Data from differentially expressed proteins in platelet components associated with adverse transfusion reactions.

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Pellets of ATR platelet components and their controls were subjected to high-throughput proteomics analysis using a Q Exactive high-resolution tandem mass spectrometer. The data reported here constitutes an extension of \"Differential protein expression of blood platelet components associated with adverse transfusion reactions\" article Aloui et al., 2018. The reported data herein have been deposited into the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifiers PXD003510 for the pooled platelet components (PPCs) and PXD008886 for the apheresis platelet components (SDA-PCs) associated with ATRs.", "claims": [{"id": "claim-method", "statement": "The obtained raw proteomic data were statistically analysed (ANOVA test and absolute fold change).", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:31297409", "locator": "sections[2] \"Data\" paragraph 2", "quote": "The obtained raw proteomic data were statistically analysed (ANOVA test and absolute fold change)."}], "state": "complete"}, {"id": "claim-data-access", "statement": "The reported data herein have been deposited into the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifiers PXD003510 for the pooled platelet components (PPCs) and PXD008886 for the apheresis platelet components (SDA-PCs) associated with ATRs.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:31297409", "locator": "sections[0] \"Abstract\" paragraph 1", "quote": "The reported data herein have been deposited into the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifiers PXD003510 for the pooled platelet components (PPCs) and PXD008886 for the apheresis platelet components (SDA-PCs) associated with ATRs."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": null, "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:31297409"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. 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Data were searched with SEQUEST through Proteome Discoverer 1.4 (Thermo Fisher Scientific) against the Homo sapiens reference proteome set (UniProt version 2015–07). Raw LC-MS/MS data were then imported into Progenesis QI 2.0 (Nonlinear Dynamics Ltd., Newcastle, UK) to analyse the label-free quantitative data."], ["Data format", "Raw and processed data"], ["Experimental factors", "Platelet pellets from leukodepleted platelet components (PCs) were sampled from 6 PCs implicated in ATRs and in matched controls. The collected samples were centrifuged at 1500 rpm for 10 min. The PC pellet was washed with sterile 1X PBS. The pellet was then resuspended in 80 μL of PBS and 20 μL of 5X Laemmli buffer (with 0.5 M DTT). After denaturation at 100°C for 3 min, the samples were stored at -80°C until analysis."], ["Experimental features", "For nanoLC-MS/MS analysis, 10 mg of each protein sample were solubilised in Laemmli buffer and deposited into a 10% acrylamide SDS-PAGE gel. Proteins were denatured, reduced, alkylated and digested with trypsin. The supernatant was collected, and an H2O/ACN/HCOOH (47.5:47.5:5) extraction solution was added onto the gel pieces for 15 min. Supernatants were dried in a vacuum centrifuge and resuspended in 100 μL of water acidified with 0.1% HCOOH. The peptide mixture generated was injected into the nano-liquid chromatography-mass spectrometry system."], ["Data source location", "Proteome Platform, CGFB, University of Bordeaux Segalen, 33 076 Bordeaux, France"], ["Data accessibility", "Data within this article were deposited to the ProteomeXchange via the PRIDE repository with the following PRIDE identifiers: PXD003510https://www.ebi.ac.uk/pride/archive/projects/PXD003510(for PPCs) and PXD008886https://www.ebi.ac.uk/pride/archive/projects/PXD008886(for SDA-PCs)."], ["Related research article", "C. Aloui, C. Barlier, S. Claverol, J. Fagan, D. Awounou, E. Tavernier, D. Guyotat, H. Hamzeh-Cognasse, F. Cognasse, O. Garraud, S. Laradi, Differential protein expression of blood platelet components associated with adverse transfusion reactions, J Proteomics 194 (2018) 25–36[1]."]], "row_count": 10, "column_count": 2, "numeric_cells": 6, "header_rows": 0, "locator": "section[1]/table-wrap[1]#undtbl1"}}, {"id": "asset:table:pmid:31297409:2", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:ff86b9936b69e856c878656912c72789951323659709dacfe54f23f7a8093f00", "bytes": 992, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[1]/table-wrap[2]#undtbl2", "version": null, "note": null, "structure": {"pmcid": "PMC6598860", "section_index": 1, "section_title": "p", "row_count": 1, "column_count": 1}, "table": {"label": null, "caption": null, "rows": [["Value of the data•This dataset presents the first exploration of the platelet proteomic signature associated with adverse transfusion reaction (ATRs) in two types of PCs•These data constitute an interesting resource, essential to direct subsequent/future studies, especially in the context of inflammation•These data provide a basis for subsequent comparisons of differential protein expression of blood platelet component associated with ATRs, including the investigation of the biological processes such as i) between platelet pellets and supernatants ii) between different preparation processes•This proteomics analysis paves the way to a better understanding of the pathophysiological mechanisms involved in ATRs•The provided dataset can be useful for transfusion medicine in order to improve transfusion safety and efficacy."]], "row_count": 1, "column_count": 1, "numeric_cells": 0, "header_rows": 0, "locator": "section[1]/table-wrap[2]#undtbl2"}}, {"id": "asset:table:pmid:31297409:3", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": 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