CoChat
Sign Up
Cited by 16Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisRNA modifications and cancer

The DOI matches its Crossref record; the references it cites are not checked yet.

Glycosylation in cancer: mechanisms, diagnostic markers, and therapeutic applications

Qusairy, Zahraa, Rada, Miran·2025·Molecular and Cellular Biochemistry
DOI 10.1007/s11010-025-05303-1
Open this paper in CoChat — free account

Abstract

Glycosylation, a key post-translational modification, plays a pivotal role in cancer progression by influencing critical processes such as protein folding, immune modulation, and intercellular signaling. Altered glycosylation patterns are increasingly recognized as fundamental drivers of tumorigenesis, contributing to key cancer hallmarks like enhanced tumor migration, metastasis, and immune evasion. These aberrant glycosylation signatures not only offer insights into cancer biology but also serve as valuable diagnostic markers and potential therapeutic targets across a range of malignancies. This review explores the mechanisms underlying glycosylation alterations in cancer. We discuss the molecular basis of these changes, including genetic mutations, epigenetic regulation, and oncogene-driven shifts in glycosylation pathways. Additionally, we highlight recent advancements in glycomics research, with a focus on how these alterations influence tumor progression, angiogenesis, and the tumor microenvironment. Furthermore, the review considers the clinical implications of glycosylation changes, including their role in resistance to anti-cancer therapies and their potential as biomarkers for personalized treatment strategies. By bridging fundamental glycosylation research with clinical applications, this review underscores the promise of glycosylation as both a diagnostic tool and a therapeutic target in oncology, offering new avenues for improved patient stratification and precision medicine.

Overview

Integrity signals

Registry

Crossref · 10.1007/s11010-025-05303-1

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

The citation lists are queued

They are fetched later and appear here then.

