Antitumor activity of recombinant RGD-IFN-α2a-core fusion protein in vitro. Issue 1 (January 2017)

• Record Type: Journal Article
• Authors: Wen, Zhengwei; Jia, Qunying; Kang, Xiaojuan; Lou, Yongliang; Zou, Lilin; Yang, Jifeng; Gao, Jimin; Han, Liping; Li, Xiang
• Is Part Of: Anti-cancer drugs. Volume 28:Issue 1(2017)
• Publication Date: 2017-01
• Subjects: antitumor activity -- arginine–glycine–aspartic acid peptides -- cancer-targeting therapy -- interferon-α2a; Antineoplastic agents -- Periodicals; Cancer -- Chemotherapy -- Periodicals; Antineoplastic Agents -- therapeutic use -- Periodicals; Drug Therapy -- Periodicals; 616.994061
• DOI: 10.1097/CAD.0000000000000421
• Languages: English
• ISSNs: 0959-4973

Abstract

Abstract : Interferon (IFN) regulates immune responses and antitumor activity. Arginine–glycine–aspartic acid (RGD) peptides can specifically bind to integrin αv β3, a transmembrane receptor that is highly expressed on the surface of various cancer cells. In this study, we expressed recombinant RGD-IFN-α2a-core fusion proteins and assessed their antitumor activity in vitro . Two RGD-IFN-α2a-core fusion proteins and a negative control protein were expressed in vitro . These two RGD-IFN-α2a-core fusion proteins could bind the tumor cell surface specifically and did not bind to normal cells. RGD-IFN-α2a-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-α2a-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-α2a-core fusion proteins.