Dataset Information

PRM analysis of serum samples obtained from PCa and BPH patients

ABSTRACT: The aim of this project was the development of a predicitive model combining clinical variables and a panel of proteins measured by targeted-MS able to distinguish PCa from BPH. In particular, a total of 32 formerly N-glycosylated peptides were quantified by PRM.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

DISEASE(S): Prostate Adenocarcinoma

SUBMITTER: Caterina Gabriele

LAB HEAD: Marco Gaspari

PROVIDER: PXD035935 | Pride | 2024-01-26

REPOSITORIES: Pride

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Publications

Development of a predictive model to distinguish prostate cancer from benign prostatic hyperplasia by integrating serum glycoproteomics and clinical variables.

Gabriele Caterina C Aracri Federica F Prestagiacomo Licia Elvira LE Rota Maria Antonietta MA Alba Stefano S Tradigo Giuseppe G Guzzi Pietro Hiram PH Cuda Giovanni G Damiano Rocco R Veltri Pierangelo P Gaspari Marco M

Clinical proteomics 20231121 1

<h4>Background</h4>Prostate Cancer (PCa) represents the second leading cause of cancer-related death in men. Prostate-specific antigen (PSA) serum testing, currently used for PCa screening, lacks the necessary sensitivity and specificity. New non-invasive diagnostic tools able to discriminate tumoral from benign conditions and aggressive (AG-PCa) from indolent forms of PCa (NAG-PCa) are required to avoid unnecessary biopsies.<h4>Methods</h4>In this work, 32 formerly N-glycosylated peptides were ...[more]

PMID: 37990292

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Project description:Glycobiology plays a central role in prostate cancer (PCa), as evidenced by the aberrant glycosylation in PCa-derived glycoproteins. Understanding the protein glycosylation changes underling PCa onset and progression may open opportunities for the discovery of novel biomarkers for PCa detection and stratification as well as targets for PCa metastasis. Advances in mass spectrometry-based glycomics and glycoproteomics have opened up exciting avenues for deep characterisation of the immensely, yet poorly understood complex glycoproteome. In this study, we have used integrated glycomics and glycoproteomics to explore the protein, cell and tumour-grade specific N- and O- glycosylation signatures in surgically-removed fresh PCa tissues grouped into five PCa disease grades and tissues from benign prostatic hyperplasia patients (BPH). Porous graphitised carbon–liquid chromatography (PGC–LC)-MS/MS analysis was used to profile the N-and O-glycome, revealing PCa grade specific N and O glycosylation changes, including oligomannosidic and paucimannosidic, bisecting-GlcNAc and highly branched tri- and tetra-antennary fucosylated and sialylated N-glycans as well as sialylated core 1 and 2 type O-glycans. High resolution LC-MS/MS was then employed to capture the micro and macroheterogeneity of 1,085 N-glycosites (>7,400 unique N-glycopeptides) from 540 N-glycoproteins and 360 O-glycosites (>500 unique O-glycopeptides) from 178 O-glycoproteins and reveal protein and cell specific N- and O- glycosylation changes associated with PCa progression. We also showed PCa grade-specific increase in the expression of oligosaccharyltransferase (OST) subunits that correlate with changes in the site occupancy of N-glycoproteins. In conclusion, this study shows that integrated glycomics and glycoproteomics can provide unprecedented insight into key molecular features and site-specific glycan heterogeneity contributing to the highly diverse tumour-microenvironment and allow us to deconstruct the regulation of the protein, cell and tumour-grade-specific glycosylation associated with PCa onset and development.

			Action	DRS
	PRM_method.txt	Txt
	UMG-01-A.raw	Raw
	UMG-01-B.raw	Raw
	UMG-07-A.raw	Raw
	UMG-07-B.raw	Raw