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Sci Rep
2014 Mar 28;4:4505. doi: 10.1038/srep04505.
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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
.
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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.
Figure 2. Subcellular distribution of DlFBL.Hep3B or BEL-7404 cells were transfected with pEGFP-DlFBL-C1. After 24 h, cells were then stained with DiI (a), Mito Tracker Red Mitochondrion-Selective Probe (b), Golgi-Tracker Red (c), ER-Tracker Red (d), and PI (e), and followed by analysis under a confocal laser scanning microscope. Bars show 20 μm.
Figure 3. Subcellular distribution of SpRBL.Hep3B, BEL-7404, or Huh7 cells were transfected with pEGFP-SpRBL-C1. After 24 h, cells were then stained with DiI (a), ER-Tracker Red (b), Mito Tracker Red Mitochondrion-Selective Probe (c), Golgi-Tracker Red (d), and PI (e), followed by analysis under a confocal laser scanning microscope. Bars show 20 μm for Hep3B and BEL-7404 cells, 50 μm for Huh7 cells.
Figure 4. PRMT5 acts as a common target for various exogenous proteins.(a) Hep3B cells were cotransfected with pEGFP-DlFBL-C1 and pdsRed-PRMT5. (b) Hep3B cells were cotransfected with pEGFP-SpRBL-C1 and pdsRed-PRMT5. (c) Hep3B cells treated with Ad.FLAG, Ad.FLAG-DlFBL, or Ad.FLAG-SpRBL at 20 MOI as well as PBS control for 48 h. Cell lysates were analyzed by Western blot for the levels of E2F-1. GAPDH served as the loading control. Full length blots were shown in Fig. S1. Plasmid pdsRed-PRMT5 was cotransfected into Hep3B cells or BEL-7404 cells with (d) pEGFP-PPA-C1, pEGFP-HddSBL-C1, pEGFP-UPL1-C1, and (e) pEGFP-EqtII (S105-P142)-C1. After 48 h, the co-localization of PPA, HddSBL, UPL1, and EqtII (S105-P142) fragment with PRMT5 was observed under a confocal laser scanning microscope. Bars show 20 μm.
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