References 245 · Cited by 16

Research works printed but not linked: 236

  1. He M, Zhou X, Wang X (2024) Glycosylation: mechanisms, biological functions and clinical implications. Signal Transduct Target Ther 9:194 · DOI
  2. Varki A et al (2009) Essentials of Glycobiology. Cold Spring Harbor Laboratory Press, NY
  3. Pinho SS, Reis CA (2015) Glycosylation in cancer: mechanisms and clinical implications. Nat Rev Cancer 15:540–555 · DOI
  4. Srivastava S, Ghosh S, Kagan J, Mazurchuk R (2018) Altered glycosylation in cancer: What a difference a sugar makes. Trends Cancer 4:513–514 · DOI
  5. Ju T et al (2013) Tn and sialyl-Tn antigens, aberrant O-glycomics as human disease markers. Proteomics Clin Appl 7:618–631 · DOI
  6. Mereiter S, Balmaña M, Campos D, Gomes J, Reis CA (2019) Glycosylation in the Era of Cancer-Targeted Therapy: Where Are We Heading? Cancer Cell 36:6–1 · DOI
  7. Gupta R, Ponangi R, Indresh KG (2023) Role of glycosylation in breast cancer progression and metastasis: implications for miRNA, EMT and multidrug resistance. Glycobiology 33:545–555 · DOI
  8. Porębska N et al (2021) Galectins as modulators of receptor tyrosine kinases signaling in health and disease. Cytokine Growth Factor Rev 60:89–106 · DOI
  9. Contessa JN, Bhojani MS, Freeze HH, Rehemtulla A, Lawrence TS (2008) Inhibition of N-linked glycosylation disrupts receptor tyrosine kinase signaling in tumor cells. Cancer Res 68:3803–3809 · DOI
  10. Hoffmann M, Hayes MR, Pietruszka J, Elling L (2020) Synthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins. Glycoconj J 37:457–470 · DOI
  11. Matsumoto Y et al (2019) Identification of Tn Antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies. Glycobiology. https://doi.org/10.1093/glycob/cwz095 · DOI
  12. Thomas D, Rathinavel AK, Radhakrishnan P (2021) Altered glycosylation in cancer: A promising target for biomarkers and therapeutics. Biochimica et Biophysica Acta (BBA) – Rev Cancer 1875:18846 · DOI
  13. Li R et al (2025) Glycosylation gene expression profiles enable prognosis prediction for colorectal cancer. Sci Rep 15:798 · DOI
  14. Berois N, Pittini A, Osinaga E (2022) Targeting tumor glycans for cancer therapy: successes, limitations, and perspectives. Cancers (Basel) 14:645 · DOI
  15. Schachner LF et al (2024) Exposing the molecular heterogeneity of glycosylated biotherapeutics. Nat Commun 15:3259 · DOI · Paper page
  16. Jayaprakash NG, Surolia A (2017) Role of glycosylation in nucleating protein folding and stability. Biochemical Journal 474:2333–2347 · DOI
  17. Kölbl AC, Andergassen U, Jeschke U (2015) The role of glycosylation in breast cancer metastasis and cancer control. Front Oncol. https://doi.org/10.3389/fonc.2015.00219 · DOI
  18. Matsumoto Y, Ju T (2023) Aberrant glycosylation as immune therapeutic targets for solid tumors. Cancers (Basel) 15:3536 · DOI
  19. Fernández-Ponce C et al (2021) The role of glycosyltransferases in colorectal cancer. Int J Mol Sci 22:5822 · DOI
  20. Lan Y et al (2016) Serum glycoprotein-derived N- and O-linked glycans as cancer biomarkers. Am J Cancer Res 6:2390–2415
  21. Xu X et al (2024) Altered glycosylation in cancer: molecular functions and therapeutic potential. Cancer Commun 44:1316–1336 · DOI
  22. Pinto D, Parameswaran R (2023) Role of truncated O-GalNAc glycans in cancer progression and metastasis in endocrine cancers. Cancers (Basel) 15:3266 · DOI
  23. Munkley J (2016) The role of Sialyl-Tn in cancer. Int J Mol Sci 17:275 · DOI
  24. Mercanoglu B et al (2024) A comprehensive analysis of Tn and STn antigen expression in esophageal adenocarcinoma. Cancers (Basel) 16:240 · DOI
  25. Pietrobono S, Stecca B (2021) Aberrant sialylation in cancer: biomarker and potential target for therapeutic intervention? Cancers (Basel) 13:2014 · DOI
  26. Li F, Ding J (2019) Sialylation is involved in cell fate decision during development, reprogramming and cancer progression. Protein Cell 10:550–565 · DOI
  27. Munkley J (2022) Aberrant sialylation in cancer: therapeutic opportunities. Cancers (Basel) 14:4248 · DOI
  28. Kudelka, M. R., Ju, T., Heimburg-Molinaro, J. & Cummings, R. D. Simple Sugars to Complex Disease—Mucin-Type O-Glycans in Cancer. in 53–135 (2015). https://doi.org/10.1016/bs.acr.2014.11.002. · DOI
  29. Kawarada Y et al (2000) The role of Sialylated Lewis antigens on hematogeneous metastases of human pancreas carcinoma cell lines in vivo. Pathol Res Pract 196:259–263 · DOI
  30. Mantuano NR, Läubli H (2024) Sialic acid and Siglec receptors in tumor immunity and immunotherapy. Semin Immunol 74–75:101893
  31. Osuka RF et al (2023) The cancer-associated glycosyltransferase GnT-V (MGAT5) recognizes the N-glycan core via residues outside its catalytic pocket. FEBS Lett 597:3102–3113 · DOI
  32. Saito T et al (2002) A secreted Type tof β1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation. J Biol Chem 277:17002–17008 · DOI
  33. Zhan Y et al (2024) N-acetylglucosaminyltransferase V drives colorectal cancer metastasis by facilitating ZO-1 ubiquitination and degradation. Cancer Cell Int 24:366 · DOI
  34. Takahashi N et al (2009) High expression of N-acetylglucosaminyltransferase V in mucinous tumors of the ovary. Oncol Rep. https://doi.org/10.3892/or_00000531 · DOI
  35. Nie H et al (2024) Targeting branched N-glycans and fucosylation sensitizes ovarian tumors to immune checkpoint blockade. Nat Commun 15:2853 · DOI
  36. Wang Y-N, Lee H-H, Hsu JL, Yu D, Hung M-C (2020) The impact of PD-L1 N-linked glycosylation on cancer therapy and clinical diagnosis. J Biomed Sci 27:77 · DOI
