References
- Ghosh, S. ‘Sialic Acid and Biology of Life: An Introduction’, Sialic Acids and Sialoglycoconjugates in the Biology of Life, Health and Disease 2020, pp. 1–61.
- Varki, A. ‘Biological Roles of Glycans’, Glycobiology, vol. 27, 2017, pp. 3–49.
- Li, Y and Chen, X. ‘Sialic Acid Metabolism and Sialyltransferases: Natural Functions and Applications’, Applied Microbiology and Biotechnology; vol. 94, no. 4, 2012, pp. 887–905.
- Zhou, X, Yang, G, Guan, F. ‘Biological Functions and Analytical Strategies of Sialic Acids in Tumor’, Cells, 9, 2020, p. 273.
- Zhang, Z, Wuhrer, M and Holst, S. ‘Serum Sialylation Changes in Cancer’ Glycoconjugate Journal, vol. 35, 2018, pp. 139–160.
- Rodrigues, E and Macauley, MS. ‘Hypersialylation in cancer: Modulation of Inflammation and Therapeutic Opportunities’, Cancers, vol. 10,, no. 6, 2018, p. 207.
- Büll, C, Stoel, MA, Den Brok, MH and Adema, GJ. ‘Sialic Acids Sweeten a Tumor’s Life’, Cancer Res, vol. 74, no. 12, 2014, pp. 3,199–3,204.
- Teoh, ST, Ogrodzinski, MP, Ross, C, Hunter, KW, Lunt, SY. ‘Sialic Acid Metabolism: A Key Player in Breast Cancer Metastasis Revealed by Metabolomics’, Front. Oncol, vol. 8, 2018, p 174.
- Ugorski, M, Laskowska, A. Sialyl, Lewis a, ‘A Tumor-Associated Carbohydrate Antigen In-Volved in Adhesion and Metastatic Potential of Cancer Cells. Acta Biochemica Plonica’, vol. 49, no 2, 2002 pp. 303–311.
- Seales, EC, Jurado, GA, Singhal, A, Bellis, SL. ‘Ras Oncogene Directs Expression of a Differentially Sialylated, Functionally Altered β1 Integrin’, Oncogene, vol. 22, no. 46, 2003, pp. pp. 7,137–7,145.
- Sakuma, K, Aoki, M, Kannagi, R. ‘Transcription Factors C-Myc and CDX2 Mediate E-Selectin Ligand Expression in Colon Cancer Cells Undergoing EGF/Bfgf-Induced Epithelial-Mesenchymal Transition’, Proc. Natl. Acad. Sci. U.S.A, vol. 109, no. 20, pp., pp. 7,776–7,781.
- Almaraz, RT, Tian, Y, Bhattarcharya, R, et al. ‘Metabolic Flux Increases Glycoprotein Sialylation: Implications for Cell Adhesion and Cancer Metastasis’, Mol. Cell. Proteomics, vol. 11, no. 7, 2012, M112.017558.
- Miyagi, T, Takahashi, K, Hata, K, Shiozaki, K, Yamaguchi, K. ‘Sialidase Significance for Cancer Progression’, Glycoconj. J, vol. 29, 2012, pp. 567–577.
- Büll, C, den Brok, MH, Adema, GJ. ‘Sweet Escape: Sialic Acids in Tumor Immune Evasion’, Biochim. Biophys. Acta, vol 1,846, no. 1, 2014, pp. 238–246.
- Varki, A, Gagneux, P. ‘Multifarious Roles of Sialic Acids in Immunity’,. Ann. N. Y. Acad. Sci, vol. 1253, no. 1., 2012 pp. 16–36.
- Ferreira, VP, Pangburn, MK, Cortés, C. ‘Complement Control Protein Factor H: The Good, the Bad, and the Inadequate’ Molecular Immunology, vol. 47, no. 13, pp. 2,187–2,197.
- Gancz, D, Fishelson, Z. ‘Cancer Resistance to Complement-Dependent Cytotoxicity (CDC): Problem-Oriented Research and Development’, Molecular Immunology, vol. 46, no. 14, 2009, pp. 2,794–2,800.
- Pio, R, Ajona, D, Lambris, JD. ‘Complement Inhibition in Cancer Therapy’, Seminars in Immunology, vol. 25, no. 1, pp. 54–64.
- Cheng, M, Chen, Y, Xiao, W, Sun, R, Tian, Z. ‘NK Cell-Based Immunotherapy for Malignant Diseases, Cellular and Molecular Immunology, vol. 10,, no. 3, 2013pp. 230–252.
- Cohen, M. et al., ‘’Sialylation of 3-Methylcholanthrene–Induced Fibrosarcoma Determines Antitumor Immune Responses during Immunoediting’, J. Immunol, vol. 185, no. 10, 2010, pp. 5,869–5,878.
- Jandus, C. et al. ‘Interactions between Siglec-7/9 receptors and ligands influence NK cell-dependent tumor immunosurveillance’, J. Clin. Invest, vol. 124, no. 4, 2014, \ pp. 1,810–1,820.
- Daly, J, Carlsten, M, O’Dwyer, M. ‘Sugar Free: Novel Immunotherapeutic Approaches Targeting Siglecs and Sialic Acids to Enhance Natural Killer Cell Cytotoxicity Against Cancer’, Front. Immunol, vol. 10, 2019, p. 1,047.
- Park, JE. et al. ‘Fine Specificity of Natural Killer T Cells Against GD3 Ganglioside and Identification of GM3 As an Inhibitory Natural Killer T-Cell Ligand’, Immunology, vol. 123, no. 1, 2008, pp. 145–155.
