Tel 08-30 60 10 info@bionordika.se

Glycobiology plays an important role in oncology. Most cancer researchers have thought about the genome and mutations in their research topic, and glanced through papers of proteomics, but the third major biomolecule group, carbohydrates, is often getting less attention. Glycobiology and its importance in cancer has gotten more attention (1).

Lectins are proteins that can bind to carbohydrates and thus they could be used in interesting cancer related applications like coating of drug molecules, as they are specifically targeting specific cell surface glycans. For instance, wheat germ agglutinin (WGA), was the first lectin that was shown to adhere to cancer cells (2). However, most often the commercially available lectins are originated from plants origin.

Modifications in glycosylation of proteins play a role in several hall marks of cancer: cell signaling, angiogenesis, cell-matrix interactions, immune modulation and metastasis. Lectins can also be used to recognize specific glycan structures in a similar way to antibodies recognize 3D peptide sequences in proteins, HRP- or fluorophore conjugated lectins are a simple way to differentiate cancer tissue or cells from healthy tissue once you know what you are targeting. Agarose bound lectins can be used for assisting in purifying certain cells, antibodies or proteins from a solution.  Many lectins can also bind multiple ligands simultaneously. Vector laboratories has a wide selection of labelled lectins that can be used for this purpose. 2 interesting lectin products for cancer research are highlighted underneath and can be purchased from BioNordika’s webshop.

 

Highlighted lectin products in cancer research:

Wheat Germ Agglutinin (WGA)

WGA is not only binding to sialic acid and N-acetyl-D-glucosamine. Wheat Germ Agglutinin has shown promising effect in killing primary acute myeloid leukemia cells, but leaving healthy cells unharmed. The lectin is also attaching to hepatoma, choriocarcinoma, melanoma and osteosarcoma cell lines. (2-3)

Wheat Germ Agglutinin (WGA), Unconjugated L-1020

Wheat Germ Agglutinin (WGA), Fluorescein FL-1021

Peanut Agglutinin (PNA)

PNA binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates. The sugar chain is detected on the transmembrane mucin protein (MUC-1) on the surface of pre-cancerous and cancerous cells. It is suspected to possibly have pro-metastatic effect. (4-5)

Peanut Agglutinin (PNA), Unconjugated L-1070

Peanut Agglutinin (PNA), Fluorescein FL-1071

 

If you want to learn more about lectins in cancer biomarker detection visit this blog post on Vector laboratories website or contact our product specialists through info@bionordika.se

References:

  • Gupta, Anita. (2020). Emerging applications of lectins in cancer detection and biomedicine. Materials Today: Proceedings. 31. 10.1016/j.matpr.2020.05.810.
  • C. Aub, B. H. Sanford, and M. N. Cote, “Studies on reactivity of tumor and normal cells to a wheat germ agglutinin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 54, no. 2, pp. 396–399, 1965.
  • Wang H, Ng TB, Ooi VE, Liu WK. Effects of lectins with different carbohydrate-binding specificities on hepatoma, choriocarcinoma, melanoma and osteosarcoma cell lines. Int J Biochem Cell Biol. 2000 Mar;32(3):365-72. doi: 10.1016/s1357-2725(99)00130-2. PMID: 10716633.
  • Zhao Q, Duckworth CA, Wang W, Guo X, Barrow H, Pritchard DM, Rhodes JM, Yu LG. Peanut agglutinin appearance in the blood circulation after peanut ingestion mimics the action of endogenous galectin-3 to promote metastasis by interaction with cancer-associated MUC1. Carcinogenesis. 2014 Dec;35(12):2815-21. doi: 10.1093/carcin/bgu216. Epub 2014 Oct 17. PMID: 25326505.
  • Wang W, Sindrewicz-Goral P, Chen C, Duckworth CA, Pritchard DM, Rhodes JM, Yu LG. Appearance of peanut agglutinin in the blood circulation after peanut ingestion promotes endothelial secretion of metastasis-promoting cytokines. 2021 Aug 19;42(8):1079-1088. doi: 10.1093/carcin/bgab059. PMID: 34223877; PMCID: PMC8643467.