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Cancer-associated O-glycans include truncated mucin-type structures and elongated terminal motifs that act as ligands for glycan-binding proteins. Rather than a simple binary switch, tumors display heterogeneous mixtures of glycoforms across the cell surface and within the tumor glycocalyx. Truncated OGalNAc glycans regulate differentiation, barrier integrity, signaling, and immunosuppression via Siglecs and MGL, while elongated antigens promote metastasis and trafficking. Site-specific GalNAc-transferase isoenzymes further tune oncogenic processes, positioning O-glycans as context-dependent drivers and promising precision-therapy entry points.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":35,"@type":76,"position":81},"https://docshare.wps.com/document/healthcare/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/from-glycocode-to-precision-oncology-therapeutic-strategies-targeting-aberrant-o-galnac-glycosylation-in-cancer/356146/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/from-glycocode-to-precision-oncology-therapeutic-strategies-targeting-aberrant-o-galnac-glycosylation-in-cancer/356146.png","ImageObject",300,407,{"name":92,"@type":93},"LangkahRina","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-23","2026-09-23",true,{"@type":102,"interactionType":103,"userInteractionCount":52},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What role does aberrant O-glycosylation play in cancer progression?","Question",{"text":112,"@type":113},"Aberrant O-glycosylation contributes directly to multiple hallmarks of malignant transformation by shaping cancer cell surface glycoforms and influencing tumor behavior.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"How do truncated and elongated O-GalNAc glycans differ in function?",{"text":117,"@type":113},"Truncated aberrant OGalNAc glycans (e.g., Tn, STn, T) perturb differentiation, barrier integrity, signaling, and immunosuppression, while more elongated O-glycans (e.g., Lewis antigens) interact with receptors such as selectins to support metastasis and cellular trafficking.",{"name":119,"@type":110,"acceptedAnswer":120},"What therapeutic strategies are discussed for targeting aberrant O-GalNAc glycosylation?",{"text":121,"@type":113},"The review covers glycan vaccination approaches, development of monoclonal antibodies against specific antigens, direct targeting of glycopeptides, targeting STn and Lewis antigens, and strategies that alter interactions at the glycocalyx.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},356146,1790527055,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":34,"category_name":35,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":52,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":139,"language":140,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":67,"update_tm":144,"read_time":145},962090893776,"https://ap-avatar.wpscdn.com/davatar_155a257f0dc6eb9ab79c44ca47cae57d","This article is licensed under CC-BY-NC-ND 4.0  \n[pubs.acs.org/CR](pubs.acs.org/CR)  Review   \nFrom Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O‑GalNAc Glycosylation in Cancer  \nMikkel Koed Møller Aasted, Thapakorn Jaroentomeechai, Sally Dabelsteen, Hiren Joshi, Sean R. Stowell, and Hans H. Wandall *  \n Cite This: Chem. Rev. 2026, 126, 8957−9005  \nRead Online  \n\n|  |  |  |  |  |  |\n| --- | --- | --- | --- | --- | --- |\n| ACCESS   | Metrics & More |  |  Article Recommendations |  | *sı Supporting Information |\n\nABSTRACT: Aberrant O-glycosylation is a prominent feature of cancer and contributes directly to multiple hallmarks of malignant transformation. Cancer-associated O-glycans include both truncated structures that are unique to mucin-type O-glycosylation and more elongated terminal motifs that function as ligands for glycan-binding proteins. Instead of representing a simple binary change from elongated to truncated structures, it is increasingly understood that these glycans decorate the cancer cell surface with a heterogeneous pattern of truncated, elongated, capped, and partially processed glycoforms, which coexist even on individual proteins and within the tumor glycocalyx. Functionally, truncated aberrant OGalNAc glycans, such as Tn, STn, and T perturb epithelial differentiation, barrier integrity, signaling, and immunosuppression through interactions with glycan binding receptors, such as Siglecs and MGL. In addition, more elongated O-glycans, including Lewis antigens, interact with selectins promoting metastasis and cellular trafficking. Moreover, individual GalNAc-transferase isoenzymes, governing site-specific O-glycosylation, are emerging as  \ncontext-dependent regulators of oncogenic processes through glycosylation of selected proteins. These observations establish cancerassociated O-glycans as context-dependent molecular drivers of tumor progression and promising therapeutic entry points. In this review, we discuss the expression, regulation, and functions of cancer-associated O-glycans, their roles in glycan-binding protein biology, and emerging therapeutic strategies that may enable a new generation of glycan-directed precision treatments in oncology.  \n■ CONTENTS  \n1. Introduction 8958  \n1.1. Biosynthesis of O-GalNAc-Glycans 8958  \n2. Surface Exposed Aberrant O-GalNAc Glycans Area Hallmark of Cancer 8958  \n2.1. Cancer-Associated O-Glycans 8958  \n2.2. Mechanisms Underlying Aberrant O-Glycosylation in Cancer 8962  \n2.3. O-Glycans Promote Oncogenesis 8963  \n2.4. Individual GalNAc-T Isoenzymes Emerge Asan Oncogenic Driver 8967  \n3. Effects of O-GalNAc Glycans on Cancer Progression through Glycan-Binding Proteins 8969  \n3.1. Selectins Recognize Elongated Cancer-Associated O-GalNAc Glycans to Promote Metastasis 8970  \n3.2. Siglecs Recognize Clustered O-GalNAc Glycan SAMPs on Mucin Domains to Serve As Immune Checkpoints 8970  \n3.3. MGL Receptor Mediates Immunosuppression through Tn-Recognition 8971  \n3.4. Galectins Regulate Various Processes and Immune Homeostasis in Cancer 8972  \n3.5. Context and Avidity Shape How CancerAssociated O-GalNAc Glycans Engage Glycan-Binding Proteins 8976  \n4. Therapeutic Strategies Targeting Aberrant OGalNAc Glycosylation in Cancer 8977  \n4.1. O-GalNAc Glycan Vaccination Strategies 8977  \n4.2. Development of Monoclonal Antibodies against Tn, STn, and Lewis Antigens 8978  \n4.3. Direct Targeting of Tn- and Tn-Glycopeptides with Monoclonal Antibodies 8978  \n4.4. Targeting of STn-Antigen 8980  \n4.5. Targeting of the Lewis-Antigens 8980  \n4.6. Altering Interactions at the Glycocalyx 8981  \n5. Future Directions: Toward Context-Driven Exploitation of Cancer Associated Glycans in Precision Oncology 8982  \n6. Conclusion 8984  \nAssociated Content 8984  \n\n| Received: October 20, 2025\u003Cbr>Revised: July 3, 2026\u003Cbr>Accepted: July 8, 2026\u003Cbr>Published: August 4, 2026 | |\n| --- | --- |\n\n© 2026 The Authors. Published by American Chemical Society  \n8957  \n[https://doi.org/10","cbCaihBxTrDS2J8V","https://ap.wps.com/l/cbCaihBxTrDS2J8V","pdf",9503063,49,"English","# Introduction\n## Biosynthesis of O-GalNAc Glycans\n# Surface Exposed Aberrant O-GalNAc Glycans Area Hallmark of Cancer\n## Cancer-Associated O-Glycans\n## Mechanisms Underlying Aberrant O-Glycosylation in Cancer\n## O-Glycans Promote Oncogenesis\n## Individual GalNAc-T Isoenzymes Emerge As an Oncogenic Driver\n# Effects of O-GalNAc Glycans on Cancer Progression through Glycan-Binding Proteins\n## Selectins Recognize Elongated Cancer-Associated O-GalNAc Glycans to Promote Metastasis\n## Siglecs Recognize Clustered O-GalNAc Glycan SAMPs on Mucin Domains to Serve As Immune Checkpoints\n## MGL Receptor Mediates Immunosuppression through Tn-Recognition\n## Galectins Regulate Various Processes and Immune Homeostasis in Cancer\n## Context and Avidity Shape How Cancer-Associated O-GalNAc Glycans Engage Glycan-Binding Proteins\n# Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer\n## O-GalNAc Glycan Vaccination Strategies\n## Development of Monoclonal Antibodies against Tn, STn, and Lewis Antigens\n## Direct Targeting of Tn- and Tn-Glycopeptides with Monoclonal Antibodies\n## Targeting of STn-Antigen\n## Targeting of the Lewis Antigens\n## Altering Interactions at the Glycocalyx\n# Future Directions: Toward Context-Driven Exploitation of Cancer Associated Glycans in Precision Oncology\n# Conclusion","[{\"question\":\"What role does aberrant O-glycosylation play in cancer progression?\",\"answer\":\"Aberrant O-glycosylation contributes directly to multiple hallmarks of malignant transformation by shaping cancer cell surface glycoforms and influencing tumor behavior.\"},{\"question\":\"How do truncated and elongated O-GalNAc glycans differ in function?\",\"answer\":\"Truncated aberrant OGalNAc glycans (e.g., Tn, STn, T) perturb differentiation, barrier integrity, signaling, and immunosuppression, while more elongated O-glycans (e.g., Lewis antigens) interact with receptors such as selectins to support metastasis and cellular trafficking.\"},{\"question\":\"What therapeutic strategies are discussed for targeting aberrant O-GalNAc glycosylation?\",\"answer\":\"The review covers glycan vaccination approaches, development of monoclonal antibodies against specific antigens, direct targeting of glycopeptides, targeting STn and Lewis antigens, and strategies that alter interactions at the glycocalyx.\"}]","From Glycocode to Precision Oncology - Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer | PDF",1790123636,123]