- Wondimu, A, Liu, Y, Ma JS, Radoja S, Ladisch S. ‘Ganglioside Inhibition of CD8 + T Cell Cytotoxicity: Interference with Lytic Granule Trafficking and Exocytosis’, J. Immunol, vol. 189, no. 7, 2012, pp. 3,521–3,527.
- Li, F, Ding, J. ‘Sialylation Is Involved in Cell Fate Decision During Development, Reprogramming and Cancer Progression’, Protein and Cell, vol. 10, no. 8, 2018, pp 550–565.
- Asano, K. et al. ‘CD169-Positive Macrophages Dominate Antitumor Immunity by Crosspresenting Dead Cell-Associated Antigens’, Immunity, vol. 34, no. 1, 2011; pp. 85–95.
- Jales, A. et al., ‘Ganglioside-Exposed Dendritic Cells Inhibit T-Cell Effector Function by Promoting Regulatory Cell Activity’, Immunology, vol. 132, no. 1, 2011, pp. 134–143.
- Munkley, J, Scott, E., ‘Targeting Aberrant Sialylation to Treat Cancer’, Medicines, vol. 6, no. 4, 2019 p. 102.
- Shen, L. et al., ‘Enhanced Expression of α2,3-Linked Sialic Acids Promotes Gastric Cancer Cell Metastasis and Correlates with Poor Prognosis’, Int. J. Oncol, vol. 50, no. 4, 2017 pp. 1,201–1,210.
- Van Slambrouck, S. et al., ‘Carbohydrate-to-Carbohydrate Interactions Between α2,3-Linked Sialic Acids on α2 Integrin Subunits and Asialo-GM1 Underlie the Bone Metastatic Behaviour of LNCAP-Derivative C4-2B Prostate Cancer Cells’, Biosci. Rep, vol. 34, no. 5, 2014 pp. 546–557.
- Yuan, Q. et al., ‘Modification of α2,6-Sialylation Mediates the Invasiveness and Tumorigenicity of Non-Small Cell Lung Cancer Cells In Vitro and In Vivo Via Notch1/Hes1/MMPs Pathway’, Int. J. Cancer, vol. 143, no. 9, 2018, pp. 1–27.
- Lu J., et al., ‘β-Galactoside α2,6-Sialyltranferase 1 Promotes Transforming Growth Factor-β-Mediated Epithelial-Mesenchymal Transition’, J. Biol. Chem, vol. 289, no. 50, 2014, pp. 34,627–34,641.
- Zhou, X. et al., ‘Sialidase NEU1 Suppresses Progression of Human Bladder Cancer Cells by Inhibiting Fibronectin-Integrin α5β1 Interaction and Akt Signaling Pathway’, Cell Commun. Signal, vol. 18, no. 1, 2020, p. 44.
- Yamanami, H. et al., ‘Down-Regulation of Sialidase NEU4 May Contribute to Invasive Properties of Human Colon Cancers’, Cancer Sci, vol. 98, no. 3, 2007, pp. 299–307.
- Roncati, L, Barbolini, G, Gatti, AM, Pusiol, T, Piscioli, F, Maiorana, A., ‘The Uncontrolled Sialylation Is Related to Chemoresistant Metastatic Breast Cancer’, Pathol. Oncol. Res., vol. 22, no. 4, 2016, pp. 869–873.
- Yen HY. et al. ‘Effect of sialylation on EGFR phosphorylation and resistance to tyrosine kinase inhibition’ Proc. Natl. Acad. Sci. U. S. A., vol. 112, no. 22, 2015, pp. 6,955–6,960.
- Li, Y, Luo, S, Dong, W, Song, X, Zhou, H, Zhao, L, Jia, L, ‘Alpha-2, 3-Sialyltransferases Regulate the Multidrug Resistance of Chronic Myeloid Leukemia Through miR-4701-5p Targeting ST3GAL1’, Lab. Investig, vol. 96, no. 7, 2016, pp. 731–740.
- Britain, CM, Holdbrooks, AT, Anderson, JC, Willey, C.D., and Bellis, S.L., ‘Sialylation of EGFR by the ST6Gal-I Sialyltransferase Promotes EGFR Activation and Resistance to Gefitinib-Mediated Cell Death’, J. Ovarian Res, vol. 11, no. 12, p.12.
- Büll, C. et al., ‘Targeting Aberrant Sialylation in Cancer Cells Using a Fluorinated Sialic Acid Analog Impairs Adhesion, Migration, and In Vivo Tumor Growth’, Mol. Cancer Ther, vol. 12, no. 10, 2013, pp.1,935–1,946.
- Sharma, P, Allison, JP, ‘Immune Checkpoint Targeting in Cancer Therapy: Toward Combination Strategies with Curative Potential’, Cell, vol. 161, no. 2, 2015, pp. 205–214.
- King, T, Posey, AD, ‘Co-Expression of an Engineered Cell-Surface Sialidase by CART Cells Improves Anti-Cancer Activity of NK Cells in Solid Tumors’, Cytotherapy, vol. 21, no. 5, 2019, p. S27.
- Dusoswa, SA. et al., ‘Glycan Modification of Glioblastoma-Derived Extracellular Vesicles Enhances Receptor-Mediated Targeting of Dendritic Cells’, J. Extracell. Vesicles, vol. 8, no. 1, 2019, p. 1,648,995.
- Wang J., et al., ‘Siglec-15 as an Immune Suppressor and Potential Target for Normalization Cancer Immunotherapy’, Nat. Med, vol. 25, no. 4, 2019, pp. 656–666.