Evidence map›Paper›PMID 40635354›Full record

ArticleThe Prostate2025

Altered Glycosylation of PSA in Prostate Cancer Tissue.

Hannu Koistinen, Ruusu-Maaria Merivirta, Timo-Pekka Lehto, Anna Lempiäinen, Andrew Erickson, Ulf-Håkan Stenman, Antti Rannikko, Tuomas Mirtti

Abstract read
In one paragraph

Article in The Prostate, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Hannu KoistinenDepartment of Clinical Chemistry and Haematology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.ORCID 0000-0003-0926-3109
Ruusu-Maaria MerivirtaDepartment of Clinical Chemistry and Haematology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.ORCID 0000-0001-5817-890X
Timo-Pekka LehtoResearch Program in Systems Oncology, University of Helsinki, Helsinki, Finland.
Anna LempiäinenDepartment of Clinical Chemistry and Haematology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Andrew EricksonResearch Program in Systems Oncology, University of Helsinki, Helsinki, Finland.
Ulf-Håkan StenmanDepartment of Clinical Chemistry and Haematology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Antti RannikkoResearch Program in Systems Oncology, University of Helsinki, Helsinki, Finland.
Tuomas MirttiResearch Program in Systems Oncology, University of Helsinki, Helsinki, Finland.

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 funds (Anna Lempiäinen, Hannu Koistinen, Tuomas Mirtti) and State funding for university level health research (Tuomas Mirtti, Antti Rannikko).
6 · The paper itself

Abstract

backgroundThe 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.

methodsPSA-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.

resultsUsing 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 germ (WGA

conclusionsWe showed here that glycosylation of PSA is changed in situ in prostate cancer. The identified lectins, showing preferential binding to cancer-associated PSA-glycoforms, will aid the future development of a diagnostic serum test of prostate cancer. Such a test has potential to revolutionize prostate cancer diagnostics.

Indexed as

ProstateProstate-Specific AntigenProstatic NeoplasmsAgedBiomarkers, TumorGlycosylationHumansMaleMiddle AgedTissue Array AnalysisBiomarkers, TumorProstate-Specific Antigenglycosylationin situ proximity ligationlectinprostate cancerPSA

Identifiers

PMID40635354
PMCPMC12379856

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.