Anticancer Activity of Mannose-Specific Lectin, BPL2, from Marine Green Alga Bryopsis plumosa .
Jei Ha LeeSet Byul LeeHeabin KimJae Min ShinMoongeun YoonHye Suck AnJong Won HanPublished in: Marine drugs (2022)
Lectin is a carbohydrate-binding protein that recognizes specific cells by binding to cell-surface polysaccharides. Tumor cells generally show various glycosylation patterns, making them distinguishable from non-cancerous cells. Consequently, lectin has been suggested as a good anticancer agent. Herein, the anticancer activity of Bryopsis plumosa lectins (BPL1, BPL2, and BPL3) was screened and tested against lung cancer cell lines (A549, H460, and H1299). BPL2 showed high anticancer activity compared to BPL1 and BPL3. Cell viability was dependent on BPL2 concentration and incubation time. The IC 50 value for lung cancer cells was 50 μg/mL after 24 h of incubation in BPL2 containing medium; however, BPL2 (50 μg/mL) showed weak toxicity in non-cancerous cells (MRC5). BPL2 affected cancer cell growth while non-cancerous cells were less affected. Further, BPL2 (20 μg/mL) inhibited cancer cell invasion and migration (rates were ˂20%). BPL2 induced the downregulation of epithelial-to-mesenchymal transition-related genes (Zeb1, vimentin, and Twist). Co-treatment with BPL2 and gefitinib (10 μg/mL and 10 μM, respectively) showed a synergistic effect compared with monotherapy. BPL2 or gefitinib monotherapy resulted in approximately 90% and 70% cell viability, respectively, with concomitant treatment showing 40% cell viability. Overall, BPL2 can be considered a good candidate for development into an anticancer agent.
Keyphrases
- induced apoptosis
- cell cycle arrest
- small cell lung cancer
- binding protein
- signaling pathway
- combination therapy
- epithelial mesenchymal transition
- squamous cell carcinoma
- cell surface
- papillary thyroid
- long non coding rna
- open label
- endothelial cells
- pi k akt
- epidermal growth factor receptor
- squamous cell
- diabetic rats
- low density lipoprotein