AI Article Synopsis

  • Lectins are proteins that can target specific cancer cells by binding to their unique surface sugars, with BPL2 showing the most promise as a potential anticancer agent out of three tested types (BPL1, BPL2, and BPL3).
  • BPL2 significantly decreases the survival of lung cancer cells while having minimal effect on normal cells, with a notable IC value of 50 μg/mL after 24 hours.
  • Additionally, BPL2 inhibits cancer cell migration and invasion, works better in combination with gefitinib, and reduces the expression of genes related to cancer progression, indicating its strong potential for cancer treatment development.

Article Abstract

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 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 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9788543PMC
http://dx.doi.org/10.3390/md20120776DOI Listing

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