{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["85(14)"],"submitter":["Koistinen H"],"funding":["This study was supported by grants from Sigrid Jusélius Foundation (Hannu Koistinen, Tuomas Mirtti, Andrew Erickson), Cancer Foundation Finland (Andrew Erickson, Tuomas Mirtti, Antti Rannikko), Finnish Cancer Institute (Tuomas Mirtti), Finnish Society of Sciences and Letters (Hannu Koistinen), Magnus Ehrnrooth Foundation (Hannu Koistinen), Finnish Society of Clinical Chemistry (Hannu Koistinen), Laboratoriolääketieteen edistämissäätiö (Hannu Koistinen), Research Council of Finland (Andrew Erickson, Antti Rannikko), Instrumentarium Science Foundation (Andrew Erickson grant), Digital Precision Cancer Medicine Flagship iCAN (Andrew Erickson), Faculty of Medicine University of Helsinki (Andrew Erickson), Jane and Aatos Erkko Foundation (Antti Rannikko), Helsinki University Hospital research fu"],"pubmed_abstract":["<h4>Background</h4>The glycosylation of proteins is commonly altered in cancer. This offers novel opportunities for cancer biomarker development. As prostate-specific antigen (PSA) is a glycoprotein, identification of cancer-specific PSA-glycoforms is feasible. Such PSA-glycoforms may provide valuable diagnostic and prognostic information.<h4>Methods</h4>PSA-glycoforms were studied in tissues, using in situ proximity-ligation assay (PLA)-based detection with a PSA-specific antibody and 25 different glycan-binding lectins.<h4>Results</h4>Using 25 different lectins and a small tissue microarray (TMA), we showed that glycosylation of PSA in cancerous tissues is different from that in benign prostate. In a larger TMA with samples from 162 patients, PSA-glycoforms detected by succinylated wheat"],"journal":["The Prostate"],"pagination":["1290-1298"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12379856"],"repository":["biostudies-literature"],"pubmed_title":["Altered Glycosylation of PSA in Prostate Cancer Tissue."],"pmcid":["PMC12379856"],"pubmed_authors":["Merivirta RM","Koistinen H","Rannikko A","Erickson A","Lempiainen A","Stenman UH","Mirtti T","Lehto TP"],"additional_accession":[]},"is_claimable":false,"name":"Altered Glycosylation of PSA in Prostate Cancer Tissue.","description":"<h4>Background</h4>The glycosylation of proteins is commonly altered in cancer. This offers novel opportunities for cancer biomarker development. As prostate-specific antigen (PSA) is a glycoprotein, identification of cancer-specific PSA-glycoforms is feasible. Such PSA-glycoforms may provide valuable diagnostic and prognostic information.<h4>Methods</h4>PSA-glycoforms were studied in tissues, using in situ proximity-ligation assay (PLA)-based detection with a PSA-specific antibody and 25 different glycan-binding lectins.<h4>Results</h4>Using 25 different lectins and a small tissue microarray (TMA), we showed that glycosylation of PSA in cancerous tissues is different from that in benign prostate. In a larger TMA with samples from 162 patients, PSA-glycoforms detected by succinylated wheat","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-05-09T17:59:18.423Z","creation":"2026-04-08T01:08:41.204Z"},"accession":"S-EPMC12379856","cross_references":{"pubmed":["40635354"],"doi":["10.1002/pros.70014"]}}