Sustained mitogenic effect on K562 human chronic myelogenous leukemia cells by dietary lectin, jacalin
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Dietary lectins have been shown to affect the proliferation of human cancer cell lines. The anti-proliferative effects of lectins from varied sources have been extensively studied and in some cases, the underlying mechanism has been explored. Except for peanut agglutinin (PNA), the mitogenic effects of no other lectins have been studied in detail. In the present study, we have shown that jacalin, lectin purified from jackfruit (Artocarpus integrifolia) seeds act as a mitogen for K562, the Bcr-Abl expressing erythroleukemia cell line (K562) and the effect was found to be dose dependent. K562 cells remained in the proliferative state for a longer period even after the withdrawal of jacalin stimulation, thus jacalin was found to induce sustained mitogenic effect on K562 cells. Further, conditioned media from K562 cells treated with jacalin were observed to have the similar mitogenic effect even in the presence of galactose. Importantly, galactose which is a known ligand for jacalin will interact with functionally active jacalin present in the conditioned media and neutralise its effect. In addition, jacalin treatment also resulted in increased mRNA expression levels of pro-inflammatory cytokines including IL-1β, IL-6 and IFN-γ. Our results indicate that jacalin induces secretion of soluble molecules, which maybe responsible for this observed increased proliferation of K562 cells.
KeywordsLectins Jacalin Cell proliferation K562 erythroleukemia cells Thomsen-Friendenreich disaccharide Pro inflammatory cytokines
The authors thank Prof. JAK Tareen for setting up the School of Life Sciences at BSAU, Prof. S. Hemalatha for her constant support and Ms.M.K. Saranya for technical assistance. L.V. is recipient of a junior research fellowship from B. S. Abdur Rahman University, K.A.K, N.A. and S.J. are Assistant Professors (Senior Grade) at School of Life Sciences, B. S. Abdur Rahman University. Financial assistance was provided by B. S. Abdur Rahman University.
Compliance with ethical standards
Conflicts of interest
The authors declare that they have no conflicts of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
- 3.Pusztai A.: Plant Lectins, Chemistry and Pharmacology of Natural Products Series. Cambridge University Press, Cambridge (1991)Google Scholar
- 8.Singh R., Subramanian S., Rhodes J.M., Campbell B.J.: Peanut lectin stimulates proliferation of colon cancer cells by interaction with glycosylated CD44v6 isoforms and consequential activation of c-Met and MAPK: functional implications for disease-associated glycosylation changes. Glycobiology. 16, 594–601 (2006)CrossRefPubMedGoogle Scholar
- 13.Zhao Q., Duckworth C.A., Wang W., Guo X., Barrow H., Pritchard D.M., Rhodes J.M., Yu L.G.: 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. 35, 2815–2821 (2014)CrossRefPubMedGoogle Scholar
- 19.Yu L.G., Andrews N., Weldon M., Gerasimenko O.V., Campbell B.J., Singh R., Grierson I., Petersen O.H., Rhodes J.M.: An Nterminal truncated form of Orp150 is a cytoplasmic ligand for the anti-proliferative mushroom Agaricus bisporus lectin and is required for nuclear localization sequence-dependent nuclearprotein import. J. Biol. Chem. 277, 24538–24545 (2002)CrossRefPubMedGoogle Scholar
- 21.Yu L.G., Fernig D.G., White M.R., Spiller D.G., Appleton P., Evans R.C., Grierson I., Smith J.A., Davies H., Gerasimenko O.V., Petersen O.H., Milton J.D., Rhodes J.M.: Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import. J. Biol. Chem. 274, 4890–4899 (1999)CrossRefPubMedGoogle Scholar
- 25.Amarante-Mendes G.P., Naekyung Kim C., Liu L., Huang Y., Perkins C.L., Green D.R., Bhalla K.: Bcr-Abl exerts its antiapoptotic, effect against diverse apoptotic stimuli through blockage of mitochondrial release of cytochrome C and activation of caspase-3. Blood. 91, 1700–1705 (1998)PubMedGoogle Scholar
- 36.Campbell B.J., Finnie I.A., Hounsell E.F., Rhodes J.M.: Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin. J. Clin. Invest. 95, 571–576 (1995)CrossRefPubMedPubMedCentralGoogle Scholar
- 37.Inamdar S.R., Savanur M.A., Eligar S.M., Chachadi V.B., Nagre N.N., Chen C., Barclaays M., Ingle A., Mahajan P., Borges A., Shastry P., Kalraiya R.D., Swamy B.M., Rhodes J.M., Yu L.G.: The TF-antigen binding lectin from Sclerotiumrolfsii inhibits growth of human colon cancer cells by inducing apoptosis in vitro and suppresses tumor growth in vivo. Glycobiology. 22, 1227–1235 (2012)CrossRefPubMedGoogle Scholar
- 39.Fadeev R.S., Solovieva M.E., Slyadovskiy D.A., Zkharov S.J., Fadeeva I.S., Senotov A.S., Dolgikh N.V., Golenkov A.K., Akatov V.S.: Cell aggregation increases drug resistance of acute myeloid leukemia cells. Biol. Membr.: Zh. Membr. Klet. Biol. 32, 125–132 (2015)Google Scholar
- 48.Higuchi M., Suga M., Iwai K.: Participation of lectin in biological effects of raw winged bean seeds on rats. Agric. Biol. Chem. 47, 1879–1886 (1983)Google Scholar