  37. Steen PV, den, Rudd, P. M., Dwek, R. A. & Opdenakker, G. (1998) Concepts and Principles of O-Linked Glycosylation. Crit Rev Biochem Mol Biol 33:151–208 · DOI
  38. Gupta R, Leon F, Rauth S, Batra SK, Ponnusamy MP (2020) A systematic review on the implications of O-linked glycan branching and truncating enzymes on cancer progression and metastasis. Cells 9:446 · DOI
  39. Tran DT, Ten Hagen KG (2013) Mucin-type O-glycosylation during development. J Biol Chem 288:6921–6929 · DOI
  40. Zhang Y et al (2022) A sweet warning: mucin-type O-glycans in cancer. Cells 11:3666 · DOI
  41. Bergstrom K et al (2017) Core 1– and 3–derived O-glycans collectively maintain the colonic mucus barrier and protect against spontaneous colitis in mice. Mucosal Immunol 10:91–103 · DOI
  42. Fukuda, M. Roles of mucin-type O-glycans in cell adhesion. Biochimica et Biophysica Acta (BBA) - General Subjects 1573, 394–405 (2002). · DOI
  43. Nath S, Mukherjee P (2014) MUC1: a multifaceted oncoprotein with a key role in cancer progression. Trends Mol Med 20:332–342 · DOI
  44. Tsuboi S (2012) MUC1 carrying core 2 O-glycans functions as a molecular shield against NK cell attack, promoting bladder tumor metastasis. Int J Oncol. https://doi.org/10.3892/ijo.2012.1411 · DOI
  45. Mao W, Zhang H, Wang K, Geng J, Wu J (2024) Research progress of MUC1 in genitourinary cancers. Cell Mol Biol Lett 29:135 · DOI
  46. Scott DA, Drake RR (2019) Glycosylation and its implications in breast cancer. Expert Rev Proteomics 16:665–680 · DOI
  47. Padler-Karavani V (2014) Aiming at the sweet side of cancer: Aberrant glycosylation as possible target for personalized-medicine. Cancer Lett 352:102–112 · DOI
  48. Hugonnet M, Singh P, Haas Q, von Gunten S (2021) The distinct roles of sialyltransferases in cancer biology and onco-immunology. Front Immunol. https://doi.org/10.3389/fimmu.2021.799861 · DOI
  49. Hakomori S (2002) Glycosylation defining cancer malignancy: New wine in an old bottle. Proc Natl Acad Sci 99:10231–10233 · DOI
  50. Wang L et al (2019) α2,6-Sialylation promotes immune escape in hepatocarcinoma cells by regulating T cell functions and CD147/MMP signaling. J Physiol Biochem 75:199–207 · DOI
  51. Dobie C, Skropeta D (2021) Insights into the role of sialylation in cancer progression and metastasis. Br J Cancer 124:76–90 · DOI
  52. Tu L, Banfield DK (2010) Localization of Golgi-resident glycosyltransferases. Cell Mol Life Sci 67:29–41 · DOI
  53. Lairson LL, Henrissat B, Davies GJ, Withers SG (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu Rev Biochem 77:521–555 · DOI
  54. Yagi H, Takagi K, Kato K (2024) Exploring domain architectures of human glycosyltransferases: Highlighting the functional diversity of non-catalytic add-on domains. Biochimica et Biophysica Acta (BBA) - General Subjects 1868:130687 · DOI
  55. Yonekura-Sakakibara K, Hanada K (2011) An evolutionary view of functional diversity in family 1 glycosyltransferases. Plant J 66:182–193 · DOI
  56. Harduin-Lepers A et al (2001) The human sialyltransferase family. Biochimie 83:727–737 · DOI
  57. Li Y, Chen X (2012) Sialic acid metabolism and sialyltransferases: natural functions and applications. Appl Microbiol Biotechnol 94:887–905 · DOI
  58. Angata T, Varki A (2002) Chemical diversity in the sialic acids and related α-keto acids: an evolutionary perspective. Chem Rev 102:439–470 · DOI
  59. Nag S et al (2022) Sialyltransferases and neuraminidases: potential targets for cancer treatment. Diseases 10:114 · DOI
  60. Zhou X, Chi K, Zhang C, Liu Q, Yang G (2023) Sialylation: a cloak for tumors to trick the immune system in the microenvironment. Biology (Basel) 12:832
  61. Britain CM et al (2021) Glycosyltransferase ST6Gal-I promotes the epithelial to mesenchymal transition in pancreatic cancer cells. J Biol Chem 296:100034 · DOI
  62. Shan M, Yang D, Dou H, Zhang L (2019) Fucosylation in cancer biology and its clinical applications. Prog Mol Biol Transl Sci. https://doi.org/10.1016/bs.pmbts.2019.01.002 · DOI
  63. Vasconcelos, A. O., Vieira, L. M., Rocha, C. R. C. & Beltrão, E. I. C. The contribution of fucosyltransferases to cancer biology. Brazilian J Biol 84, (2024). · DOI
  64. Ma M et al (2021) Fucosyltransferase 8 regulation and breast cancer suppression by transcription factor activator protein 2γ. Cancer Sci 112:3190–3204 · DOI
  65. Bastian K, Scott E, Elliott DJ, Munkley J (2021) FUT8 alpha-(1,6)-Fucosyltransferase in cancer. Int J Mol Sci 22:455 · DOI
  66. Lai T-Y et al (2019) Fucosyltransferase 1 and 2 play pivotal roles in breast cancer cells. Cell Death Discov 5:74 · DOI
  67. Hennet T (2002) The galactosyltransferase family. Cell Mol Life Sci 59:1081–1095 · DOI
  68. Rabinovich GA, van Kooyk Y, Cobb BA (2012) Glycobiology of immune responses. Ann N Y Acad Sci 1253:1–15 · DOI
  69. Chen Y et al (2021) Galactosyltransferase B4GALT1 confers chemoresistance in pancreatic ductal adenocarcinomas by upregulating N-linked glycosylation of CDK11p110. Cancer Lett 500:228–243 · DOI
  70. Lee A et al (2011) Liver membrane proteome glycosylation changes in mice bearing an extra-hepatic tumor. Mol Cellular Proteomics. https://doi.org/10.1074/mcp.M900538-MCP200 · DOI
  71. Su Y et al (2025) C1GALT1 high expression enhances the progression of glioblastoma through the EGFR-AKT/ERK cascade. Cell Signal 125:111513
  72. Wu D, Sun L, Chang X, Zhang G (2024) B4GALT5 a sialylation-related genes associated with patient prognosis and immune microenvironment in ovarian cancer and pan-cancer. J Ovarian Res 17:176 · DOI
