PXD030043-1

PXD030043 is an original dataset announced via ProteomeXchange.

Title	Quantitative analysis of redox proteome reveals protein thiol switches regulating fundamental processes in developmental haematopoiesis
Description	Foetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behaviour in normal and malignant haematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approach to comprehensively describe reversible cysteine modifications in primary mouse foetal and adult HSPCs. We defined the redox state of 4455 cysteines in foetal and adult HSPCs and demonstrated a higher susceptibility to oxidation of protein thiols in foetal HSPCs. Our data identified ontogenically active redox switches in proteins with a pronounced role in metabolism and protein homeostasis. Additional redox proteomic analysis identified redox switches acting in mitochondrial respiration as well as protein homeostasis to be triggered during onset of MLL-ENL leukemogenesis in foetal HSPCs. Our data has demonstrated that redox signalling contributes to the regulation of fundamental processes of developmental haematopoiesis and has pinpointed potential targetable redox-sensitive proteins in in utero-initiated MLL-rearranged leukaemia.
HostingRepository	PRIDE
AnnounceDate	2022-06-09
AnnouncementXML	Submission_2022-06-09_05:25:21.579.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Kristyna Pimkova
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	acetylated residue; monohydroxylated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-29 08:22:38	ID requested
⏵ 1	2022-06-09 05:25:22	announced

Pimkova K, Jassinskaja M, Munita R, Ciesla M, Guzzi N, Cao Thi Ngoc P, Vajrychova M, Johansson E, Bellodi C, Hansson J, Quantitative analysis of redox proteome reveals oxidation-sensitive protein thiols acting in fundamental processes of developmental hematopoiesis. Redox Biol, 53():102343(2022) [pubmed]

submitter keyword: hematopoiesis, leukemia, redox proteomics, oxidative modifications

Kristyna Pimkova
contact affiliation	Lund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden
contact email	kristyna.pimkova@lf1.cuni.cz
lab head
Kristyna Pimkova
contact affiliation	BIOCEV, 1st Medical Faculty, Charles University, Vestec, Czech Republic
contact email	kristyna.pimkova@lf1.cuni.cz
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD030043
     1. Label: PRIDE project
     2. Name: Quantitative analysis of redox proteome reveals protein thiol switches regulating fundamental processes in developmental haematopoiesis