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Quantitative analysis of redox proteome reveals oxidation-sensitive protein thiols acting in fundamental processes of developmental hematopoiesis

Pimkova, K LU ; Jassinskaja, M LU ; Munita, R LU ; Ciesla, M LU ; Guzzi, N LU ; Cao Thi Ngoc, P LU ; Vajrychova, M LU ; Johansson, E LU orcid ; Bellodi, C LU and Hansson, Jenny LU orcid (2022) In Redox Biology 53.
Abstract

Fetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behavior in normal and malignant hematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approach to comprehensively describe reversible cysteine modifications in primary mouse fetal and adult HSPCs. We defined the redox state of 4,438 cysteines in fetal and adult HSPCs and demonstrated a higher susceptibility to oxidation of protein thiols in fetal HSPCs. Our data identified ontogenic changes to oxidation state of thiols in proteins with a pronounced role in metabolism and protein homeostasis. Additional redox proteomic analysis... (More)

Fetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behavior in normal and malignant hematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approach to comprehensively describe reversible cysteine modifications in primary mouse fetal and adult HSPCs. We defined the redox state of 4,438 cysteines in fetal and adult HSPCs and demonstrated a higher susceptibility to oxidation of protein thiols in fetal HSPCs. Our data identified ontogenic changes to oxidation state of thiols in proteins with a pronounced role in metabolism and protein homeostasis. Additional redox proteomic analysis identified oxidation changes to thiols acting in mitochondrial respiration as well as protein homeostasis to be triggered during onset of MLL-ENL leukemogenesis in fetal HSPCs. Our data has demonstrated that redox signaling contributes to the regulation of fundamental processes of developmental hematopoiesis and has pinpointed potential targetable redox-sensitive proteins in in utero-initiated MLL-rearranged leukemia.

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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Animals, Cysteine/metabolism, Hematopoiesis, Mice, Oxidation-Reduction, Proteome/metabolism, Proteomics, Sulfhydryl Compounds
in
Redox Biology
volume
53
article number
102343
publisher
Elsevier
external identifiers
  • scopus:85131554987
  • pmid:35640380
ISSN
2213-2317
DOI
10.1016/j.redox.2022.102343
language
English
LU publication?
yes
additional info
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
id
5fcdf501-d53e-4f06-9f48-396ac20e7a7f
date added to LUP
2022-07-05 16:11:45
date last changed
2024-04-18 08:47:35
@article{5fcdf501-d53e-4f06-9f48-396ac20e7a7f,
  abstract     = {{<p>Fetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behavior in normal and malignant hematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approach to comprehensively describe reversible cysteine modifications in primary mouse fetal and adult HSPCs. We defined the redox state of 4,438 cysteines in fetal and adult HSPCs and demonstrated a higher susceptibility to oxidation of protein thiols in fetal HSPCs. Our data identified ontogenic changes to oxidation state of thiols in proteins with a pronounced role in metabolism and protein homeostasis. Additional redox proteomic analysis identified oxidation changes to thiols acting in mitochondrial respiration as well as protein homeostasis to be triggered during onset of MLL-ENL leukemogenesis in fetal HSPCs. Our data has demonstrated that redox signaling contributes to the regulation of fundamental processes of developmental hematopoiesis and has pinpointed potential targetable redox-sensitive proteins in in utero-initiated MLL-rearranged leukemia.</p>}},
  author       = {{Pimkova, K and Jassinskaja, M and Munita, R and Ciesla, M and Guzzi, N and Cao Thi Ngoc, P and Vajrychova, M and Johansson, E and Bellodi, C and Hansson, Jenny}},
  issn         = {{2213-2317}},
  keywords     = {{Animals; Cysteine/metabolism; Hematopoiesis; Mice; Oxidation-Reduction; Proteome/metabolism; Proteomics; Sulfhydryl Compounds}},
  language     = {{eng}},
  publisher    = {{Elsevier}},
  series       = {{Redox Biology}},
  title        = {{Quantitative analysis of redox proteome reveals oxidation-sensitive protein thiols acting in fundamental processes of developmental hematopoiesis}},
  url          = {{http://dx.doi.org/10.1016/j.redox.2022.102343}},
  doi          = {{10.1016/j.redox.2022.102343}},
  volume       = {{53}},
  year         = {{2022}},
}