Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/112594
Title: The mammalian peroxisomal membrane is permeable to both GSH and GSSG - Implications for intraperoxisomal redox homeostasis
Authors: Ferreira, Maria J.
Rodrigues, Tony A.
Pedrosa, Ana G.
Gales, Luís
Salvador, Armindo 
Francisco, Tânia
Azevedo, Jorge E.
Keywords: Peroxisome; Glutathione; Membrane permeability; Glutaredoxin; Protein import; Kinetic simulation
Issue Date: Jul-2023
Publisher: Elsevier
Project: UIDB/04293/2020 
POCI-01-0145-FEDER-007274 
UIDB/04539/2020 
LA/P/0058/2020 
UIDB/00313/2020 
info:eu-repo/grantAgreement/UIDP/04539/2020 
UIDP/00313/2020 
NORTE-01-0145-FEDER-000008 
Serial title, monograph or event: Redox Biology
Volume: 63
Abstract: Despite the large amounts of H2O2 generated in mammalian peroxisomes, cysteine residues of intraperoxisomal proteins are maintained in a reduced state. The biochemistry behind this phenomenon remains unexplored, and simple questions such as "is the peroxisomal membrane permeable to glutathione?" or "is there a thiol-disulfide oxidoreductase in the organelle matrix?" still have no answer. We used a cell-free in vitro system to equip rat liver peroxisomes with a glutathione redox sensor. The organelles were then incubated with glutathione solutions of different redox potentials and the oxidation/reduction kinetics of the redox sensor was monitored. The data suggest that the mammalian peroxisomal membrane is promptly permeable to both reduced and oxidized glutathione. No evidence for the presence of a robust thiol-disulfide oxidoreductase in the peroxisomal matrix could be found. Also, prolonged incubation of organelle suspensions with glutaredoxin 1 did not result in the internalization of the enzyme. To explore a potential role of glutathione in intraperoxisomal redox homeostasis we performed kinetic simulations. The results suggest that even in the absence of a glutaredoxin, glutathione is more important in protecting cysteine residues of matrix proteins from oxidation by H2O2 than peroxisomal catalase itself.
URI: https://hdl.handle.net/10316/112594
ISSN: 22132317
DOI: 10.1016/j.redox.2023.102764
Rights: openAccess
Appears in Collections:I&D CQC - Artigos em Revistas Internacionais
I&D CNC - Artigos em Revistas Internacionais

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