptides can specifically bind to integrin &agr;v&bgr;3, a transmembrane receptor that is highly expressed on the surface of various cancer cells. In this study, we expressed recombinant RGD-IFN-&agr;2a-core fusion proteins and assessed their antitumor activity in vitro. Two RGD-IFN-&agr;2a-core fusion proteins and a negative control protein were expressed in vitro. These two RGD-IFN-&agr;2a-core fusion proteins could bind the tumor cell surface specifically and did not bind to normal cells. RGD-IFN-&agr;2a-core fusion protein treatment of tumor cells significantly reduced cell viability and induced apoptosis in a dose-dependent manner. At the ‘mRNA’ level, both proteins could upregulate CASP3 expression. These data indicate that both laboratory-engineered RGD-IFN-&agr;2a-core fusion proteins could bind the surface of tumor cells and induce apoptosis in vitro. Further studies will investigate the in-vivo antitumor activities of the RGD-IFN-&agr;2a-core fusion proteins.
               
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