  73. Echeverri D, Orozco J (2022) β-1,4-Galactosyltransferase-V colorectal cancer biomarker immunosensor with label-free electrochemical detection. Talanta 243:123337 · DOI
  74. Chen W-S, Chang H-Y, Li C-P, Liu JM, Huang T-S (2005) Tumor β-1,4-galactosyltransferase IV overexpression is closely associated with colorectal cancer metastasis and poor prognosis. Clin Cancer Res 11:8615–8622 · DOI
  75. Taniguchi N, Miyoshi E, Ko JH, Ikeda Y, Ihara Y (1999) Implication of N-acetylglucosaminyltransferases III and V in cancer: gene regulation and signaling mechanism. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1455:287–300 · DOI
  76. Takamatsu S et al (2013) N-Acetylglucosaminyltransferase (GnT) assays using fluorescent oligosaccharide acceptor substrates: GnT-III, IV, V, and IX (GnT-Vb). Methods Mol Biol 1022:283–298 · DOI
  77. Link-Lenczowski P et al (2018) The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans. Glycoconj J 35:217–231 · DOI
  78. Dosaka-Akita H et al (2004) Expression of N-acetylglucosaminyltransferase v is associated with prognosis and histology in non-small cell lung cancers. Clin Cancer Res 10:1773–1779 · DOI
  79. Bojarová-Fialová P, Křen V (2007) Enzymatic approaches to O-Glycoside Introduction: Glycosidases. Comprehensive Glycosci. https://doi.org/10.1016/B978-044451967-2/00013-1 · DOI
  80. Bernacki RJ, Niedbala MJ, Korytnyk W (1985) Glycosidases in cancer and invasion. Cancer Metastasis Rev 4:81–101 · DOI
  81. Amin K, Tranchimand S, Benvegnu T, Abdel-Razzak Z, Chamieh H (2021) Glycoside hydrolases and glycosyltransferases from hyperthermophilic archaea: insights on their characteristics and applications in biotechnology. Biomolecules 11:1557 · DOI
  82. Freeze HH, Kranz C (2010) Endoglycosidase and glycoamidase release of N-linked glycans. Curr Protoc Mol Biol. https://doi.org/10.1002/0471142735.im0815s89 · DOI
  83. Chojnowska S et al (2011) Exoglycosidase markers of diseases. Biochem Soc Trans 39:406–409 · DOI
  84. Martin H, Lázaro LR, Gunnlaugsson T, Scanlan EM (2022) Glycosidase activated prodrugs for targeted cancer therapy. Chem Soc Rev 51:9694–9716 · DOI
  85. Läubli H, Borsig L (2019) Altered cell adhesion and glycosylation promote cancer immune suppression and metastasis. Front Immunol. https://doi.org/10.3389/fimmu.2019.02120 · DOI
  86. Lillehoj, E. P., Luzina, I. G. & Atamas, S. P. Mammalian neuraminidases in immune-mediated diseases: mucins and beyond. Front Immunol 13, (2022). · DOI
  87. Aljohani MA, Sasaki H, Sun X-L (2024) Cellular translocation and secretion of sialidases. J Biol Chem 300:107671 · DOI
  88. Toussaint K et al (2022) Neuraminidase-1: a sialidase involved in the development of cancers and metabolic diseases. Cancers (Basel) 14:4868 · DOI
  89. Nath S, Mandal C, Chatterjee U, Mandal C (2018) Association of cytosolic sialidase Neu2 with plasma membrane enhances Fas-mediated apoptosis by impairing PI3K-Akt/mTOR-mediated pathway in pancreatic cancer cells. Cell Death Dis 9:210 · DOI
  90. Miyagi T (2008) Aberrant expression of sialidase and cancer progression. Proc Jpn Acad Ser B Phys Biol Sci 84:407–418 · DOI
  91. Li L, Jia F, Li Y, Peng Y (2024) Design strategies and biological applications of β-galactosidase fluorescent sensor in ovarian cancer research and beyond. RSC Adv 14:3010–3023 · DOI
  92. Kubo H et al (2021) β-Galactosidase is a target enzyme for detecting peritoneal metastasis of gastric cancer. Sci Rep 11:10664 · DOI
  93. Almammadov T et al (2022) Locked and loaded: β-galactosidase activated photodynamic therapy agent enables selective imaging and targeted treatment of glioblastoma multiforme cancer cells. ACS Appl Bio Mater 5:4284–4293 · DOI
  94. Wu Q et al (2022) Evolving an ultra-sensitive near-infrared β-galactosidase fluorescent probe for breast cancer imaging and surgical resection navigation. ACS Sens 7:3829–3837 · DOI
  95. Zhang Y, Li J, Yin X (2023) High-expression of Galactosidase alpha is correlated with poor prognosis and immune infiltration in low-grade glioma. J Cancer 14:646–656 · DOI
  96. Suzuki T et al (2002) Endo-β-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol. Proc Natl Acad Sci 99:9691–9696 · DOI
  97. Trastoy B et al (2021) GH18 endo-β-N-acetylglucosaminidases use distinct mechanisms to process hybrid-type N-linked glycans. J Biol Chem 297:101011 · DOI
  98. Dall’Olio, F. & Trinchera, M (2017) Epigenetic bases of aberrant glycosylation in cancer. Int J Mol Sci 18:998 · DOI
  99. Stowell SR, Ju T, Cummings RD (2015) Protein glycosylation in cancer. Annu Rev Pathol 10:473–510 · DOI · Paper page
  100. Mizumoto S, Ikegawa S, Sugahara K (2013) Human genetic disorders caused by mutations in genes encoding biosynthetic enzymes for sulfated glycosaminoglycans. J Biol Chem 288:10953–10961 · DOI
  101. Dorsett KA et al (2021) Regulation of ST6GAL1 sialyltransferase expression in cancer cells. Glycobiology 31:530–539 · DOI
  102. Agrawal P et al (2017) A systems biology approach identifies FUT8 as a driver of melanoma metastasis. Cancer Cell 31:804-819.e7 · DOI
  103. Venkitachalam S et al (2016) Biochemical and functional characterization of glycosylation-associated mutational landscapes in colon cancer. Sci Rep 6:23642 · DOI
  104. Häuselmann I, Borsig L (2014) Altered tumor-cell glycosylation promotes metastasis. Front Oncol. https://doi.org/10.3389/fonc.2014.00028 · DOI
  105. Lefeber DJ, Freeze HH, Steet R, Kinoshita T (2022) Congenital Disorders of Glycosylation. Cold Spring Harbor Laboratory Press, NY
