Investigation of TF-binding lectins from dietary sources and SRL on proliferation and cell cycle progression in human colon HT29 and SW620 cells

References

• Varki A: Biological roles of oligosaccharides: All of the theories are correct. Glycobiology 3, 97–130, 1993.
   PubMed Web of Science ®Google Scholar
• Christiansen MN, Chik J, Lee L, Anugraham M, Abrahams JL, et al.: Cell surface protein glycosylation in cancer. Proteomics 14, 525–546, 2014.
   PubMed Web of Science ®Google Scholar
• De Mejía EG and Prisecaru VI: Lectins as bioactive plant proteins: A potential in cancer treatment. Critical Rev Food Sci Nutr 45, 425–445, 2005.
   PubMed Web of Science ®Google Scholar
• Ryder SD, Smith JA, and Rhodes JM: Peanut lectin: A mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells. J Natl Cancer Inst 84, 1410–1416, 1992.
   PubMedGoogle Scholar
• Ryder SD, Parker N, Ecclestone D, Haqqani MT, and Rhodes JM: Peanut lectin stimulates proliferation in colonic explants from patients with inflammatory bowel disease and colon polyps. Gastroenterology 106, 117–124, 1994.
   PubMed Web of Science ®Google Scholar
• Liener IE, Sharon N, and Goldstein IJ: The Lectins: Properties, Functions, and Applications in Biology and Medicine. New York: Academic Press, 1986.
   Google Scholar
• Carraway KL and Carraway CA: Membrane-cytoskeleton interactions in animal cells. Biochim Biophys Acta 988, 147–171, 1989.
   PubMed Web of Science ®Google Scholar
• Hadden JW: Transmembrane signals in the activation of T-lymphocytes by lectin mitogens. Mol Immunol 25, 1105–1112, 1988.
   PubMed Web of Science ®Google Scholar
• Sharon N:I: Mitogens in immunmobiology (Oppenheim and rosenstreich eds). New York: Academic Press, 1976, pp. 31–41.
   Google Scholar
• Yu LG, Milton JD, Fernig DG, and Rhodes JM: Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins. J Cell Physiol 186, 282–287, 2001. doi:10.1002/1097-4652(200102)186:2 < 282::AID-JCP1028 > 3.0.CO;2-2
   PubMed Web of Science ®Google Scholar
• Yu LG, Fernig DG, Smith JA, Milton JD, and Rhodes JM: Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin. Cancer Res 53, 4627–4632, 1993.
   PubMed Web of Science ®Google Scholar
• Singh R, Subramanian S, Rhodes JM, and Campbell BJ: 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.
   PubMed Web of Science ®Google Scholar
• Yu LG, Fernig DG, White MR, Spiller DG, Appleton P, et al.: 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.
   PubMed Web of Science ®Google Scholar
• Yu LG, Andrews N, Weldon M, Gerasimenko OV, Campbell BJ, et al.: An N-terminal truncated form of Orp150 is a cytoplasmic ligand for the anti-proliferative mushroom Agaricus bisporus lectin and is required for nuclear localization sequence-dependent nuclear protein import. J Biol Chem 277, 24538–24545, 2002. doi:10.1074/jbc.M203550200.
   PubMed Web of Science ®Google Scholar
• Yu LG, Packman LC, Weldon M, Hamlett J, and Rhodes JM: Protein phosphatase 2A, a negative regulator of the ERK signaling pathway, is activated by tyrosine phosphorylation of putative HLA class II-associated protein I (PHAPI)/pp32 in response to the antiproliferative lectin, jacalin. J Biol Chem 279, 41377–41383, 2004.
   PubMed Web of Science ®Google Scholar
• Inamdar SR, Savanur MA, Eligar SM, Chachadi VB, Nagre NN, et al.: The TF-antigen binding lectin from Sclerotium rolfsii inhibits growth of human colon cancer cells by inducing apoptosis in vitro and suppresses tumor growth in vivo. Glycobiology 22, 1227–1235, 2012.
   PubMed Web of Science ®Google Scholar
• Eligar SM, Pujari R, Savanur MA, Nagre NN, Barkeer S, et al.: Rhizoctonia bataticola lectin (RBL) induces apoptosis in human ovarian cancer PA-1 cells and suppresses tumor growth in vivo. J Glycobiol S1, 2013.
   Google Scholar
• Pujari R, Eligar SM, Kumar N, Barkeer S, Reddy V, et al.: Rhizoctonia bataticola lectin (RBL) induces caspase-8-mediated apoptosis in human T-cell leukemia cell lines but not in normal CD3 and CD34 positive cells. PLoS One 8, e79311, 2013.
   PubMed Web of Science ®Google Scholar
• Hegde P, Jagadeesh N, Swamy BM, and Inamdar SR: Efficacy studies of Sclerotium rolfsii lectin on breast cancer using NOD SCID mice model. Chem Biol Drug Design, 2018. doi:10.1111/cbdd.13314.
   PubMed Web of Science ®Google Scholar
• Swamy BM, Hedge GV, and Rs and Inamdar Sr N: T-antigen binding lectin from the phytopathogenic fungus Sclerotium rolfsii. Lect Biol Biochem 15, 2001.
   Google Scholar
• Yu LG: The oncofetal Thomsen-Friedenreich carbohydrate antigen in cancer progression. Glycoconj J 24, 411–420, 2007.
   PubMed Web of Science ®Google Scholar
• Zhao Q, Guo X, Nash GB, Stone PC, Hilkens J, et al.: Circulating galectin-3 promotes metastasis by modifying MUC1 localization on cancer cell surface. Cancer Res 69, 6799–6806, 2009.
