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Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway
Wu, L.; Yang, X.; Duan, X.; Cui, L.; Li, G. (2014). Exogenous expression of marine lectins DlFBL and SpRBL induces cancer cell apoptosis possibly through PRMT5-E2F-1 pathway. NPG Scientific Reports 4(4505): 7 pp. hdl.handle.net/10.1038/srep04505
In: Scientific Reports (Nature Publishing Group). Nature Publishing Group: London. ISSN 2045-2322, more
Peer reviewed article  

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Keywords
    Biological resources; Lectins; Pharmaceutical products; Dicentrarchus labrax (Linnaeus, 1758) [WoRMS]; Strongylocentrotus purpuratus (Stimpson, 1857) [WoRMS]; Marine

Authors  Top 
  • Wu, L.
  • Yang, X.
  • Duan, X.
  • Cui, L.
  • Li, G.

Abstract
    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. The cellular response to exogenous lectins may provide insights into a novel way for cancer gene therapy.

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