  106. Brasil S et al (2022) Systematic review: drug repositioning for congenital disorders of glycosylation (CDG). Int J Mol Sci 23:8725 · DOI
  107. Hollander EE et al (2024) N-glycosylation by Mgat5 imposes a targetable constraint on immune-mediated tumor clearance. JCI Insight. https://doi.org/10.1172/jci.insight.178804 · DOI
  108. Sudhir P-R et al (2012) Label-free quantitative proteomics and N-glycoproteomics analysis of KRAS-activated human bronchial epithelial cells. Mol Cell Proteomics 11:901–915 · DOI
  109. Smith BAH et al (2023) MYC-driven synthesis of Siglec ligands is a glycoimmune checkpoint. Proceed Natl Acad Sci. https://doi.org/10.1073/pnas.2215376120 · DOI
  110. Yu Y, Wang Z, Zheng Q, Li J (2021) GALNT2/14 overexpression correlate with prognosis and methylation: potential therapeutic targets for lung adenocarcinoma. Gene 790:145689
  111. Chugh S et al (2015) Pathobiological implications of mucin glycans in cancer: Sweet poison and novel targets. Biochimica et Biophysica Acta BBA - Reviews on Cancer 1856:211–225 · DOI
  112. Wang Z-Q et al (2014) Role of the polypeptide N-acetylgalactosaminyltransferase 3 in ovarian cancer progression: possible implications in abnormal mucin O-glycosylation. Oncotarget 5:544–560 · DOI
  113. Keita M et al (2013) Global methylation profiling in serous ovarian cancer is indicative for distinct aberrant DNA methylation signatures associated with tumor aggressiveness and disease progression. Gynecol Oncol 128:356–363 · DOI
  114. Hatano K et al (2012) Androgen-regulated transcriptional control of sialyltransferases in prostate cancer cells. PLoS ONE 7:e31234 · DOI
  115. Indellicato R, Trinchera M (2021) Epigenetic regulation of glycosylation in cancer and other diseases. Int J Mol Sci 22:2980 · DOI
  116. Suzuki Y, Yanagisawa M, Ariga T, Yu RK (2011) Histone acetylation-mediated glycosyltransferase gene regulation in mouse brain during development. J Neurochem 116:874–880 · DOI
  117. Rada M et al (2017) Human EHMT2/G9a activates p53 through methylation-independent mechanism. Oncogene 36:922–932 · DOI
  118. Greer EL, Shi Y (2012) Histone methylation: a dynamic mark in health, disease and inheritance. Nat Rev Genet 13:343–357 · DOI · Paper page
  119. Li CH et al (2013) Enhancer of Zeste homolog 2 silences MicroRNA-218 in human pancreatic ductal adenocarcinoma cells by inducing formation of heterochromatin. Gastroenterology 144:1086-1097.e9 · DOI
  120. Duca M, Malagolini N, Dall’Olio, F. (2022) The mutual relationship between glycosylation and non-coding RNAs in cancer and other physio-pathological conditions. Int J Mol Sci 23:15804 · DOI
  121. Dyrskjøt L et al (2009) Genomic profiling of microRNAs in bladder cancer: miR-129 is associated with poor outcome and promotes cell death in vitro. Cancer Res 69:4851–4860 · DOI
  122. Wu H et al (2017) MicroRNA-30e functions as a tumor suppressor in cervical carcinoma cells through targeting GALNT7. Transl Oncol 10:876–885 · DOI
  123. Pedersen ME et al (2013) An epidermal MicroRNA regulates neuronal migration through control of the cellular glycosylation state. Science 1979(341):1404–1408 · DOI · Paper page
  124. Lu Q et al (2016) miR-214 inhibits invasion and migration via downregulating GALNT7 in esophageal squamous cell cancer. Tumor Biology 37:14605–14614 · DOI
  125. Li W, Ma H, Sun J (2014) microRNA-34a/c function as tumor suppressors in Hep-2 laryngeal carcinoma cells and may reduce GALNT7 expression. Mol Med Rep 9:1293–1298 · DOI
  126. Li Y et al (2018) Long non-coding RNA-SNHG7 acts as a target of miR-34a to increase GALNT7 level and regulate PI3K/Akt/mTOR pathway in colorectal cancer progression. J Hematol Oncol 11:89 · DOI
  127. Gaziel-Sovran A et al (2011) miR-30b/30d regulation of GalNAc transferases enhances invasion and immunosuppression during metastasis. Cancer Cell 20:104–118 · DOI
  128. Shan SW et al (2013) Mature MiR-17-5p and passenger miR-17-3p induce hepatocellular carcinoma by targeting PTEN, GalNT7, and vimentin in different signal pathways. J Cell Sci. https://doi.org/10.1242/jcs.122895 · DOI
  129. Brown Chandler K, Costello E, C. & Rahimi, N (2019) Glycosylation in the tumor microenvironment: implications for tumor angiogenesis and metastasis. Cells 8:544 · DOI
  130. Peixoto A, Relvas-Santos M, Azevedo R, Santos LL, Ferreira JA (2019) Protein glycosylation and tumor microenvironment alterations driving cancer hallmarks. Front Oncol. https://doi.org/10.3389/fonc.2019.00380 · DOI
  131. Pinho SS et al (2009) Role of E-cadherin N-glycosylation profile in a mammary tumor model. Biochem Biophys Res Commun 379:1091–1096 · DOI
  132. Mao Y et al (2019) GALNT6 promotes tumorigenicity and metastasis of breast cancer cell via β-catenin/MUC1-C signaling pathway. Int J Biol Sci 15:169–182 · DOI
  133. Venkitachalam S, Guda K (2017) Altered glycosyltransferases in colorectal cancer. Expert Rev Gastroenterol Hepatol 11:5–7 · DOI
  134. Sethi MK et al (2014) Comparative N-glycan profiling of colorectal cancer cell lines reveals unique bisecting GlcNAc and α-2,3-linked sialic acid determinants are associated with membrane proteins of the more metastatic/aggressive cell lines. J Proteome Res 13:277–288 · DOI
  135. Jia L et al (2017) miR-182 and miR-135b mediate the tumorigenesis and invasiveness of colorectal cancer cells via targeting ST6GALNAC2 and PI3K/AKT pathway. Dig Dis Sci 62:3447–3459 · DOI
  136. Schneider F et al (2001) Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas. Cancer Res 61:4605–4611