   PubMed Web of Science ®Google Scholar
• Rhodes JM, Campbell BJ, and Yu LG: Lectin–epithelial interactions in the human colon. Biochm Soc Trans 36, 1482–1486, 2008. doi:10.1042/BST0361482.
   PubMed Web of Science ®Google Scholar
• Chen Y, Jain RK, Chandrasekaran EV, and Matta KL: Use of sialylated or sulfated derivatives and acrylamide copolymers of Gal beta 1,3GalNAc alpha- and GalNAc alpha- to determine the specificities of blood group T- and Tn-specific lectins and the copolymers to measure anti-T and anti-Tn antibody levels in cancer patients. Glycoconj J 12, 55–62, 1995.
   PubMed Web of Science ®Google Scholar
• Rinderle SJ, Goldstein IJ, Matta KL, and Ratcliffe RM: Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T- (or cryptic T)-antigen. J Biol Chem 264, 16123–16131, 1989.
   PubMed Web of Science ®Google Scholar
• Ahmed H and Chatterjee BP: Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin. J Biol Chem 264, 9365–9372, 1989.
   PubMed Web of Science ®Google Scholar
• Chachadi VB, Inamdar SR, Yu LG, Rhodes JM, and Swamy BM: Exquisite binding specificity of Sclerotium rolfsii lectin toward TF-related O-linked mucin-type glycans. Glycoconj J 28, 49–56, 2011. doi:10.1007/s10719-011-9323-8.
   PubMed Web of Science ®Google Scholar
• Zhao C, Sun H, Tong X, and Qi Y: An antitumour lectin from the edible mushroom Agrocybe aegerita. Biochem J 374, 321–327, 2003. doi:10.1042/BJ20030300.
   PubMed Web of Science ®Google Scholar
• Lam SK and Ng TB: Apoptosis of human breast cancer cells induced by hemagglutinin from Phaseolus vulgaris cv Legumi secchi. Food Chem 138, 595–602, 2011.
   Web of Science ®Google Scholar
• Yan Q, Li Y, Jiang Z, Sun Y, Zhu L, et al.: Antiproliferation and apoptosis of human tumor cell lines by a lectin (AMML) of Astragalus mongholicus. Phytomedicine 16, 586–593, 2009. doi:10.1016/j.phymed.2008.12.024.
   PubMed Web of Science ®Google Scholar
• Eligar SM, Pujari R, Swamy BM, Shastry P, and Inamdar SR: Sclerotium rolfsii lectin inhibits proliferation and induces apoptosis in human ovarian cancer cell line PA-1. Cell Prolif 45, 397–403, 2012. doi:10.1111/j.1365-2184.2012.00831.x.
   PubMed Web of Science ®Google Scholar
• Barkeer S, Guha N, Hothpet V, Saligrama Adavigowda D, Hegde P, et al.: Molecular mechanism of anticancer effect of Sclerotium rolfsii lectin in HT29 cells involves differential expression of genes associated with multiple signalling pathways: A microarray analysis. Glycobiology 25, 1375–1391, 2015. doi:10.1093/glycob/cwv067.
   PubMed Web of Science ®Google Scholar
• Barkeer S, Gudihal R, Eligar SM, Hegde P, Yu G, et al.: Identification and characterization of Sclerotium rolfsii lectin (SRL) binding proteins from human colon epithelial cancer HT29 cells. Translational Biomedicine 2015.
   Google Scholar
• Matsushime H, Ewen ME, Strom DK, Kato JY, Hanks SK, et al.: Identification and properties of an atypical catalytic subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins. Cell 71, 323–334, 1992.
   PubMed Web of Science ®Google Scholar
• Weinberg RA: The retinoblastoma protein and cell cycle control. Cell 81, 323–330, 1995.
   PubMed Web of Science ®Google Scholar
• Arber N, Hibshoosh H, Moss SF, Sutter T, Zhang Y, et al.: Increased expression of cyclin D1 is an early event in multistage colorectal carcinogenesis. Gastroenterology 110, 669–674, 1996.
   PubMed Web of Science ®Google Scholar
• Arber N, Doki Y, Han EK, Sgambato A, Zhou P, et al.: Antisense to cyclin D1 inhibits the growth and tumorigenicity of human colon cancer cells. Cancer Res 57, 1569–1574, 1997.
   PubMed Web of Science ®Google Scholar
• Mermelshtein A, Gerson A, Walfisch S, Delgado B, Shechter-Maor G, et al.: Expression of D-type cyclins in colon cancer and in cell lines from colon carcinomas. Br J Cancer 93, 338–345, 2005.
   PubMed Web of Science ®Google Scholar
• Hwang HC and Clurman BE: Cyclin E in normal and neoplastic cell cycles. Oncogene 24, 2776–2786, 2005.
   PubMed Web of Science ®Google Scholar
• Donnellan R and Chetty R: Cyclin E in human cancers. Faseb J 24, 773–780, 1999.
   Web of Science ®Google Scholar
• Kawauchi T: Cdk5 regulates multiple cellular events in neural development, function and disease. Develop Growth Differ 56, 335–348, 2014. doi:10.1111/dgd.12138.
   PubMed Web of Science ®Google Scholar
• Robb CM: Inhibition of CDK5 in colorectal cancer. In: Proceedings of the 106th Annual Meeting of the American Association for Cancer Research. 2015; Philadelphia, PA: AACR; 75(15 Suppl): Abstract no 3088. doi:10.1158/1538-7445.AM2015-3088.
   Google Scholar