PXD039914

PXD039914 is an original dataset announced via ProteomeXchange.

Title	Phosphoproteomics and Morphology of Red Blood Cells treated by Protein-Tyrosine-Phosphatases Inhibitor
Description	Phosphorylation of proteins is involved in cell functions, of which cytoskeleton organization. In particular, the phosphotyrosine (pY) has been reported to play a role in red blood cell (RBC) functions. During the storage of RBC in the context of transfusion medicine, cells suffer from storage lesions that affect energy metabolism as well as cell morphology. In the present research work, RBCs were treated (in absence of calcium) with a protein tyrosine phosphatase inhibitor (orthovanadate, OV) to trigger phosphorylation allowing to investigate this effect on RBCs during the storage. Erythrocytes were studied by phosphoproteomics, Western blot analyses and cell morphology by digital holographic microscopy in presence of kinase inhibitors. The OV treatment triggered phosphorylation events, that disappeared during the storage. As a result, 609 phosphoproteins containing 5’298 phosphosites were detected in the membrane extract, of which 43 pY were up- or down-regulated. Following these phosphorylation processes, shape of RBCs shifted from discocytes to spherocytes, and the addition of kinase inhibitors (KIs) inhibited this transition by counteracting the OV treatment. In addition, the different KIs used highlighted potentially two mechanisms involving membrane proteins and playing a role in RBC shape. The capacity of RBCs to maintain their function is central in transfusion medicine and the presented results contribute to a better understanding of RBC biology.
HostingRepository	PRIDE
AnnounceDate	2024-01-26
AnnouncementXML	Submission_2024-01-26_10:10:24.451.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Romain Hamelin
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; monohydroxylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-07 06:51:12	ID requested
⏵ 1	2024-01-26 10:10:25	announced

Bardyn M, Crettaz D, Rappaz B, Hamelin R, Armand F, Tissot JD, Turcatti G, Prudent M, Phosphoproteomics and morphology of stored human red blood cells treated by protein tyrosine phosphatases inhibitor. Blood Adv, 8(1):1-13(2024) [pubmed]

10.1182/bloodadvances.2023009964;

submitter keyword: Protein tyrosine phosphorylation, storage of red blood cells, kinase inhibitors, digital holographic microscopy, transfusion medicine.

Michel Prudent
contact affiliation	Laboratoire de Recherche sur les Produits Sanguins, Transfusion Interrégionale CRS, Epalinges, Switzerland Center for Research and Innovation in Clinical Pharmaceutical Sciences, Institute of Pharmaceutical Sciences of Western Switzerland, University Hospital and University of Lausanne, Lausanne, Switzerland Institute of Pharmaceutical Sciences of Western Switzerland, University of Geneva, University of Lausanne, Switzerland
contact email	Michel.Prudent@itransfusion.ch
lab head
Romain Hamelin
contact affiliation	PCF
contact email	romain.hamelin@epfl.ch
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/2024/01/PXD039914

PRIDE project URI

• PRIDE
  1. PXD039914
     1. Label: PRIDE project
     2. Name: Phosphoproteomics and Morphology of Red Blood Cells treated by Protein-Tyrosine-Phosphatases Inhibitor