{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Link_between_files.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220608_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot210126_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220608_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220302_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220302_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/fs200703_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220608_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot210126_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/Oncoprot220608_04.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/RP_UP000005640_Homo_sapiens_2022_01.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010743.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010744.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F017085.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F016215.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010788.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F012622.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010762.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F012618.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010785.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F017097.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F017088.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F016216.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F010763.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD039814/F017084.dat"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["anne-aurelie.raymond@inserm.fr"],"submitter":["Dupuy Jean-William"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Proteomics","Amyloidosis typing","Mass spectrometry","Label-free quantification"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD039814"],"sample_protocol":["Laser microdissected sections were collected and immerged in 50 mM Ammonium bicarbonate buffer. Fragments were heated at 90°C for 120 min with occasional vortexing. Samples were reduce in 10mM DTT and alkyled in 100mM IAA before to be digested into tryptic peptides overnight and analysed by liquid chromatography electrospray tandem mass spectrometry (MS)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For protein identification, Mascot 2.5 algorithm through Proteome Discoverer 2.5 Software (Thermo Fisher Scientific Inc.) was used in batch mode by searching against the UniProt Homo sapiens database (79 071 entries, Reference Proteome Set, release date: January, 2022) from http://www.uniprot.org/ website. Two missed enzyme cleavages were allowed for the trypsin. Mass tolerances in MS and MS/MS were set to 10 ppm and 0.02 Da. Oxidation of methionine and acetylation of lysine were searched as dynamic modifications. Carbamidomethylation on cysteine was searched as static modification. Raw LC-MS/MS data were imported in Proline Studio for feature detection, alignment, and quantification. Proteins identification was accepted only with at least 2 specific peptides with a pretty rank=1 and with a protein FDR value less than 1.0% calculated using the “decoy” option in Mascot. Label-free quantification of MS1 spectra by extracted ion chromatograms (XIC) was carried out with parameters indicated previously [Henriet E et al. Hepatology. 2017]. Protein ratios were median normalized."],"omics_type":["Proteomics"],"labhead":["Anne-Aurelie Raymond"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Oncoprot Platform, TBM-Core US 005, F-33000 Bordeau, France.  univ. Bordeaux, Inserm UMR1312 BoRdeaux Institute of onCology (BRIC), F-33000 Bordeaux, France"],"species":["Homo Sapiens (human)"],"submitter_mail":["jean-william.dupuy@u-bordeaux.fr"],"publication":["41845213 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. 2026 23(1):25 10.1186/s12014-026-09598-0"],"submitter_affiliation":["OncoProt plateform, UAR TBMCore CNRS 3427 INSERM US005 University of Bordeaux"],"submitter_country":["France"],"pubmed_abstract":["<h4>Introduction</h4>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 has become the new standard. However, without quantification, selecting the amyloid precursor from proteins that may be ubiquitous under non-pathological conditions can be equivocal. Therefore, we quantified protein enrichment in amyloid deposits to improve amyloidosis typing.<h4>Methods</h4>Protein enrichment was measured by extracted ion chromatogram-based label-free quantification by comparing a microdissected amyloid area to a non-amyloid area. We assessed the discrimination ability of candidate precursors with this approach compared to the two practiced identification methods.<h4>Results</h4>As a proof of concept, we selected 9 cases including the most common amyloidosis subtypes, 6 typed by immunohistochemistry and 3 inconclusive by immunohistochemistry. Proteins associated with amyloid deposits were identified in all samples, confirming the pathology. Where the routine clinical mass spectrometric identification techniques allowed unambiguous conclusions for 3 of 9 cases, quantification of the enrichment ratio in amyloid deposits allowed unambiguous precursor selection in all cases.<h4>Conclusion</h4>Quantification of precursor enrichment in amyloid deposits is a promising optimization for amyloidosis typing, which should be studied in larger cohorts. Incorporated into routine clinical processes, it could improve patient care in difficult diagnostic situations."],"pubmed_title":["Quantitative enrichment of amyloid precursors refines mass spectrometry-based amyloidosis diagnosis."],"pubmed_authors":["Di Tommaso Sylvaine S, Chauveau Bertrand B, Dourthe Cyril C, Dupuy Jean-William JW, Saltel Frédéric F, Bail Brigitte Le BL, Raymond Anne-Aurélie AA"],"additional_accession":[]},"is_claimable":false,"name":"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 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