{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13"],"submitter":["Takakura D"],"pubmed_abstract":["Aberrant glycosylation is a prominent feature of cancer, that can be used as targets to improve the existing cancer biomarkers, and help to assess metastasis risks, and therapeutic effects. We developed a targeted O-glycoproteomics method using serum specimens, and evaluated its utility in identifying advanced colorectal cancer (CRC) markers. To this end, we combined consecutive lectin affinity purification using <i>Maclura pomifera</i> lectin (MPL), jacalin, and <i>Sambucus nigra</i> lectin, which have affinities for the following O-glycans, that have received attention as cancer-related antigens, Tn (GalNAc-Ser/Thr), Sialyl Tn (Siaα2-6GalNAc-Ser/Thr), T (Galβ1-3GalNAc-Ser/Thr), Sialyl T (Siaα2-3Galβ1-GalNAc-Ser/Thr), and di-Sialyl T (Siaα2-3Galβ1-3[Siaα2-6] GalNAc-Ser/Thr), with a unique"],"journal":["Frontiers in oncology"],"pagination":["1104936"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9948623"],"repository":["biostudies-literature"],"pubmed_title":["Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer."],"pmcid":["PMC9948623"],"pubmed_authors":["Tokuhisa M","Ichikawa Y","Kawasaki N","Takakura D","Kobayashi N","Ohashi S"],"additional_accession":[]},"is_claimable":false,"name":"Targeted O-glycoproteomics for the development of diagnostic markers for advanced colorectal cancer.","description":"Aberrant glycosylation is a prominent feature of cancer, that can be used as targets to improve the existing cancer biomarkers, and help to assess metastasis risks, and therapeutic effects. We developed a targeted O-glycoproteomics method using serum specimens, and evaluated its utility in identifying advanced colorectal cancer (CRC) markers. To this end, we combined consecutive lectin affinity purification using <i>Maclura pomifera</i> lectin (MPL), jacalin, and <i>Sambucus nigra</i> lectin, which have affinities for the following O-glycans, that have received attention as cancer-related antigens, Tn (GalNAc-Ser/Thr), Sialyl Tn (Siaα2-6GalNAc-Ser/Thr), T (Galβ1-3GalNAc-Ser/Thr), Sialyl T (Siaα2-3Galβ1-GalNAc-Ser/Thr), and di-Sialyl T (Siaα2-3Galβ1-3[Siaα2-6] GalNAc-Ser/Thr), with a unique","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023","modification":"2025-04-29T10:47:46.387Z","creation":"2024-11-20T19:24:49.108Z"},"accession":"S-EPMC9948623","cross_references":{"pubmed":["36845686"],"doi":["10.3389/fonc.2023.1104936"]}}