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Thiol redox proteomic changes in Jurkat cells resulting from knockout of peroxiredoxin 1 or peroxiredoxin 2

ABSTRACT: Peroxiredoxins are thiol proteins involved in antioxidant defense and redox signaling. One putative signaling mechanism involves the facilitated oxidation of associated proteins via a redox relay. We have investigated if removal of the cytoplasmic peroxiredoxins Prdx1 and Prdx2 influences the redox state of other thiol proteins in cultured cells. A mass spectrometric proteomic approach in which reduced thiols in one cell type were labelled with a heavy isotope tag and reduced thiols in the other cell type with a light isotope tag, was used to compare wild type (WT) Jurkat cells with cells in which either Prdx1 or Prdx2 was knocked out (KO).

ORGANISM(S): Homo Sapiens

SUBMITTER: Jing Yang

PROVIDER: PXD053545 | iProX | Tue Jul 02 00:00:00 BST 2024

REPOSITORIES: iProX

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Ascorbic acid depletion and scorbutic extracellular matrix in mice deficient in endoplasmic reticulum thiol oxidases

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