[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-381843-105":59,"doc-detail-381843-en":130},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":123,"head_meta":125,"extra_data":127,"updated_unix":129},105,"en","chemical-proteomic-approach-for-in-depth-glycosylation-profiling-of-plasma-carcinoembryonic-antigen-in-cancer-patients","Chemical Proteomic Approach for In-Depth Glycosylation Profiling of Plasma Carcinoembryonic Antigen in Cancer Patients","","A chemical proteomic workflow is established to characterize protein glycosylation of plasma carcinoembryonic antigen (CEA) at low abundance, addressing the limitations of existing CEA assays in sensitivity and specificity. Glycosylation at the intact glycopeptide level adds a molecular-feature dimension to improve cancer diagnosis and progression monitoring. The strategy enables capture and analysis from as little as 1 ng/mL CEA, identifying the majority of potential N-glycosylation sites, including cancer-associated site-specific glycoform changes across colorectal and lung cancers.",{"@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/chemical-proteomic-approach-for-in-depth-glycosylation-profiling-of-plasma-carcinoembryonic-antigen-in-cancer-patients/381843/",{"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/chemical-proteomic-approach-for-in-depth-glycosylation-profiling-of-plasma-carcinoembryonic-antigen-in-cancer-patients/381843.png","ImageObject",300,407,{"name":92,"@type":93},"4398046744996","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-29","2026-09-24",true,{"@type":102,"interactionType":103,"userInteractionCount":34},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What problem does the chemical proteomic approach address for plasma CEA analysis?","Question",{"text":112,"@type":113},"It addresses the low abundance of plasma CEA that makes systematic, site-specific glycosylation characterization difficult, which limits diagnostic sensitivity and specificity.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"How does the method enable in-depth glycosylation profiling at intact glycopeptide level?",{"text":117,"@type":113},"It uses chemical proteomics combined with multienzymatic digestion and a trifunctional probe to capture plasma CEA and generate covalent linkage to its antibody under UV irradiation for intact glycopeptide characterization.",{"name":119,"@type":110,"acceptedAnswer":120},"What clinical findings were observed in cancer patients using this strategy?",{"text":121,"@type":113},"Differential site-specific CEA glycoforms were detected in patients with colorectal cancer and lung cancer, with distributions varying across colorectal cancer progression and many site-specific glycoforms overexpressed at stage II.","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},381843,1790449989,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":66,"doc_module":4,"category_id":34,"category_name":35,"doc_title":65,"doc_description":67,"doc_content":133,"file_id":134,"file_url":135,"file_type":136,"file_size":137,"view_count":34,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":138,"language":139,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":140,"faqs":141,"seo_title":142,"seo_description":67,"update_tm":143,"read_time":41},4398046744996,"Chemical Proteomic Approach for In-Depth Glycosylation Profiling of Plasma Carcinoembryonic Antigen in Cancer Patients  \nAuthors  \nJin Chen, Lijun Yang, Chang Li, Luobin Zhang, Weina Gao, Ruilian Xu, and Ruijun Tian  \nCorrespondence [xuruilian@126.com](xuruilian@126.com) ; tianrj@ [sustech.edu.cn](sustech.edu.cn)  \nIn Brief  \nA chemical proteomic approach for glycosylation profiling of proteins was established for glycosylation characterization of plasma CEA with low abundance. Although CEA has been widely used in diagnosis and prognosis of many cancers, it lacks specificity and sensitivity. We found that the glycosylation of CEA on intact glycopeptide level provided additional dimension of molecular features to improve the performance of CEA in cancer diagnosis and progression.  \nGraphical Abstract  \nHighlights  \n• A chemical proteomic approach for glycosylation profiling of low abundant proteins.  \n• In-depth profiling of plasma carcinoembryonic antigen on intact glycopeptide level.  \n• Glycosylation identification with high sensitivity and reproducibility.  \n• Glycosylation features of plasma carcinoembryonic antigen in cancer patients.  \n2023, Mol Cell Proteomics 22(11), 100662  \n© 2023 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license ([http://creativecommons.org/](http://creativecommons.org/)[ ](http://creativecommons.org/)[licenses/by/4.0/](licenses/by/4.0/)).  \n[https://doi.org/10.1016/j.mcpro.2023.100662](https://doi.org/10.1016/j.mcpro.2023.100662)  \n RESEARCH  \n| Chemical Proteomic Approach for In-Depth Glycosylation Profiling of Plasma Carcinoembryonic Antigen in Cancer Patients\u003Cbr>Jin Chen 1 ,2 ,‡, Lijun Yang3 ,4 ,‡, Chang Li 1, Luobin Zhang3, Weina Gao 1 , Ruilian Xu3 ,* , and\u003Cbr>Ruijun Tian 1 ,* |  |\n| --- | --- |\n| Carcinoembryonic antigen (CEA) of human plasma is abiomarker of many cancer diseases, and its N-glycosylation accounts for 60% of molecular mass. It is highly desirable to characterize its glycoforms for providing additional dimension of features to increase its performance in prognosis and diagnosis of cancers. However, to systematically characterize its site-specific glycosylationis challenging because of its low abundance. Here, we developed a highly sensitive strategy for in-depth glycosylation profiling of plasma CEA through chemical proteomics combined with multienzymatic digestion. Atrifunctional probe was utilized to generate covalent bond of plasma CEA and its antibody upon UV irradiation. As low as 1 ng/ml CEA in plasma could be captured and digested with trypsin and chymotrypsin for intact glycopeptide characterization. Twenty six of 28 potential Nglycosylation sites were well identified, which were the most comprehensive N-glycosylation site characterization of CEA on intact glycopeptide level as far as we known. Importantly, this strategy was applied to the glycosylation analysis of plasma CEA in cancer patients. Differential site-specific glycoforms of plasma CEA were observed inpatients with colorectal cancers (CRCs) and lung cancer. The distributions of site-specific glycoforms were different as the progression of CRC, and most site-specific glycoforms were overexpressed in stage II of CRC. Overall, we established a highly sensitive chemical proteomic method to profile site-specific glycosylation of plasma CEA, which should generally applicable to other well-established cancer glycoprotein biomarkers for improving their cancer diagnosis and monitoring performance.\u003Cbr>Protein glycosylation is a crucial post-translational modification in health and disease (1) . Evidences showed that glycosites and glycan structures are both essential for | glycosylation and various biological processes. For example, N-glycosylation regulates cancer metastasis and invasion (2 , 3), and the alternation of N-glycan was correlated with the development of cancer (4) . PD-L1 contributes to the immune escape of c","cbCaicMFcmlCDpIJ","https://ap.wps.com/l/cbCaicMFcmlCDpIJ","pdf",3218453,12,"English","# In Brief\n# Research\n## CEA glycosylation and analytical challenges\n## Chemical proteomics strategy for low-abundance plasma biomarkers\n## Application to cancer patients: site-specific glycoform changes\n# Background and Rationale\n## Glycosylation in health and cancer\n## Plasma biomarkers and limitations of conventional capture methods","[{\"question\":\"What problem does the chemical proteomic approach address for plasma CEA analysis?\",\"answer\":\"It addresses the low abundance of plasma CEA that makes systematic, site-specific glycosylation characterization difficult, which limits diagnostic sensitivity and specificity.\"},{\"question\":\"How does the method enable in-depth glycosylation profiling at intact glycopeptide level?\",\"answer\":\"It uses chemical proteomics combined with multienzymatic digestion and a trifunctional probe to capture plasma CEA and generate covalent linkage to its antibody under UV irradiation for intact glycopeptide characterization.\"},{\"question\":\"What clinical findings were observed in cancer patients using this strategy?\",\"answer\":\"Differential site-specific CEA glycoforms were detected in patients with colorectal cancer and lung cancer, with distributions varying across colorectal cancer progression and many site-specific glycoforms overexpressed at stage II.\"}]","Chemical Proteomic Approach for In-Depth Glycosylation Profiling of Plasma Carcinoembryonic Antigen in Cancer Patients | PDF",1790247435]