Evidence map›Paper›PMID 40036572›Full record

ArticleGlycobiology2025

Intact glycopeptide analysis of human prostate tissue reveals site-specific heterogeneity of protein glycosylation in prostate cancer.

Kathryn L Kapp, Fernando Garcia-Marques, Sarah M Totten, Abel Bermudez, Cheylene Tanimoto, James D Brooks, Sharon J Pitteri

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Glycobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Kathryn L KappCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.
Fernando Garcia-MarquesCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.
Sarah M TottenCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.
Abel BermudezCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.
Cheylene TanimotoCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.
James D BrooksDepartment of Urology, Stanford University School of Medicine, Center of Academic Medicine, 453 Quarry Rd, Urology-5656, Palo Alto, California 94304, USA.
Sharon J PitteriCanary Center at Stanford for Cancer Early Detection, Department of Radiology, Stanford University School of Medicine, 3155 Porter Drive, Palo Alto, CA 94304, USA.ORCID 0000-0002-3119-873X

Funding

Stanford O'Brien Urology Research CenterU54DK130065 · NIDDK · STANFORD UNIVERSITY · PI JAMES D. BROOKS · 2021 to 2026
$8.3M
Stanford Molecular and Cellular Characterization LaboratoryU01CA196387 · NCI · STANFORD UNIVERSITY · PI BROOKS, JAMES D. · 2015 to 2020
$5.2M
Glycosylation and Immune Evasion in Urologic TumorsU01CA226051 · NCI · STANFORD UNIVERSITY · PI BERTOZZI, CAROLYN, BROOKS, JAMES D. · 2019 to 2023
$3.0M
NCI NIH HHS U01 CA196387NCI NIH HHS U01 CA226051NIDDK NIH HHS U54 DK130065
6 · The paper itself

Abstract

Approximately 300,000 American men were diagnosed with prostate cancer in 2024. Existing screening approaches based on measuring levels of prostate-specific antigen in the blood lack specificity for prostate cancer. Studying the glycans attached to proteins has the potential to generate new biomarker candidates and/or increase the specificity of existing protein biomarkers, and studying protein glycosylation changes in prostate cancer could also add new information to our understanding of prostate cancer biology. Here, we present the analysis of N-glycoproteins in clinical prostate cancer tissue and patient-matched, non-cancerous adjacent tissue using LC-MS/MS-based intact N-linked glycopeptide analysis. This analysis allowed us to characterize protein N-linked glycosylation changes in prostate cancer at the glycoprotein, glycopeptide, and glycosite levels. Overall, 1894 unique N-glycosites on 7022 unique N-glycopeptides from 1354 unique glycoproteins were identified. Importantly, we observed an overall increase in glycoprotein, glycopeptide, and glycosite counts in prostate cancer tissue than non-cancerous tissue. We identified biological functions enriched in prostate cancer that relate to cancer development. Additionally, we characterized N-glycosite-specific changes in prostate cancer, demonstrating significant meta- and micro-heterogeneity in N-glycan composition in prostate cancer in comparison to non-cancerous tissue. Our findings support the idea that protein glycosylation is heavily impacted and aberrant in prostate cancer and provide examples of N-glycosite-specific changes that could be exploited for more specific markers of prostate cancer.

Indexed as

GlycopeptidesGlycoproteinsProstateProstatic NeoplasmsChromatography, LiquidGlycosylationHumansMaleTandem Mass SpectrometryGlycopeptidesGlycoproteinscancerglycosylationmass spectrometryprostate

Identifiers

PMID40036572
PMCPMC11899575

What OpenQuestion holds

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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.