{"refrec":{"BRefID":234604,"RR":"<b>Wu, L.; Yang, X.; Duan, X.; Cui, L.; Li, G.</b> (2014). Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway. <i>NPG Scientific Reports 4(4505)</i>: 7 pp. <a href=\"http://dx.doi.org/10.1038/srep04505\" target=\"_blank\">http://dx.doi.org/10.1038/srep04505</a>","BEntID":226288,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>NPG Scientific Reports 4(4505)</i>: 7 pp. <a href=\"http://dx.doi.org/10.1038/srep04505\" target=\"_blank\">http://dx.doi.org/10.1038/srep04505</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Wu, L.; Yang, X.; Duan, X.; Cui, L.; Li, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Wu, L. <i>et al.</i>","Englishabstract":"Lectins are widely existed in marine bioresources, and some purified marine lectins were found toxic to cancer cells. In this report, genes encoding Dicentrarchus labrax fucose-binding lectin (DlFBL) and Strongylocentrotus purpuratus rhamnose-binding lectin (SpRBL) were inserted into an adenovirus vector to form Ad.FLAG-DlFBL and Ad.FLAG-SpRBL, which elicited significant in vitro suppressive effect on a variety of cancer cells. Anti-apoptosis factors Bcl-2 and XIAP were determined to be downregulated by Ad.FLAG-DlFBL and Ad.FLAG-SpRBL. Subcellular localization studies showed that DlFBL but not SpRBL widely distributed in membrane systems. Both DlFBL and SpRBL were shown associated with protein arginine methyltransferase 5 (PRMT5), and PRMT5-E2F-1 pathway was suggested to be responsible for the DlFBL and SpRBL induced apoptosis. Further investigations revealed that PRMT5 acted as a common binding target for various exogenous lectin and non-lectin proteins, suggesting a role of PRMT5 as a barrier for foreign gene invasion. 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