  137. Bos PD et al (2009) Genes that mediate breast cancer metastasis to the brain. Nature 459:1005–1009 · DOI · Paper page
  138. Shiratori Y et al (1992) Inhibition of hepatic metastasis of colon carcinoma by asialo GM1–positive cells in the liver. Hepatology 16:469–478 · DOI
  139. Sawada M et al (2002) Reduced sialidase expression in highly metastatic variants of mouse colon adenocarcinoma 26 and retardation of their metastatic ability by sialidase overexpression. Int J Cancer 97:180–185 · DOI
  140. Kawakami Y et al (2002) Tetraspanin CD9 is a ‘proteolipid’, and its interaction with alpha 3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility. J Biol Chem 277:34349–34358 · DOI
  141. Nakamori S, Ota DM, Cleary KR, Shirotani K, Irimura T (1994) MUC1 mucin expression as a marker of progression and metastasis of human colorectal carcinoma. Gastroenterology 106:353–361 · DOI
  142. Kato K et al (2010) Loss of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 and reduced O-glycosylation in colon carcinoma cells selected for hepatic metastasis. Glycoconj J 27:267–276 · DOI
  143. Dosaka-Akita H et al (2002) N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers. Br J Cancer 87:751–755 · DOI
  144. Hoff SD et al (1989) Increased expression of sialyl-dimeric LeX antigen in liver metastases of human colorectal carcinoma. Cancer Res 49:6883–6888
  145. Nakamori S et al (1993) Increased expression of sialyl Lewisx antigen correlates with poor survival in patients with colorectal carcinoma: clinicopathological and immunohistochemical study. Cancer Res 53:3632–3637
  146. Ono M, Hakomori S (2004) Glycosylation defining cancer cell motility and invasiveness. Glycoconj J 20:71–78 · DOI
  147. Fujita T et al (2011) CSLEX (Sialyl Lewis X) is a useful tumor marker for monitoring of breast cancer patients. Jpn J Clin Oncol 41:394–399 · DOI
  148. Very N, Lefebvre T, El Yazidi-Belkoura I (2018) Drug resistance related to aberrant glycosylation in colorectal cancer. Oncotarget 9:1380–1402 · DOI
  149. Rada M et al (2017) BTK blocks the inhibitory effects of MDM2 on p53 activity. Oncotarget 8:106639–106647 · DOI
  150. Shental-Bechor D, Levy Y (2008) Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc Natl Acad Sci U S A 105:8256–8261 · DOI
  151. Li D et al (2008) Knockdown of Mgat5 inhibits breast cancer cell growth with activation of CD4+ T cells and macrophages. J Immunol 180:3158–3165 · DOI
  152. Carrascal MA et al (2014) Sialyl Tn-expressing bladder cancer cells induce a tolerogenic phenotype in innate and adaptive immune cells. Mol Oncol 8:753–765 · DOI
  153. Soldati R et al (2012) Neuroblastoma triggers an immunoevasive program involving galectin-1-dependent modulation of T cell and dendritic cell compartments. Int J Cancer 131:1131–1141 · DOI
  154. Tsuboi S, Hatakeyama S, Ohyama C, Fukuda M (2012) Two opposing roles of O-glycans in tumor metastasis. Trends Mol Med 18:224–232 · DOI
  155. Kim YJ, Borsig L, Varki NM, Varki A (1998) P-selectin deficiency attenuates tumor growth and metastasis. Proc Natl Acad Sci U S A 95:9325–9330 · DOI · Paper page
  156. Labelle M, Hynes RO (2012) The initial hours of metastasis: the importance of cooperative host-tumor cell interactions during hematogenous dissemination. Cancer Discov 2:1091–1099 · DOI
  157. Rada M et al (2018) Inhibitor of apoptosis proteins (IAPs) mediate collagen type XI alpha 1-driven cisplatin resistance in ovarian cancer. Oncogene 37:4809–4820 · DOI
  158. Nallanthighal S et al (2020) Inhibition of collagen XI alpha 1-induced fatty acid oxidation triggers apoptotic cell death in cisplatin-resistant ovarian cancer. Cell Death Dis 11:1–12 · DOI
  159. Song E, Mechref Y (2013) LC-MS/MS identification of the O-glycosylation and hydroxylation of amino acid residues of collagen α-1 (II) chain from bovine cartilage. J Proteome Res 12:3599–3609 · DOI
  160. Gautieri A et al (2017) Advanced glycation end-products: Mechanics of aged collagen from molecule to tissue. Matrix Biol 59:95–108 · DOI
  161. Laferté S, Dennis JW (1988) Glycosylation-dependent collagen-binding activities of two membrane glycoproteins in MDAY-D2 tumor cells. Cancer Res 48:4743–4748
  162. Pouysségur J, Dayan F, Mazure NM (2006) Hypoxia signalling in cancer and approaches to enforce tumour regression. Nature 441:437–443 · DOI · Paper page
  163. Petrova V, Annicchiarico-Petruzzelli M, Melino G, Amelio I (2018) The hypoxic tumour microenvironment. Oncogenesis 7:10 · DOI
  164. Rada M, Lazaris A, Kapelanski-Lamoureux A, Mayer TZ, Metrakos P (2021) Tumor microenvironment conditions that favor vessel co-option in colorectal cancer liver metastases: A theoretical model. Semin Cancer Biol 71:52–64 · DOI
  165. Ferrer CM et al (2014) O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway. Mol Cell 54:820–831 · DOI
  166. Hu J et al (2005) Gene expression signature for angiogenic and nonangiogenic non-small-cell lung cancer. Oncogene 24:1212–1219 · DOI
  167. Pàez-Ribes M et al (2009) Antiangiogenic therapy elicits malignant progression of tumors to increased local invasion and distant metastasis. Cancer Cell 15:220–231 · DOI
  168. Rada, M., Reynolds, A. R., Lazaris, A., Seidah, N. & Metrakos, P. Inhibition of proprotein convertase subtilisin-like kexin type 9 (PCSK9) potentiates anti-angiogenic therapy in colorectal cancer liver metastases. BioRxiv 1–12 (2023). · DOI
  169. Rada M, Krzywon L, Petrillo S, Lazaris A, Metrakos P (2023) A retrospective study on the role of metformin in colorectal cancer liver metastases. Biomedicines 11:731 · DOI
