PXD039814

PXD039814 is an original dataset announced via ProteomeXchange.

Title	Quantification of amyloid protein enrichment by mass spectrometry improves typing of amyloidosis
Description	Amyloidosis typing is crucial to determine the best therapeutic strategy for patients. Since conventional histological techniques often fail, the identification of amyloid precursors by mass spectrometry became the new standard. However, without quantification, selecting the amyloid precursor from proteins that may be ubiquitous under non-pathological conditions may be equivocal. Therefore, we quantified protein enrichment in amyloid deposits to improve typing. Protein enrichment was measured by extracted ion chromatogram based label-free (LFX) quantification by comparing a microdissected amyloid area with a non-amyloid area. We assessed the discrimination ability of candidate precursors with this approach compared to the two practiced identification methods. As proof of concept, we selected seven cases, 5 typical of the most common amyloidosis subtypes and typed by immunostainings (IHC), 2 unconclusive after immunohistochemistry. Proteins associated with amyloid deposits were identified in all samples confirming the pathology. When the routine clinical mass spectrometric identification techniques allowed unambiguous conclusions for 2/3 of 7 cases, quantification of the enrichment ratio in the amyloid deposit allowed unambiguous precursor selection in all cases. Quantification of precursor enrichment in amyloid deposits is a promising optimization for amyloidosis typing. Incorporated into routine clinical processes, it will improve patient care in difficult diagnostic situations.
HostingRepository	PRIDE
AnnounceDate	2026-05-25
AnnouncementXML	Submission_2026-05-24_16:28:41.567.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Dupuy Jean-William
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-03 01:38:35	ID requested
⏵ 1	2026-05-24 16:28:42	announced

Di Tommaso S, Chauveau B, Dourthe C, Dupuy JW, Saltel F, Bail BL, Raymond AA, Quantitative enrichment of amyloid precursors refines mass spectrometry-based amyloidosis diagnosis. Clin Proteomics, 23(1):(2026) [pubmed]

10.1186/s12014-026-09598-0;

submitter keyword: proteomics, mass spectrometry, label-free quantification,amyloidosis typing

Anne-Aurelie Raymond
contact affiliation	Oncoprot Platform, TBM-Core US 005, F-33000 Bordeau, France. univ. Bordeaux, Inserm UMR1312 BoRdeaux Institute of onCology (BRIC), F-33000 Bordeaux, France
contact email	anne-aurelie.raymond@inserm.fr
lab head
Dupuy Jean-William
contact affiliation	OncoProt plateform, UAR TBMCore CNRS 3427 INSERM US005 University of Bordeaux
contact email	jean-william.dupuy@u-bordeaux.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814

PRIDE project URI

• PRIDE
  1. PXD039814
     1. Label: PRIDE project
     2. Name: Quantification of amyloid protein enrichment by mass spectrometry improves typing of amyloidosis