LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

Antitumor activity of recombinant RGD-IFN-α2a-core fusion protein in vitro

Photo by p1mm1 from unsplash

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.

Keywords: core fusion; rgd ifn; ifn agr

Journal Title: Anti-Cancer Drugs
Year Published: 2017

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.