  170. Rada M et al (2022) Angiopoietin-1 upregulates cancer cell motility in colorectal cancer liver metastases through actin-related protein 2/3. Cancers (Basel) 14:2540 · DOI
  171. Rada M et al (2021) Runt related transcription factor-1 plays a central role in vessel co-option of colorectal cancer liver metastases. Commun Biol 4:1–15 · DOI
  172. Rada M et al (2022) Cancer cells promote phenotypic alterations in hepatocytes at the edge of cancer cell nests to facilitate vessel co-option establishment in colorectal cancer liver metastases. Cancers 14:1318 · DOI
  173. Cheng WK, Oon CE (2018) How glycosylation aids tumor angiogenesis: An updated review. Biomed Pharmacother 103:1246–1252 · DOI
  174. Carrera-Aguado I et al (2024) The inhibition of vessel Co-option as an emerging strategy for cancer therapy. Int J Mol Sci 25:921 · DOI
  175. Shao R et al (2009) YKL-40, a secreted glycoprotein, promotes tumor angiogenesis. Oncogene 28:4456–4468 · DOI
  176. Goveia J, Stapor P, Carmeliet P (2014) Principles of targeting endothelial cell metabolism to treat angiogenesis and endothelial cell dysfunction in disease. EMBO Mol Med 6:1105–1120 · DOI
  177. Nie H et al (2020) O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth. Nat Commun 11:36 · DOI
  178. Lynch TP et al (2012) Critical role of O-linked β-N-Acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis. J Biol Chem 287:11070–11081 · DOI
  179. Ma Z, Vosseller K (2014) Cancer metabolism and elevated O-GlcNAc in oncogenic signaling. J Biol Chem 289:34457–34465 · DOI
  180. Weis SM, Cheresh DA (2011) Tumor angiogenesis: molecular pathways and therapeutic targets. Nat Med 17:1359–1370 · DOI
  181. Bergers G et al (2000) Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2:737–744 · DOI · Paper page
  182. Yeo HL et al (2019) Sialylation of vasorin by ST3Gal1 facilitates TGF-β1-mediated tumor angiogenesis and progression. Int J Cancer 144:1996–2007 · DOI
  183. Imamaki R et al (2018) Glycosylation controls cooperative PECAM-VEGFR2-β3 integrin functions at the endothelial surface for tumor angiogenesis. Oncogene 37:4287–4299 · DOI
  184. Mandal C, Sarkar S, Chatterjee U, Schwartz-Albiez R, Mandal C (2014) Disialoganglioside GD3-synthase over expression inhibits survival and angiogenesis of pancreatic cancer cells through cell cycle arrest at S-phase and disruption of integrin-β1-mediated anchorage. Int J Biochem Cell Biol 53:162–173 · DOI
  185. Rada M et al (2022) Disruption of integrin alpha-5/beta-1-dependent transforming growth factor beta-1 signaling pathway attenuates vessel co-option in colorectal cancer liver metastases. BioRxiv. https://doi.org/10.1101/2022.05.24.493291 · DOI
  186. Rada M et al (2022) Vitamin D supplementation improves the prognosis of patients with colorectal cancer liver metastases. medRxiv 38:1–18
  187. Palmieri V et al (2020) Neutrophils expressing lysyl oxidase-like 4 protein are present in colorectal cancer liver metastases resistant to anti-angiogenic therapy. J Pathol 251:213–223 · DOI
  188. Ibrahim NS et al (2020) Angiopoietin1 deficiency in hepatocytes affects the growth of colorectal cancer liver metastases (Crclm). Cancers (Basel) 12:35 · DOI
  189. García-Gómez P, Valiente M (2020) Vascular co-option in brain metastasis. Angiogenesis 23:3–8 · DOI
  190. Ibrahim SA et al (2020) Cancer-associated V-ATPase induces delayed apoptosis of protumorigenic neutrophils. Mol Oncol 14:590–610 · DOI
  191. Mayer TZ et al (2020) Role of innate immune cells in the development of vessel co-opting CRC liver metastases. Can Res. https://doi.org/10.1158/1538-7445.AM2020-3331 · DOI
  192. da Fonseca LM et al (2016) Glycosylation in cancer: interplay between multidrug resistance and epithelial-to-mesenchymal transition? Front Oncol. https://doi.org/10.3389/fonc.2016.00158 · DOI
  193. Zeng W et al (2021) Elevated N-glycosylation contributes to the cisplatin resistance of non-small cell lung cancer cells revealed by membrane proteomic and glycoproteomic analysis. Front Pharmacol. https://doi.org/10.3389/fphar.2021.805499 · DOI
  194. Lee G, Joung J-Y, Cho J-H, Son C-G, Lee N (2018) Overcoming P-glycoprotein-mediated multidrug resistance in colorectal cancer: potential reversal agents among herbal medicines. Evidence-Based Complement Alternative Med. https://doi.org/10.1155/2018/3412074 · DOI
  195. Ashique S et al (2024) Multi drug resistance in Colorectal Cancer- approaches to overcome, advancements and future success. Adv Cancer Biol—Metastasis 10:100114 · DOI
  196. Wang M, Zhu J, Lubman DM, Gao C (2019) Aberrant glycosylation and cancer biomarker discovery: a promising and thorny journey. Clin Chem Laboratory Med (CCLM) 57:407–416 · DOI
  197. Jiang Z et al (2018) β3GnT8 promotes colorectal cancer cells invasion via CD147/MMP2/Galectin3 axis. Front Physiol. https://doi.org/10.3389/fphys.2018.00588 · DOI
  198. Shen L et al (2014) Knockdown of β3GnT8 reverses 5-fluorouracil resistance in human colorectal cancer cells via inhibition the biosynthesis of polylactosamine-type N-glycans. Int J Oncol 45:2560–2568 · DOI
  199. Xu T et al (2014) Upregulation of CD147 promotes cell invasion, epithelial-to-mesenchymal transition and activates MAPK/ERK signaling pathway in colorectal cancer. Int J Clin Exp Pathol 7:7432–7441
  200. Peng L et al (2015) MiR-492 is functionally involved in Oxaliplatin resistance in colon cancer cells LS174T via its regulating the expression of CD147. Mol Cell Biochem 405:73–79 · DOI

200 of 236 shown

Metadata

Authors
Qusairy, Z., & Rada, M.
Affiliations
  • Research Institute of the McGill University Health Centre (CA)
  • Komar University of Science and Technology (IQ)
Corresponding author
Rada, Miran
ORCID
Rada, Miran
Venue
Molecular and Cellular Biochemistry
Publisher
Springer Science and Business Media LLC
Published
2025-05-19
Volume
480
Issue
9
Pages
4941-4959
ISSN
  • 0300-8177 (ISSN-L)
  • 1573-4919
DOI
10.1007/s11010-025-05303-1
OpenAlex
W4410485050
Cited by
16
References
245
Citations by year
2026: 12 · 2025: 4
FWCI
1.42
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Molecular and Cellular Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords
glycosylation, cancer, post-translational modification, tumor glycosylation, glycomics, tumor markers, tumor microenvironment, angiogenesis, metastasis, immune evasion, epigenetic regulation, drug resistance, precision medicine, personalized treatment
MeSH terms
Animals, Glycosylation, Humans, Neoplasms, Protein Processing, Post-Translational, Biomarkers, Tumor, Tumor Microenvironment

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Glycosylation in cancer: mechanisms, diagnostic markers, and therapeutic applications. https://app.cochat.ai/papers/10.1007/s11010-025-05303-1
The paper
Qusairy, Z., & Rada, M. (2025). Glycosylation in cancer: mechanisms, diagnostic markers, and therapeutic applications. Molecular and Cellular Biochemistry. https://doi.org/10.1007/s11010-025-05303-1